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(2,2,6,6-tetramethyl-piperidine-N-oxyl) radical + O2
?
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoic acid + O2
?
-
-
-
-
?
(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoic acid + O2
?
-
-
-
-
?
(2Z,2'Z)-2,2'-(1Z,2Z)-hydrazine-1,2-diylidenebis(3-ethyl-2,3-dihydro-1,3-benzothiazole-6-sulfonic acid) + O2
?
-
-
-
-
?
(4a'S)-2',3',6',7'-tetrahydroxy-1,1'',3,3''-tetramethyl-4a',9a'-dihydro-2H,2''H-dispiro[pyrimidine-5,9'-anthracene-10',5''-pyrimidine]-2,2'',4,4'',6,6''(1H,1''H,3H,3''H)-hexone + O2
2',3',6',7'-tetrahydroxy-1,1'',3,3''-tetramethyldispiro[pyrimidine-5(2H),9'(10'H)-anthracene-10',5''(2''H)-pyrimidine]-2,2'',4,4'',6,6''-(1H,1''H,3H,3''H)-hexone + H2O2
-
-
a polycyclic dispiropyrimidinone
-
?
1,2,4-benzenetriol + O2
?
-
-
-
-
?
1,3,5-trihydroxybenzene + O2
?
1,4-dioxane + O2
?
the oxidation reaction is accelerated by 25, 22, 6 and 19% in presence of 1 mM syringaldehyde, vanillin, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) and guaiacol mediators respectively
-
-
?
1,8-diaminonaphthalene + O2
?
-
-
-
-
?
1-(2,4,5-trihydroxyphenyl)butan-1-one + O2
?
-
-
-
-
?
1-(4-hydroxy-3,5-dimethoxyphenyl)ethanone + O2
?
-
-
-
-
?
1-hydroxybenzotriazole + O2
?
1-naphthol + O2
?
-
-
-
?
2 2,6-dimethoxyphenol + O2
?
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
2 catechol + O2
2 6-hydroxycyclohexa-2,4-dienone + 2 H2O
2 catechol + O2
2 o-quinone + 2 H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzathiazoline-6-sulfonate) + O2
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
? + H2O
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic) acid + O2
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate) + O2
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonate) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate) + O2
?
2,2'-azinobis(3-ethylbenz-thiazoline-6-sulfonic acid) + O2
?
Thermochaetoides thermophila
-
-
-
-
?
2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic acid) + O2
?
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) + O2
?
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
2,2,6,6-tetramethyl-piperidine-1-oxyl radical + O2
?
2,2,6,6-tetramethylpiperidin-N-oxide radical + O2
?
2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
2,2-azino-bis-(3-ethylbenzthiazolin-6-sulfonate) + O2
?
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
2,3-dihydroxybenzoate + H2O
?
-
-
-
?
2,3-dihydroxybenzoic acid + O2
?
-
-
-
?
2,4,6-trichlorophenol + O2
?
-
-
-
-
?
2,4-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
2,4-dichlorophenol + O2
?
-
-
-
-
?
2,4-dichlorophenol + O2
? + H2O
-
-
-
-
?
2,4-dimethylphenol + O2
?
-
-
-
-
?
2,5-diaminotoluene + O2
?
-
-
-
?
2,6-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
2,6-dichlorophenol + O2
? + H2O
2,6-dimethoxy phenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + 4-aminoantipyrine + O2
? + H2O
2,6-dimethoxyphenol + H2O
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
2,6-dimethoxyphenol + O2
?
2,6-dimethoxyphenol + O2
? + H2O
2,6-dimethylphenol + O2
?
2,6-dimethylphenol + O2
? + H2O
-
-
-
-
?
2,6-dimethylphthalate + O2
?
2-benzoquinone + O2
?
-
-
-
-
?
2-chlorophenol + O2
?
-
-
-
-
?
2-ethoxyphenol + O2
?
-
-
-
-
?
2-methylcatechol + O2
?
-
17.2% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
2-naphthol + O2
? + H2O
-
-
-
-
?
3,4,5-trihydroxybenzoic acid + O2
?
3,4-dihydroxy L-phenylalanine + O2
?
-
-
-
?
3,4-dihydroxybenzoic acid + O2
?
3,4-dihydroxyphenylacetate + O2
? + H2O
-
-
-
-
?
3,4-dimethoxybenzyl alcohol + O2
?
-
-
-
-
?
3,5-dimethoxy-hydroxy-benzaldazine + O2
? + H2O
-
-
-
-
?
3-(4-dimethylamino-1-phenylazo) benzene sulfonic acid sodium salt + O2
?
-
i.e. methyl orange, decolorization of the azo dye
-
-
?
3-amino-4-hydroxybenzoic acid + O2
?
-
-
-
-
?
3-aminobenzoic acid + O2
?
-
low activity
-
-
?
3-dimethylaminobenzoic acid + 3-methyl-2-benzothiazolinone hydrazone + O2
? + H2O
-
ratio of substrates 1:0.07
-
-
?
3-hydroxy-L-tyrosine + O2
?
-
-
-
-
?
3-hydroxyanthranilic acid + O2
?
-
-
-
?
3-methylcatechol + O2
?
-
-
-
-
?
4 1,2,3-trihydroxybenzene + O2
?
4 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
4 2,6-dimethoxyphenol + O2
?
4 2,6-dimethylphenol + O2
?
-
-
-
?
4 2-methoxyphenol + O2
?
-
-
-
-
?
4 3,3',5,5'-tetramethylbenzidine + O2
?
-
-
-
?
4 3-aminobenzoic acid + O2
?
-
-
-
-
?
4 4-hydroxy-3,5-dimethoxy-benzaldehyde azine + O2
?
-
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
4 N,N-dimethyl-1,4-phenylenediamine + O2
?
-
-
-
-
?
4 pyrogallol + O2
?
-
-
-
-
?
4 syringic acid + O2
4 4-carboxy-2,6-dimethoxyphenoxyl + 2 H2O
4 toluidine + O2
?
-
-
-
-
?
4,5-dimethyl-o-phenylenediamine + O2
? + H2O
-
-
-
-
?
4-(2-aminoethyl)benzene-1,2-diol + O2
?
-
-
-
-
?
4-(hydroxymethyl)-2-methoxyphenol + O2
?
-
-
-
-
?
4-amino-3-hydroxybenzoic acid + O2
?
-
-
-
-
?
4-amino-N,N'-dimethylaniline + O2
? + H2O
-
-
-
-
?
4-aminoantipyrine + O2
? + H2O
-
19% of the activity with N,N-dimethyl-p-phenylenediamine sulfate
-
-
?
4-aminoantipyrine + phenol + O2
? + H2O
4-aminophenol + O2
?
-
-
-
-
?
4-chloro-2-methylphenol + O2
? + H2O
-
-
-
-
?
4-chlorocatechol + O2
?
-
-
-
-
?
4-fluoro-2-methylphenol + O2
?
-
-
-
?
4-hydroquinone + O2
?
-
-
-
-
?
4-hydroxy-1,6-dimethylpyridin-2(1H)-one + 3-methoxy-1,2-benzenediol
7,8-dihydroxy-6-methoxy-2,3-dimethylbenzofuro[3,2-c]pyridin-1(2H)-one
-
-
-
-
?
4-hydroxy-1,6-dimethylpyridin-2(1H)-one + 3-methyl-1,2-benzenediol
7,8-dihydroxy-2,3,6-trimethyl[1]benzofuro[3,2-c]pyridin-1(2H)-one
-
-
-
-
?
4-hydroxy-1,6-dimethylpyridin-2(1H)-one + benzenediol
7,8-dihydroxy-2,3-dimethyl[1]benzofuro[3,2-c]pyridin-1(2H)-one
-
-
-
-
?
4-hydroxy-1-thiocoumarin + 3-methoxy-1,2-benzenediol
8,9-dihydroxy-10-methoxy-6H-thiochromeno[4,3-b][1]benzofuran-6-one
-
-
-
-
?
4-hydroxy-1-thiocoumarin + 3-methyl-1,2-benzenediol
8,9-dihydroxy-10-methyl-6H-thiochromeno[4,3-b][1]benzofuran-6-one
-
-
-
-
?
4-hydroxy-1-thiocoumarin + benzenediol
8,9-dihydroxy-6H-thiochromeno[4,3-b][1]benzofuran-6-one
-
-
-
-
?
4-hydroxy-3,5-dimethoxybenzaldehyde + O2
?
-
-
-
-
?
4-hydroxy-3,5-dimethoxybenzaldehyde azine + O2
?
4-hydroxy-3,5-dimethoxybenzoic acid + O2
?
-
-
-
-
?
4-hydroxy-6-methylpyridin-2(1H)-one + 3-methoxy-1,2-benzenediol
7,8-dihydroxy-6-methoxy-3-methyl[1]benzofuro[3,2-c]pyridin-1(2H)-one
-
-
-
-
?
4-hydroxy-6-methylpyridin-2(1H)-one + 3-methyl-1,2-benzenediol
7,8-dihydroxy-3,6-dimethyl[1]benzofuro[3,2-c]pyridin-1(2H)-one
-
-
-
-
?
4-hydroxy-6-methylpyridin-2(1H)-one + benzenediol
7,8-dihydroxy-3-methyl[1]benzofuro[3,2-c]pyridin-1(2H)-one
-
-
-
-
?
4-hydroxybenzoic acid + O2
?
4-hydroxyindole + O2
? + H2O
-
-
-
-
?
4-hydroxyphenylacetic acid + O2
?
-
second-order rate constant for the reaction with dioxygen
-
-
?
4-hydroxyquinolin-2(1H)-one + 3-methoxy-1,2-benzenediol
8,9-dihydroxy-10-methoxy[1]benzofuro[3,2-c]quinolin-6(5H)-one
-
-
-
-
?
4-hydroxyquinolin-2(1H)-one + 3-methyl-1,2-benzenediol
8,9-dihydroxy-10-methyl[1]benzofuro[3,2-c]quinolin-6(5H)-one
-
-
-
-
?
4-hydroxyquinolin-2(1H)-one + benzenediol
8,9-dihydroxy[1]benzofuro[3,2-c]quinolin-6(5H)-one
-
-
-
-
?
4-methylbenzene-1,2-diol + O2
?
-
-
-
-
?
4-methylcatechol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
4-methylcatechol + O2
? + H2O
4-morpholinoaniline + 2,5-dihydroxybenzoic acid ethyl ester + O2
2,5-bis-(4-morpholin-4-yl-phenylamino)-3,6-dioxocyclohexa-1,4-dienecarboxylic acid ethyl ester
-
-
-
-
?
4-morpholinoaniline + 2,5-dihydroxybenzoic acid methyl ester + O2
2,5-bis-(4-morpholin-4-yl-phenylamino)-3,6-dioxocyclohexa-1,4-dienecarboxylic acid methyl ester
-
-
-
-
?
4-phenylcatechol + O2
?
-
-
-
-
?
4-phenylenediamine + O2
?
4-tert-butylcatechol + O2
?
-
-
-
-
?
5-(hydroxymethyl)-2-methoxyphenol + O2
?
-
-
-
-
?
acetaminophen + O2
?
-
-
-
-
?
Adizol black B + O2
?
decolorization with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), acetosyringone or syringaldehyde as mediator
-
-
?
alizarin red S + O2
?
-
-
-
-
?
alpha-naphthol + O2
? + H2O
-
11.7% of activity with syringaldazine
-
-
?
anthraquinonic dye Acid Blue 62 + O2
?
-
-
-
?
Azophloxine + O2
?
decolorization with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), acetosyringone or syringaldehyde as mediator
-
-
?
benzene-1,2,3-triol + O2
?
-
-
-
-
?
benzene-1,2-diol + O2
?
-
-
-
-
?
benzenediol + thiobarbituric acid
1,1'',3,3''-tetraethyl-2',3',6',7'-tetrahydroxy-2,2''-dithioxo-2H,2''H-dispiro[pyrimidine-5,9'-anthracene-10',5''-pyrimidine]-4,4'',6,6''(1H,1''H,3H,3''H)-tetrone
-
-
-
-
?
benzidine + O2
?
-
22.53% of the activity with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
beta-(3,4-dihydroxyphenyl)alanine + O2
beta-(3,4-dihydroxyphenyl)alanine quinone + H2O
-
i.e. L-dopa
-
-
?
brenzcatechin + O2
? + H2O
-
-
-
-
?
Bromocresol Purple + O2
?
caffeate + O2
? + H2O
-
-
-
-
?
caffeic acid + 4-aminoantipyrine + O2
? + H2O
catechol + 1/2 O2
1,2-benzoquinone + H2O
catechol + 4-aminoantipyrine + O2
? + H2O
catechol + O2
1,2-benzoquinone + H2O
-
-
-
?
chlorogenic acid + O2
? + H2O
-
26.5% of the activity with N,N-dimethyl-p-phenylenediamine sulfate
-
-
?
coniferaldehyde + O2
?
-
-
-
-
?
coniferic acid + O2
? + H2O
coniferyl alcohol + O2
? + H2O
-
-
-
-
?
Coomassie brilliant blue + O2
?
Crystal violet + O2
?
decolorization with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), acetosyringone or syringaldehyde as mediator
-
-
?
Diamond Black PV 200 + ?
2-amino-1-phenol-4-sulfonic acid + 1,5-naphthalenediol + ?
-
i.e. Mordant Black 9, Eriochrome Black PV, wool azo dye
-
-
?
diethylaniline + 4-aminoantipyrine + O2
? + H2O
dihydroxyphenylalanine + O2
? + H2O
-
23.6% of the activity with N,N-dimethyl-p-phenylenediamine sulfate
-
-
?
dimethylaniline + 4-aminoantipyrine + O2
? + H2O
DL-adrenaline + O2
?
-
-
-
-
?
enterobactin + O2
?
-
-
-
?
Eriochrome black T + O2
?
-
-
-
-
?
Evans Blue + O2
?
-
activity with mutant enzyme V159E/N398D
-
-
?
ferrocenemonocarboxylic acid + O2
?
ferulate + O2
? + H2O
-
-
-
-
?
ferulic acid + O2
3-(4-hydroxy-3-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
ferulic acid + O2
? + H2O
gallate + O2
? + H2O
-
-
-
-
?
Gly-Leu-Tyr + O2
?
-
21% of the activity with caffeic acid
-
-
?
guaiacol + 4-aminoantipyrine + O2
? + H2O
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
guaiacolsulfonic acid + O2
?
-
-
-
-
?
hydrocaffeic acid + 4-aminoantipyrine + O2
? + H2O
hydrocaffeic acid + O2
?
-
-
-
-
?
hydroquinone + 4-aminoantipyrine + O2
? + H2O
hydroquinone + O2
? + H2O
hydroxyquinone + O2
?
Thermochaetoides thermophila
-
-
-
-
?
Indigo + ?
?
-
textile dye
-
-
?
K4(FeCN6) + O2
?
-
-
-
-
?
K4Fe(CN)6 + O2
?
-
-
-
-
?
K4[Fe(CN)]6 + O2
?
-
-
-
-
?
L-3,4-dihydroxyphenylalanine + O2
?
Thermochaetoides thermophila
-
i.e. L-dopa
-
-
?
L-Tyr + O2
?
-
11% of the activity with caffeic acid
-
-
?
Lancet Marine Blue + ?
?
-
textile dye
-
-
?
lignin sulfonic acid + O2
? + H2O
-
0.9% of activity with syringaldazine
-
-
?
m-chlorophenol + 4-aminoantipyrine + O2
? + H2O
m-chlorophenol + O2
? + H2O
-
-
-
-
?
m-cresol + O2
6-hydroxy-3-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
m-cresol + O2
?
Loweporus lividus
-
-
-
-
?
m-cresol + O2
? + H2O
Loweporus lividus MTCC-1178
-
-
-
-
?
m-methoxyphenol + O2
? + H2O
-
15% of the activity with N,N-dimethyl-p-phenylenediamine sulfate
-
-
?
Malachite green
indigo carmine
methyl hydroquinone + O2
?
-
-
-
-
?
Methyl orange + O2
?
-
47.55% decolourisation efficiency
-
-
?
methyl red + O2
?
-
-
-
-
?
methyl syringate + O2
? + H2O
-
-
-
-
?
morpholine + 1,4-dihydroxynaphthalene + O2
2-morpholin-4-yl-[1,4]naphthoquinone
-
-
-
-
?
morpholine + 1,4-hydroquinone + O2
2,5-dimorpholin-4-yl-[1,4]benzoquinone
-
-
-
-
?
morpholine + 2,3-dimethyl-1,4-hydroquinone + O2
2,3-dimethyl-5-morpholin-4-yl-[1,4]benzoquinone
-
-
-
-
?
morpholine + 2,5-dihydroxy-N-(2-hydroxyethyl)-benzamide + O2
2-hydroxy-5-morpholin-4-yl-3,6-dioxocyclohexa-1,4-dienecarboxylic acid (2-hydroxyethyl)-amide
-
-
-
-
?
morpholine + 2-methyl-1,4-hydroquinone + O2
2-methyl-6-morpholin-4-yl-[1,4]benzoquinone + 2-methyl-5-morpholin-4-yl-[1,4]benzoquinone
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + O2
?
N,N-dimethyl-1,4-phenylenediamine + O2
? + H2O
-
-
-
-
?
N,N-dimethyl-4-phenylenediamine + O2
?
-
-
-
-
?
N,N-dimethyl-p-phenylenediamine + 4-aminoantipyrine + O2
? + H2O
N,N-dimethyl-p-phenylenediamine + O2
?
N,N-dimethyl-p-phenylenediamine sulfate + O2
? + H2O
-
-
-
-
?
N,N-dimethylbarbituric acid + catechol
2',3',6',7'-tetrahydroxy-1,1'',3,3''-tetramethyldispiro[pyrimidine-5(2H),9'(10'H)-anthracene-10',5''(2''H)-pyrimidine]-2,2'',4,4'',6,6''-(1H,1''H,3H,3''H)-hexone
-
-
a polycyclic dispiropyrimidinone
-
?
N-acetyldopamine + O2
?
-
-
-
?
N-beta-alanyldopamine + O2
?
-
-
-
?
N-ethyl-N-(2-hydroxy-3-sulfopropyl)-3-methylaniline + 4-aminoantipyrine + O2
? + H2O
N-hydroxyacetanilide + O2
? + H2O
-
-
-
-
?
o-chlorophenol + 4-aminoantipyrine + O2
? + H2O
o-chlorophenol + O2
? + H2O
o-cresol + 4-aminoantipyrine + O2
? + H2O
o-cresol + O2
6-hydroxy-2-methylcyclohexa-2,4-dienone + H2O
o-phenylenediamine + O2
? + H2O
-
-
-
-
?
o-quinone + N,N-dimethylbarbituric acid
?
-
-
-
-
?
p-aminophenol + O2
?
-
-
-
-
?
p-chlorophenol + O2
? + H2O
p-coumaric acid + O2
?
-
79% of the activity with caffeic acid
-
-
?
p-coumaric acid + O2
? + H2O
p-coumaryl alcohol + O2
?
-
-
-
-
?
p-cresol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
p-cresol + O2
?
-
-
-
-
?
p-cresol + O2
? + H2O
-
6.35% of activity with syringaldazine
-
-
?
p-hydroxybenzoic acid + 4-aminoantipyrine + O2
? + H2O
p-methoxyphenol + O2
? + H2O
p-phenylenediamine + 4-aminoantipyrine + O2
? + H2O
-
563% of the activity with phenol
-
-
?
p-phenylenediamine + O2
?
p-phenylenediamine + O2
? + H2O
p-toluidine + 4-aminoantipyrine + O2
? + H2O
phloroglucinol + O2
?
-
-
-
-
?
propyl gallate + 4-aminoantipyrine + O2
? + H2O
-
94% of the activity with phenol
-
-
?
protocatechuate + O2
? + H2O
-
-
-
-
?
pyrogallol + 4-aminoantipyrine + O2
? + H2O
reactive 203 brilliant orange K-7R + O2
?
Reactive Black WNN + O2
?
Reactive blue 19 + O2
?
decolorization with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), acetosyringone or syringaldehyde as mediator
-
-
?
Reactive blue 5 + O2
?
decolorization with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), acetosyringone or syringaldehyde as mediator
-
-
?
reactive blue M-2GE + O2
?
addition of mediators including methyl syringate, 3,5-dimethoxy-4-hydroxybenzaldehyde, syringic acid, 1-hydroxybenzotriazole, and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) strongly promote the decolorization rates of the recombinant enzyme rLcc9 on the dyes. Methyl syringate is the best mediator. The decolorization rate of reactive blue M-2GE is 71.9%
-
-
?
reactive brilliant red KD-8B + O2
?
addition of mediators including methyl syringate, 3,5-dimethoxy-4-hydroxybenzaldehyde, syringic acid, 1-hydroxybenzotriazole, and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) strongly promote the decolorization rates of the recombinant enzyme rLcc9 on the dyes. Methyl syringate is the best mediator. The decolorization rate of reactive brilliant red KD-8B is 89.2%
-
-
?
reactive brilliant red KM-8B + O2
?
addition of mediators including methyl syringate, 3,5-dimethoxy-4-hydroxybenzaldehyde, syringic acid, 1-hydroxybenzotriazole, and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) strongly promote the decolorization rates of the recombinant enzyme rLcc9 on the dyes. Methyl syringate is the best mediator. The decolorization rate of reactive brilliant red KM-8B is 82.5%
-
-
?
Remazol Brilliand Red + ?
?
-
textile dye
-
-
?
Remazol Brilliant Blue + O2
?
-
greater efficiency in Remazol Brilliant Blue decolourization (90%) in absence of redox mediator
-
-
?
Remazol Brilliant Blue R + O2
?
Remazol brilliant orange 3R + O2
?
resorcinol + 4-aminoantipyrine + O2
? + H2O
sinapic acid + O2
3-(3,5-dimethoxy-4-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
sinapic acid + O2
? + H2O
syringaldazine + H2O
?
-
-
-
-
?
syringaldehyde + O2
?
-
-
-
?
syringaldehyde + O2
? + H2O
-
-
-
-
?
syringate + O2
? + H2O
-
-
-
-
?
syringic acid + O2
2,6-dimethoxy-1,4-benzoquinone + CO2 + H2O
-
-
-
-
?
syringic acid + O2
? + H2O
-
-
-
-
?
thioglycolic lignin + O2
?
Turquoise blue HF6 + O2
?
vanillate + O2
? + H2O
-
-
-
-
?
vanillic acid + O2
4-carboxy-2-methoxycyclohexa-2,4-dienone + H2O
vanillic alcohol + O2
?
-
-
-
-
?
vanillin + O2
? + H2O
-
-
-
-
?
veratryl alcohol + 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
veratryl alcohol + O2
?
-
-
-
-
?
violuric acid + O2
?
-
-
-
-
?
violuric acid + O2
? + H2O
-
-
-
-
?
additional information
?
-
(2,2,6,6-tetramethyl-piperidine-N-oxyl) radical + O2
?
-
-
-
-
?
(2,2,6,6-tetramethyl-piperidine-N-oxyl) radical + O2
?
-
-
-
?
(2,2,6,6-tetramethyl-piperidine-N-oxyl) radical + O2
?
-
-
-
?
(2,2,6,6-tetramethyl-piperidine-N-oxyl) radical + O2
?
-
-
-
?
(2,2,6,6-tetramethyl-piperidine-N-oxyl) radical + O2
?
-
-
-
-
?
1,3,5-trihydroxybenzene + O2
?
-
-
-
-
?
1,3,5-trihydroxybenzene + O2
?
Trametes hirsuta Ig-9 / CGMCC 2422
-
-
-
-
?
1-hydroxybenzotriazole + O2
?
-
-
-
?
1-hydroxybenzotriazole + O2
?
-
-
-
-
?
1-hydroxybenzotriazole + O2
?
-
-
-
-
?
1-naphthol + O2
? + H2O
-
-
-
-
?
1-naphthol + O2
? + H2O
-
-
-
-
?
1-naphthol + O2
? + H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 6-hydroxycyclohexa-2,4-dienone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 6-hydroxycyclohexa-2,4-dienone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 6-hydroxycyclohexa-2,4-dienone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 6-hydroxycyclohexa-2,4-dienone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 6-hydroxycyclohexa-2,4-dienone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 6-hydroxycyclohexa-2,4-dienone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 6-hydroxycyclohexa-2,4-dienone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 6-hydroxycyclohexa-2,4-dienone + 2 H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzathiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzathiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
Inocybe longicystis
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
Leptonia lazunila
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
Lyophyllum subglobisporium
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
Lyophyllum subglobisporium ECN 100606
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic) acid + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic) acid + O2
?
-
spectrophotometric assay
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate) + O2
?
Myrioconium sp.
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate) + O2
?
Myrioconium sp. UHH 1-13-18-4
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
100% activity
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
FJ560721
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
Oscillatoria subuliformis
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
Oscillatoria subuliformis BDU100712
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
best substrate
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
best substrate
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
high activity
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
73% of the activity compared to syringaldazine
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
catalytic efficiency on 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) is 7.5 times of that on 2,6-dimethoxyphenol, 22 times of that on catechol and 65times higher than that on guaiacol
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
catalytic efficiency on 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) is 7.5 times of that on 2,6-dimethoxyphenol, 22 times of that on catechol and 65times higher than that on guaiacol
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
Sporothrix carnis
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
Sporothrix carnis CPF-05
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate) + O2
?
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
Fomes sclerodermeus
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
Fomes sclerodermeus BAFC 2752
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
53% of the activity with phenol
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
53% of the activity with phenol
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
82% of activity with syringaldazine
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
Phlebia fascicularia
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
35% of the activity with phenol
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
35% of the activity with phenol
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
44% of the activity with phenol
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) + O2
?
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) + O2
?
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) + O2
?
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) + O2
?
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) + O2
?
i.e. ABTS
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) + O2
?
i.e. ABTS
-
-
?
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2,6,6-tetramethyl-piperidine-1-oxyl radical + O2
?
-
i.e. TEMPO, model of synergistic TEMPO and activator PSPX oxidation
-
-
?
2,2,6,6-tetramethyl-piperidine-1-oxyl radical + O2
?
-
i.e. TEMPO, model of synergistic TEMPO and activator PSPX oxidation
-
-
?
2,2,6,6-tetramethyl-piperidine-1-oxyl radical + O2
?
-
i.e. TEMPO, model of synergistic TEMPO and activator PSPX oxidation
-
-
?
2,2,6,6-tetramethyl-piperidine-1-oxyl radical + O2
?
-
i.e. TEMPO, model of synergistic TEMPO and activator PSPX oxidation
-
-
?
2,2,6,6-tetramethylpiperidin-N-oxide radical + O2
?
-
-
-
-
?
2,2,6,6-tetramethylpiperidin-N-oxide radical + O2
?
-
-
-
-
?
2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2-azino-bis-(3-ethylbenzthiazolin-6-sulfonate) + O2
?
-
56% of the activity with 2,6-dimethoxyphenol
-
-
?
2,2-azino-bis-(3-ethylbenzthiazolin-6-sulfonate) + O2
?
-
-
-
-
?
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,4-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
-
80% of the activity with phenol
-
-
?
2,4-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
-
80% of the activity with phenol
-
-
?
2,4-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
-
89% of the activity with phenol
-
-
?
2,4-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
-
89% of the activity with phenol
-
-
?
2,4-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
-
93% of the activity with phenol
-
-
?
2,5-xylidine + O2
?
-
-
-
-
?
2,5-xylidine + O2
?
-
-
-
-
?
2,5-xylidine + O2
?
the enzyme also transforms the non-phenolic substrate at pH 5.0, native and recombinant enzymes, wild-type and mutant enzymes, overview
-
-
?
2,6-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
-
49% of the activity with phenol
-
-
?
2,6-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
-
49% of the activity with phenol
-
-
?
2,6-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
-
176% of the activity with phenol
-
-
?
2,6-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
-
176% of the activity with phenol
-
-
?
2,6-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
-
258% of the activity with phenol
-
-
?
2,6-dichlorophenol + O2
? + H2O
-
-
-
-
?
2,6-dichlorophenol + O2
? + H2O
-
-
-
?
2,6-dichlorophenol + O2
? + H2O
-
-
-
?
2,6-dimethoxyphenol + 4-aminoantipyrine + O2
? + H2O
-
3840% of the activity with phenol
-
-
?
2,6-dimethoxyphenol + 4-aminoantipyrine + O2
? + H2O
-
3840% of the activity with phenol
-
-
?
2,6-dimethoxyphenol + 4-aminoantipyrine + O2
? + H2O
-
104% of the activity with phenol
-
-
?
2,6-dimethoxyphenol + 4-aminoantipyrine + O2
? + H2O
-
104% of the activity with phenol
-
-
?
2,6-dimethoxyphenol + 4-aminoantipyrine + O2
? + H2O
-
159% of the activity with phenol
-
-
?
2,6-dimethoxyphenol + H2O
?
-
-
-
?
2,6-dimethoxyphenol + H2O
?
-
-
-
?
2,6-dimethoxyphenol + H2O
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O
?
-
-
-
?
2,6-dimethoxyphenol + H2O
?
-
about 5% of the activity with 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
Fomes sclerodermeus
-
preferred substrate
i.e. coerulignone
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
Fomes sclerodermeus BAFC 2752
-
preferred substrate
i.e. coerulignone
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
i.e. cerulignone
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
Loweporus lividus
-
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
preferred substrate
i.e. coerulignone
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
preferred substrate
i.e. coerulignone
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
69% of the activity compared to syringaldazine
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
75.8% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
7.1% compared to the activity with 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
best substrate
-
-
?
2,6-dimethoxyphenol + O2
?
-
best substrate
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
FJ560721
-
-
-
?
2,6-dimethoxyphenol + O2
?
FJ560721
-
-
-
?
2,6-dimethoxyphenol + O2
?
Myrioconium sp.
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
Myrioconium sp. UHH 1-13-18-4
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
24% of the activity with 2,2-azino-bis-(3-ethylbenzthiazolin-6-sulfonate)
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
Thermochaetoides thermophila
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
Trametes hirsuta Ig-9 / CGMCC 2422
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
96% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
60% of activity with syringaldazine
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
Loweporus lividus MTCC-1178
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
Phlebia fascicularia
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
36% of activity with 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
36% of activity with 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
2,6-dimethylphenol + O2
?
-
-
-
?
2,6-dimethylphenol + O2
?
-
-
-
?
2,6-dimethylphenol + O2
?
-
6% of the activity with 2,6-dimethoxyphenol
-
-
?
2,6-dimethylphenol + O2
?
-
-
-
-
?
2,6-dimethylphenol + O2
?
-
-
-
-
?
2,6-dimethylphenol + O2
?
-
1% of the activity with 2,2-azino-bis-(3-ethylbenzthiazolin-6-sulfonate)
-
-
?
2,6-dimethylphenol + O2
?
-
-
-
-
?
2,6-dimethylphthalate + O2
?
-
-
-
?
2,6-dimethylphthalate + O2
?
-
-
-
?
2-dianisidine + O2
?
-
-
-
-
?
2-dianisidine + O2
?
-
-
-
?
2-dianisidine + O2
?
-
-
-
?
2-methoxyphenol + O2
?
-
-
-
-
?
2-methoxyphenol + O2
?
-
8.6% activity compared to 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
2-methylphenol + O2
?
i.e. guaiacol
-
-
?
2-methylphenol + O2
?
-
i.e. guaiacol
-
-
?
2-methylphenol + O2
?
-
i.e. guaiacol
-
-
?
3,4,5-trihydroxybenzoic acid + O2
?
-
-
-
-
?
3,4,5-trihydroxybenzoic acid + O2
?
-
-
-
-
?
3,4-dihydroxybenzoic acid + O2
?
-
-
-
-
?
3,4-dihydroxybenzoic acid + O2
?
-
-
-
-
?
3,4-dihydroxybenzoic acid + O2
?
-
-
-
?
3,4-dihydroxybenzoic acid + O2
?
-
-
-
?
4 1,2,3-trihydroxybenzene + O2
?
-
i.e pyrogallol
-
-
?
4 1,2,3-trihydroxybenzene + O2
?
-
i.e pyrogallol
-
-
?
4 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
4 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
4 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
4 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
best substrate
-
-
?
4 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
4 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
4 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
4 2,6-dimethoxyphenol + O2
?
-
-
-
-
?
4 2,6-dimethoxyphenol + O2
?
Opuntia vulgaris
-
-
-
-
?
4 2,6-dimethoxyphenol + O2
?
-
-
-
?
4 2,6-dimethoxyphenol + O2
?
-
-
-
-
?
4 2,6-dimethoxyphenol + O2
?
-
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
-
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
-
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
FJ560721
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
-
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
-
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
-
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
-
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
-
-
-
-
?
4 catechol + O2
4 1,2-benzoquinone + 2 H2O
-
-
-
-
?
4 guaiacol + O2
?
-
-
-
?
4 guaiacol + O2
?
-
-
-
?
4 guaiacol + O2
?
-
-
-
?
4 guaiacol + O2
?
-
-
-
-
?
4 syringaldazine + O2
?
-
-
-
?
4 syringaldazine + O2
?
-
-
-
?
4 syringic acid + O2
4 4-carboxy-2,6-dimethoxyphenoxyl + 2 H2O
-
-
-
-
?
4 syringic acid + O2
4 4-carboxy-2,6-dimethoxyphenoxyl + 2 H2O
-
-
-
-
?
4 syringic acid + O2
4 4-carboxy-2,6-dimethoxyphenoxyl + 2 H2O
-
-
-
-
?
4 syringic acid + O2
4 4-carboxy-2,6-dimethoxyphenoxyl + 2 H2O
-
-
-
-
?
4-aminoantipyrine + phenol + O2
? + H2O
-
-
-
-
?
4-aminoantipyrine + phenol + O2
? + H2O
-
-
-
-
?
4-aminoantipyrine + phenol + O2
? + H2O
-
-
-
-
?
4-aminoantipyrine + phenol + O2
? + H2O
-
-
-
-
?
4-aminoantipyrine + phenol + O2
? + H2O
-
-
-
-
?
4-hydroxy-3,5-dimethoxybenzaldehyde azine + O2
?
-
i.e. syringaldazine
-
-
?
4-hydroxy-3,5-dimethoxybenzaldehyde azine + O2
?
i.e. syringaldazine
-
-
?
4-hydroxy-3,5-dimethoxybenzaldehyde azine + O2
?
i.e. syringaldazine
-
-
?
4-hydroxy-3,5-dimethoxybenzaldehyde azine + O2
?
-
i.e. syringaldazine
-
-
?
4-hydroxy-3,5-dimethoxybenzaldehyde azine + O2
?
-
i.e. syringaldazine
-
-
?
4-hydroxy-3,5-dimethoxybenzaldehyde azine + O2
?
-
-
-
-
?
4-hydroxy-3,5-dimethoxybenzaldehyde azine + O2
?
-
-
-
-
?
4-hydroxybenzoic acid + O2
?
-
-
-
?
4-hydroxybenzoic acid + O2
?
-
-
-
-
?
4-methoxyphenol + O2
?
-
-
-
-
?
4-methoxyphenol + O2
?
-
-
-
-
?
4-methyl catechol + O2
?
-
-
-
-
?
4-methyl catechol + O2
?
-
-
-
-
?
4-methyl catechol + O2
?
-
-
-
-
?
4-methylcatechol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
4-methylcatechol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
4-methylcatechol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
4-methylcatechol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
4-methylcatechol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
4-methylcatechol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
4-methylcatechol + O2
?
Sporothrix carnis
-
98% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
4-methylcatechol + O2
?
Sporothrix carnis CPF-05
-
98% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
4-methylcatechol + O2
? + H2O
-
0.9% of activity with syringaldazine
-
-
?
4-methylcatechol + O2
? + H2O
-
18% of activity with 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
4-methylcatechol + O2
? + H2O
-
18% of activity with 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
4-phenylenediamine + O2
?
-
-
-
-
r
4-phenylenediamine + O2
?
-
-
-
-
r
4-phenylenediamine + O2
?
-
-
-
-
?
4-phenylenediamine + O2
?
-
-
-
?
acetosyringone + O2
?
-
-
-
?
acetosyringone + O2
?
-
-
-
?
acid red 6B + O2
?
addition of mediators including methyl syringate, 3,5-dimethoxy-4-hydroxybenzaldehyde, syringic acid, 1-hydroxybenzotriazole, and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) strongly promote the decolorization rates of the recombinant enzyme rLcc9 on the dyes. Methyl syringate is the best mediator. The decolorization rate of acid red 6B is 98.6%
-
-
?
acid red 6B + O2
?
addition of mediators including methyl syringate, 3,5-dimethoxy-4-hydroxybenzaldehyde, syringic acid, 1-hydroxybenzotriazole, and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) strongly promote the decolorization rates of the recombinant enzyme rLcc9 on the dyes. Methyl syringate is the best mediator. The decolorization rate of acid red 6B is 98.6%
-
-
?
alpha-naphthol + O2
?
-
22.0% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
alpha-naphthol + O2
?
-
-
-
-
?
ascorbate + O2
?
-
-
-
-
?
ascorbate + O2
?
-
-
-
-
?
ascorbate + O2
?
-
-
-
-
?
ascorbate + O2
?
-
-
-
-
?
ascorbate + O2
?
-
-
-
-
?
ascorbate + O2
?
-
-
-
-
?
bilirubin + O2
?
-
-
-
?
Brilliant blue + O2
?
-
-
-
-
?
Brilliant blue + O2
?
-
-
-
-
?
Bromocresol Purple + O2
?
-
the enzyme efficiently decolorized triphenylmethane dyes such as Malachite Green (87.8%), Bromocresol Purple (71.6%), and Methyl Violet (68.1%) without redox mediator
-
-
?
Bromocresol Purple + O2
?
-
the enzyme efficiently decolorized triphenylmethane dyes such as Malachite Green (87.8%), Bromocresol Purple (71.6%), and Methyl Violet (68.1%) without redox mediator
-
-
?
caffeic acid + 4-aminoantipyrine + O2
? + H2O
-
713% of the activity with phenol
-
-
?
caffeic acid + 4-aminoantipyrine + O2
? + H2O
-
126% of the activity with phenol
-
-
?
caffeic acid + 4-aminoantipyrine + O2
? + H2O
-
39% of the activity with phenol
-
-
?
caffeic acid + O2
?
-
24.3% of the activity with guaiacol
-
-
?
caffeic acid + O2
?
-
24.3% of the activity with guaiacol
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 4-aminoantipyrine + O2
? + H2O
-
1340% of the activity with phenol
-
-
?
catechol + 4-aminoantipyrine + O2
? + H2O
-
136% of the activity with phenol
-
-
?
catechol + 4-aminoantipyrine + O2
? + H2O
-
176% of the activity with phenol
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
85.4% of the activity with guaiacol
-
-
?
catechol + O2
?
-
85.4% of the activity with guaiacol
-
-
?
catechol + O2
?
-
28% of the activity compared to syringaldazine
-
-
?
catechol + O2
?
-
28% of the activity compared to syringaldazine
-
-
?
catechol + O2
?
-
27.5% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
catechol + O2
?
-
27.5% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
1.8% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
catechol + O2
?
-
1.8% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
11.5% activity compared to 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
catechol + O2
?
Loweporus lividus
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
low activity
-
-
?
catechol + O2
?
-
low activity
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
Trametes hirsuta Ig-9 / CGMCC 2422
-
-
-
-
?
catechol + O2
?
-
44% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
catechol + O2
?
-
44% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
catechol + O2
? + H2O
-
11% of activity with syringaldazine
-
-
?
catechol + O2
? + H2O
-
-
-
-
?
catechol + O2
? + H2O
-
-
-
-
?
catechol + O2
? + H2O
Loweporus lividus MTCC-1178
-
-
-
-
?
catechol + O2
? + H2O
-
-
-
-
?
catechol + O2
? + H2O
-
2.44% of activity with syringaldazine
-
-
?
catechol + O2
? + H2O
-
6.2% of activity with 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
catechol + O2
? + H2O
-
6.2% of activity with 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
chlorogenic acid + O2
?
-
-
-
-
?
chlorogenic acid + O2
?
-
-
-
-
?
chlorogenic acid + O2
?
Thermochaetoides thermophila
-
-
-
-
?
chlorogenic acid + O2
?
Thermochaetoides thermophila O-453
-
-
-
-
?
Congo Red + O2
?
decolorization with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), acetosyringone or syringaldehyde as mediator
-
-
?
Congo Red + O2
?
the enzyme decolorizes the azo dye
-
-
?
Congo Red + O2
?
the enzyme decolorizes the azo dye
-
-
?
coniferic acid + O2
? + H2O
-
-
-
-
?
coniferic acid + O2
? + H2O
-
-
-
-
?
coniferyl alcohol + O2
?
-
-
-
-
?
coniferyl alcohol + O2
?
-
-
-
-
?
coniferyl alcohol + O2
?
the enzyme transforms the non-phenolic substrate at pH 4.5 only when recombinantly expressed in the yeast Yarrowia lipolytica strain Po1t, overview
-
-
?
Coomassie brilliant blue + O2
?
-
72.35% decolourisation efficiency
-
-
?
Coomassie brilliant blue + O2
?
-
72.35% decolourisation efficiency
-
-
?
D-catechin + O2
?
-
-
-
-
?
D-catechin + O2
?
Thermochaetoides thermophila
-
-
-
-
?
D-catechin + O2
?
Thermochaetoides thermophila O-453
-
-
-
-
?
diethylaniline + 4-aminoantipyrine + O2
? + H2O
-
10% of the activity with phenol
-
-
?
diethylaniline + 4-aminoantipyrine + O2
? + H2O
-
60% of the activity with phenol
-
-
?
diethylaniline + 4-aminoantipyrine + O2
? + H2O
-
103% of the activity with phenol
-
-
?
dimethylaniline + 4-aminoantipyrine + O2
? + H2O
-
40% of the activity with phenol
-
-
?
dimethylaniline + 4-aminoantipyrine + O2
? + H2O
-
160% of the activity with phenol
-
-
?
dimethylaniline + 4-aminoantipyrine + O2
? + H2O
-
165% of the activity with phenol
-
-
?
dopa + O2
?
-
-
-
-
?
DOPA + O2
? + H2O
-
-
-
-
?
DOPA + O2
? + H2O
-
the enzyme laccase catalyses the formation of melanin by oxidizing L-DOPA, initiating a series of presumably spontaneous reactions that ultimately leads to the polymerization of the pigment in the yeast cell wall. There, melanin protects the cell from a multitude of environmental and host assaults. Kinetics of dopachrome formation are similar for L- and D-DOPA
-
-
?
dopamine + O2
?
-
-
-
-
?
dopamine + O2
?
-
-
-
-
?
dopamine + O2
?
-
-
-
-
?
Erichrome black + O2
?
-
40.20% decolourisation efficiency
-
-
?
Erichrome black + O2
?
-
40.20% decolourisation efficiency
-
-
?
eugenol + O2
?
-
-
-
-
?
ferrocenemonocarboxylic acid + O2
?
-
-
-
-
?
ferrocenemonocarboxylic acid + O2
?
-
-
-
?
ferrocenemonocarboxylic acid + O2
?
-
-
-
?
ferrocenemonocarboxylic acid + O2
?
-
-
-
-
?
ferrocyanide + O2
?
-
-
-
-
?
ferrocyanide + O2
?
-
-
-
-
?
ferrocyanide + O2
?
-
-
-
-
?
ferrocyanide + O2
?
-
-
-
-
?
ferrocyanide + O2
?
-
-
-
?
ferrocyanide + O2
?
-
-
-
?
ferrocyanide + O2
?
-
-
-
?
ferrocyanide + O2
?
-
-
-
-
?
ferrocyanide + O2
?
-
-
-
-
?
ferulic acid + O2
3-(4-hydroxy-3-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
Coriolisimus fulvocinerea
-
-
-
-
?
ferulic acid + O2
3-(4-hydroxy-3-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
ferulic acid + O2
3-(4-hydroxy-3-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
ferulic acid + O2
3-(4-hydroxy-3-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
ferulic acid + O2
3-(4-hydroxy-3-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
ferulic acid + O2
3-(4-hydroxy-3-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
ferulic acid + O2
3-(4-hydroxy-3-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
ferulic acid + O2
3-(4-hydroxy-3-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
ferulic acid + O2
?
-
-
-
-
?
ferulic acid + O2
?
-
-
-
-
?
ferulic acid + O2
?
-
-
-
?
ferulic acid + O2
?
Fomes sclerodermeus
-
-
-
-
?
ferulic acid + O2
?
Fomes sclerodermeus BAFC 2752
-
-
-
-
?
ferulic acid + O2
?
-
-
-
-
?
ferulic acid + O2
?
-
-
-
-
?
ferulic acid + O2
?
-
-
-
-
?
ferulic acid + O2
?
-
-
-
?
ferulic acid + O2
?
-
-
-
?
ferulic acid + O2
?
-
-
-
-
?
ferulic acid + O2
?
Thermochaetoides thermophila
-
-
-
-
?
ferulic acid + O2
?
-
as active as caffeic acid
-
-
?
ferulic acid + O2
?
-
-
-
-
?
ferulic acid + O2
?
-
-
-
-
?
ferulic acid + O2
?
-
24% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
ferulic acid + O2
?
-
24% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
ferulic acid + O2
? + H2O
-
-
-
-
?
ferulic acid + O2
? + H2O
-
13.6% of activity with syringaldazine
-
-
?
ferulic acid + O2
? + H2O
-
9.4% of activity with 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
ferulic acid + O2
? + H2O
-
9.4% of activity with 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
fluorene + O2
? + H2O
-
-
-
?
fluorene + O2
? + H2O
-
-
-
?
gallic acid + O2
?
-
-
-
-
?
gallic acid + O2
?
-
-
-
-
?
gallic acid + O2
?
-
13.7% of the activity with guaiacol
-
-
?
gallic acid + O2
?
-
13.7% of the activity with guaiacol
-
-
?
gallic acid + O2
?
-
45% of the activity compared to syringaldazine
-
-
?
gallic acid + O2
?
-
45% of the activity compared to syringaldazine
-
-
?
gallic acid + O2
?
-
-
-
-
?
gallic acid + O2
?
-
-
-
-
?
gallic acid + O2
?
-
-
-
-
?
gallic acid + O2
?
-
-
-
-
?
gallic acid + O2
?
-
-
-
-
?
gallic acid + O2
?
Thermochaetoides thermophila
-
-
-
-
?
gallic acid + O2
?
-
54% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
gallic acid + O2
?
-
54% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
guaiacol + 4-aminoantipyrine + O2
? + H2O
-
1500% of the activity with phenol
-
-
?
guaiacol + 4-aminoantipyrine + O2
? + H2O
-
55% of the activity with phenol
-
-
?
guaiacol + 4-aminoantipyrine + O2
? + H2O
-
61% of the activity with phenol
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
Coriolisimus fulvocinerea
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
i.e. 1-hydroxy-2-methoxybenzene
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
6-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
90.6% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
2.3% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
guaiacol + O2
?
-
2.3% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
best substrate
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
1.4% compared to the activity with 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
Lyophyllum subglobisporium
-
-
-
-
?
guaiacol + O2
?
Lyophyllum subglobisporium ECN 100606
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
FJ560721
-
-
-
?
guaiacol + O2
?
FJ560721
-
-
-
?
guaiacol + O2
?
-
16% of the activity with 2,6-dimethoxyphenol
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
Sporothrix carnis
-
98% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
guaiacol + O2
?
Sporothrix carnis CPF-05
-
98% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
Thermochaetoides thermophila
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
Trametes hirsuta Ig-9 / CGMCC 2422
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
?
-
83% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
guaiacol + O2
?
-
-
-
-
?
guaiacol + O2
? + H2O
-
21% of activity with syringaldazine
-
-
?
guaiacol + O2
? + H2O
-
-
-
-
?
guaiacol + O2
? + H2O
-
-
-
-
?
guaiacol + O2
? + H2O
-
-
-
?
guaiacol + O2
? + H2O
-
-
-
-
?
guaiacol + O2
? + H2O
-
-
-
-
?
guaiacol + O2
? + H2O
-
-
-
-
?
guaiacol + O2
? + H2O
-
-
-
-
?
guaiacol + O2
? + H2O
-
-
-
-
?
guaiacol + O2
? + H2O
Phlebia fascicularia
-
-
-
-
?
guaiacol + O2
? + H2O
-
-
-
-
?
guaiacol + O2
? + H2O
-
-
-
-
?
guaiacol + O2
? + H2O
-
-
-
-
?
guaiacol + O2
? + H2O
-
6.41% of activity with syringaldazine
-
-
?
guaiacol + O2
? + H2O
-
-
-
-
?
guaiacol + O2
? + H2O
-
-
-
?
guaiacol + O2
? + H2O
-
-
-
-
?
guaiacol + O2
? + H2O
-
-
-
?
guaiacol + O2
? + H2O
-
33% of activity with 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
homovanillic acid + O2
?
-
-
-
-
?
homovanillic acid + O2
?
-
-
-
-
?
hydrocaffeic acid + 4-aminoantipyrine + O2
? + H2O
-
1200% of the activity with phenol
-
-
?
hydrocaffeic acid + 4-aminoantipyrine + O2
? + H2O
-
190% of the activity with phenol
-
-
?
hydrocaffeic acid + 4-aminoantipyrine + O2
? + H2O
-
185% of the activity with phenol
-
-
?
hydroquinone + 4-aminoantipyrine + O2
? + H2O
-
494% of the activity with phenol
-
-
?
hydroquinone + 4-aminoantipyrine + O2
? + H2O
-
63% of the activity with phenol
-
-
?
hydroquinone + 4-aminoantipyrine + O2
? + H2O
-
89% of the activity with phenol
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
13.5% activity compared to 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
hydroquinone + O2
?
-
-
-
?
hydroquinone + O2
?
FJ560721
-
-
-
?
hydroquinone + O2
?
FJ560721
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
-
-
-
?
hydroquinone + O2
? + H2O
-
-
-
-
?
hydroquinone + O2
? + H2O
-
9.95% of activity with syringaldazine
-
-
?
hydroquinone + O2
? + H2O
-
60% of activity with 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
indigo carmine + O2
?
decolorization with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), acetosyringone or syringaldehyde as mediator
-
-
?
indigo carmine + O2
?
decolorization with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), acetosyringone or syringaldehyde as mediator
-
-
?
indigo carmine + O2
?
addition of mediators including methyl syringate, 3,5-dimethoxy-4-hydroxybenzaldehyde, syringic acid, 1-hydroxybenzotriazole, and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) strongly promote the decolorization rates of the recombinant enzyme rLcc9 on the dyes. Methyl syringate is the best mediator. The decolorization rate of Indigo carmine is 99.1%
-
-
?
indigo carmine + O2
?
addition of mediators including methyl syringate, 3,5-dimethoxy-4-hydroxybenzaldehyde, syringic acid, 1-hydroxybenzotriazole, and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) strongly promote the decolorization rates of the recombinant enzyme rLcc9 on the dyes. Methyl syringate is the best mediator. The decolorization rate of Indigo carmine is 99.1%
-
-
?
K4[Fe(CN)6] + O2
?
-
-
-
?
K4[Fe(CN)6] + O2
?
-
-
-
?
K4[Fe(CN)6] + O2
?
-
-
-
?
K4[Fe(CN)6] + O2
?
-
-
-
?
L-DOPA + O2
?
-
-
-
-
?
L-DOPA + O2
?
-
35% of the activity compared to syringaldazine
-
-
?
L-DOPA + O2
?
-
13.7% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
L-DOPA + O2
? + H2O
-
-
-
-
?
L-DOPA + O2
? + H2O
-
-
-
-
?
L-DOPA + O2
? + H2O
-
15.4% of activity with syringaldazine
-
-
?
L-epicatechin + O2
?
Thermochaetoides thermophila
-
-
-
-
?
L-epicatechin + O2
?
Thermochaetoides thermophila O-453
-
-
-
-
?
L-tyrosine + O2
?
-
-
-
-
?
L-tyrosine + O2
?
-
-
-
-
?
m-chlorophenol + 4-aminoantipyrine + O2
? + H2O
-
80% of the activity with phenol
-
-
?
m-chlorophenol + 4-aminoantipyrine + O2
? + H2O
-
45% of the activity with phenol
-
-
?
m-chlorophenol + 4-aminoantipyrine + O2
? + H2O
-
50% of the activity with phenol
-
-
?
Malachite green
indigo carmine
-
-
-
?
Malachite green
indigo carmine
-
-
-
?
Malachite Green + O2
?
-
-
-
-
?
Malachite Green + O2
?
decolorization with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), acetosyringone or syringaldehyde as mediator
-
-
?
Malachite Green + O2
?
decolorization with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), acetosyringone or syringaldehyde as mediator
-
-
?
Malachite Green + O2
?
-
-
-
?
Malachite Green + O2
?
-
-
-
?
Malachite Green + O2
?
-
the enzyme efficiently decolorized triphenylmethane dyes such as Malachite Green (87.8%), Bromocresol Purple (71.6%), and Methyl Violet (68.1%) without redox mediator
-
-
?
Malachite Green + O2
?
-
the enzyme efficiently decolorized triphenylmethane dyes such as Malachite Green (87.8%), Bromocresol Purple (71.6%), and Methyl Violet (68.1%) without redox mediator
-
-
?
Malachite Green + O2
?
-
57.84% decolourisation efficiency
-
-
?
Malachite Green + O2
?
-
57.84% decolourisation efficiency
-
-
?
melanin + O2
?
-
-
-
-
?
melanin + O2
?
-
the enzyme decolorizes fungal melanin from Alternaria alternata strain NBCR 31805 or black hyphae of Cladosporium sp. strain B-1, but not synthetic melanin, overview
-
-
?
methyl syringate
? + H2O
-
-
-
-
?
methyl syringate
? + H2O
-
-
-
-
?
methyl syringate
? + H2O
-
-
-
-
?
methyl syringate
? + H2O
-
-
-
-
?
methyl syringate
? + H2O
-
-
-
-
?
Methyl Violet + O2
?
-
the enzyme efficiently decolorized triphenylmethane dyes such as Malachite Green (87.8%), Bromocresol Purple (71.6%), and Methyl Violet (68.1%) without redox mediator
-
-
?
Methyl Violet + O2
?
-
the enzyme efficiently decolorized triphenylmethane dyes such as Malachite Green (87.8%), Bromocresol Purple (71.6%), and Methyl Violet (68.1%) without redox mediator
-
-
?
N,N-dimethyl-1,4-phenylenediamine + O2
?
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + O2
?
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + O2
?
-
49.4% activity compared to 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
N,N-dimethyl-1,4-phenylenediamine + O2
?
-
42.6% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
N,N-dimethyl-p-phenylenediamine + 4-aminoantipyrine + O2
? + H2O
-
900% of the activity with phenol
-
-
?
N,N-dimethyl-p-phenylenediamine + 4-aminoantipyrine + O2
? + H2O
-
278% of the activity with phenol
-
-
?
N,N-dimethyl-p-phenylenediamine + 4-aminoantipyrine + O2
? + H2O
-
377% of the activity with phenol
-
-
?
N,N-dimethyl-p-phenylenediamine + O2
?
-
-
-
?
N,N-dimethyl-p-phenylenediamine + O2
?
Thermochaetoides thermophila
-
-
-
-
?
N,N-dimethyl-p-phenylenediamine + O2
?
-
-
-
-
?
N-ethyl-N-(2-hydroxy-3-sulfopropyl)-3-methylaniline + 4-aminoantipyrine + O2
? + H2O
-
15% of the activity with phenol
-
-
?
N-ethyl-N-(2-hydroxy-3-sulfopropyl)-3-methylaniline + 4-aminoantipyrine + O2
? + H2O
-
143% of the activity with phenol
-
-
?
N-ethyl-N-(2-hydroxy-3-sulfopropyl)-3-methylaniline + 4-aminoantipyrine + O2
? + H2O
-
198% of the activity with phenol
-
-
?
o-chlorophenol + 4-aminoantipyrine + O2
? + H2O
-
190% of the activity with phenol
-
-
?
o-chlorophenol + 4-aminoantipyrine + O2
? + H2O
-
102% of the activity with phenol
-
-
?
o-chlorophenol + 4-aminoantipyrine + O2
? + H2O
-
150% of the activity with phenol
-
-
?
o-chlorophenol + O2
? + H2O
-
-
-
-
?
o-chlorophenol + O2
? + H2O
-
-
-
-
?
o-cresol + 4-aminoantipyrine + O2
? + H2O
-
816% of the activity with phenol
-
-
?
o-cresol + 4-aminoantipyrine + O2
? + H2O
-
40% of the activity with phenol
-
-
?
o-cresol + 4-aminoantipyrine + O2
? + H2O
-
39% of the activity with phenol
-
-
?
o-cresol + O2
6-hydroxy-2-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
o-cresol + O2
6-hydroxy-2-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
o-dianisidine
?
-
-
-
-
?
o-dianisidine
?
-
-
-
-
?
o-dianisidine + O2
?
-
90% of the activity compared to syringaldazine
-
-
?
o-dianisidine + O2
?
-
-
-
?
o-diphenol + O2
?
-
-
-
-
?
o-diphenol + O2
?
-
-
-
-
?
o-tolidine + O2
?
-
best substrate
-
-
?
o-tolidine + O2
?
-
9.0% compared to the activity with 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
o-toluidine + O2
?
-
42.53% of the activity with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
o-toluidine + O2
?
-
15.7% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
o-toluidine + O2
?
-
15.7% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
p-chlorophenol + O2
? + H2O
-
-
-
-
?
p-chlorophenol + O2
? + H2O
-
-
-
-
?
p-coumaric acid + O2
? + H2O
-
-
-
-
?
p-coumaric acid + O2
? + H2O
-
-
-
-
?
p-coumaric acid + O2
? + H2O
-
-
-
-
?
p-cresol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
p-cresol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
p-cresol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
p-cresol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
p-cresol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
p-cresol + O2
6-hydroxy-4-methylcyclohexa-2,4-dienone + H2O
-
-
-
-
?
p-hydroxybenzoic acid + 4-aminoantipyrine + O2
? + H2O
-
52% of the activity with phenol
-
-
?
p-hydroxybenzoic acid + 4-aminoantipyrine + O2
? + H2O
-
35% of the activity with phenol
-
-
?
p-hydroxybenzoic acid + 4-aminoantipyrine + O2
? + H2O
-
3% of the activity with phenol
-
-
?
p-methoxyphenol + O2
? + H2O
-
-
-
-
?
p-methoxyphenol + O2
? + H2O
-
-
-
-
?
p-methoxyphenol + O2
? + H2O
-
-
-
-
?
p-phenylenediamine + O2
?
-
-
-
-
?
p-phenylenediamine + O2
?
-
-
-
-
?
p-phenylenediamine + O2
?
-
107% of the activity compared to syringaldazine
-
-
?
p-phenylenediamine + O2
?
-
107% of the activity compared to syringaldazine
-
-
?
p-phenylenediamine + O2
?
-
-
-
-
?
p-phenylenediamine + O2
?
-
-
-
-
?
p-phenylenediamine + O2
?
-
-
-
?
p-phenylenediamine + O2
?
-
46% of the activity with 2,6-dimethoxyphenol
-
-
?
p-phenylenediamine + O2
?
-
-
-
-
?
p-phenylenediamine + O2
?
-
-
-
-
?
p-phenylenediamine + O2
?
-
7.5% of the activity with 2,2-azino-bis-(3-ethylbenzthiazolin-6-sulfonate)
-
-
?
p-phenylenediamine + O2
?
-
-
-
-
?
p-phenylenediamine + O2
? + H2O
-
-
-
-
?
p-phenylenediamine + O2
? + H2O
-
-
-
-
?
p-phenylenediamine + O2
? + H2O
-
-
-
-
?
p-phenylenediamine + O2
? + H2O
-
-
-
?
p-phenylenediamine + O2
? + H2O
-
-
-
-
?
p-phenylenediamine + O2
? + H2O
-
-
-
-
?
p-phenylenediamine + O2
? + H2O
-
-
-
-
?
p-phenylenediamine + O2
? + H2O
-
33% of the activity with N,N-dimethyl-p-phenylenediamine sulfate
-
-
?
p-phenylenediamine + O2
? + H2O
-
-
-
-
?
p-toluidine + 4-aminoantipyrine + O2
? + H2O
-
348% of the activity with phenol
-
-
?
p-toluidine + 4-aminoantipyrine + O2
? + H2O
-
70% of the activity with phenol
-
-
?
p-toluidine + 4-aminoantipyrine + O2
? + H2O
-
51% of the activity with phenol
-
-
?
phenol + O2
?
-
-
-
-
?
phenol + O2
? + H2O
-
-
-
-
?
phenol + O2
? + H2O
-
-
-
-
?
poly R-478 + O2
?
-
dye decolorization activity
-
-
?
poly R-478 + O2
?
-
dye decolorization activity
-
-
?
poly R-478 + O2
?
Oscillatoria subuliformis
-
dye decolorization activity
-
-
?
poly R-478 + O2
?
Oscillatoria subuliformis BDU100712
-
dye decolorization activity
-
-
?
poly R-478 + O2
?
-
dye decolorization activity
-
-
?
poly R-478 + O2
?
-
dye decolorization activity
-
-
?
poly R-478 + O2
?
-
dye decolorization activity
-
-
?
poly R-478 + O2
?
-
dye decolorization activity
-
-
?
poly R-478 + O2
?
-
dye decolorization activity
-
-
?
poly R-478 + O2
?
-
dye decolorization activity
-
-
?
poly R-478 + O2
?
-
dye decolorization activity
-
-
?
poly R-478 + O2
?
-
dye decolorization activity
-
-
?
pyrocatechol + O2
?
-
-
-
-
?
pyrocatechol + O2
?
-
-
-
-
?
pyrocatechol + O2
?
Sporothrix carnis
-
99% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
pyrocatechol + O2
?
Sporothrix carnis CPF-05
-
99% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
pyrocatechol + O2
?
-
-
-
-
?
pyrocatechol + O2
?
-
-
-
-
?
pyrogallol + 4-aminoantipyrine + O2
? + H2O
-
473% of the activity with phenol
-
-
?
pyrogallol + 4-aminoantipyrine + O2
? + H2O
-
8% of the activity with phenol
-
-
?
pyrogallol + 4-aminoantipyrine + O2
? + H2O
-
10% of the activity with phenol
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
95.2% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
pyrogallol + O2
?
-
95.2% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
?
pyrogallol + O2
?
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
3.5% activity compared to 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
pyrogallol + O2
?
Loweporus lividus
-
-
-
-
?
pyrogallol + O2
?
FJ560721
-
-
-
?
pyrogallol + O2
?
FJ560721
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
57% of the activity with 2,6-dimethoxyphenol
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
?
pyrogallol + O2
?
-
-
-
?
pyrogallol + O2
?
-
7.7% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
pyrogallol + O2
?
-
19% of the activity with 2,2-azino-bis-(3-ethylbenzthiazolin-6-sulfonate)
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
? + H2O
-
7% of activity with syringaldazine
-
-
?
pyrogallol + O2
? + H2O
-
-
-
-
?
pyrogallol + O2
? + H2O
-
-
-
-
?
pyrogallol + O2
? + H2O
Loweporus lividus MTCC-1178
-
-
-
-
?
pyrogallol + O2
? + H2O
-
-
-
-
?
pyrogallol + O2
? + H2O
-
22% of the activity with N,N-dimethyl-p-phenylenediamine sulfate
-
-
?
pyrogallol + O2
? + H2O
-
2% of activity with 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
quinol + O2
? + H2O
-
-
-
-
?
quinol + O2
? + H2O
Coriolisimus fulvocinerea
-
-
-
-
?
quinol + O2
? + H2O
-
-
-
-
?
quinol + O2
? + H2O
-
-
-
-
?
quinol + O2
? + H2O
-
-
-
-
?
quinol + O2
? + H2O
-
-
-
-
?
quinol + O2
? + H2O
-
-
-
-
?
quinol + O2
? + H2O
-
-
-
-
?
quinol + O2
? + H2O
-
-
-
-
?
quinol + O2
? + H2O
-
-
-
-
?
quinol + O2
? + H2O
-
-
-
-
?
quinol + O2
? + H2O
-
-
-
-
?
quinol + O2
? + H2O
-
-
-
-
?
quinol + O2
? + H2O
Thermochaetoides thermophila
-
-
-
-
?
reactive 203 brilliant orange K-7R + O2
?
addition of mediators including methyl syringate, 3,5-dimethoxy-4-hydroxybenzaldehyde, syringic acid, 1-hydroxybenzotriazole, and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) strongly promote the decolorization rates of the recombinant enzyme rLcc9 on the dyes. Methyl syringate is the best mediator. The decolorization rate of reactive 203 brilliant orange K-7R is 94.9%
-
-
?
reactive 203 brilliant orange K-7R + O2
?
addition of mediators including methyl syringate, 3,5-dimethoxy-4-hydroxybenzaldehyde, syringic acid, 1-hydroxybenzotriazole, and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) strongly promote the decolorization rates of the recombinant enzyme rLcc9 on the dyes. Methyl syringate is the best mediator. The decolorization rate of reactive 203 brilliant orange K-7R is 94.9%
-
-
?
Reactive Black B + O2
?
the enzyme decolorizes the azo dye
-
-
?
Reactive Black B + O2
?
the enzyme decolorizes the azo dye
-
-
?
Reactive Black WNN + O2
?
the enzyme decolorizes the azo dye
-
-
?
Reactive Black WNN + O2
?
the enzyme decolorizes the azo dye
-
-
?
Remazol Brilliant Blue R + O2
?
decolorization with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), acetosyringone or syringaldehyde as mediator
-
-
?
Remazol Brilliant Blue R + O2
?
decolorization with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), acetosyringone or syringaldehyde as mediator
-
-
?
Remazol Brilliant Blue R + O2
?
-
the partial purified laccase shows a high efficient decolorization ability of Remazol Brilliant Blue R with 80.8% within 5 h at 30°C and pH 5.5
-
-
?
Remazol Brilliant Blue R + O2
?
-
the partial purified laccase shows a high efficient decolorization ability of Remazol Brilliant Blue R with 80.8% within 5 h at 30°C and pH 5.5
-
-
?
Remazol Brilliant Blue R + O2
?
the enzyme decolorizes the anthraquinone dye
-
-
?
Remazol Brilliant Blue R + O2
?
the enzyme decolorizes the anthraquinone dye
-
-
?
Remazol brilliant orange 3R + O2
?
-
-
-
-
?
Remazol brilliant orange 3R + O2
?
-
-
-
-
?
Remazol red 106 + O2
?
-
-
-
-
?
Remazol red 106 + O2
?
-
-
-
-
?
resorcinol + 4-aminoantipyrine + O2
? + H2O
-
731% of the activity with phenol
-
-
?
resorcinol + 4-aminoantipyrine + O2
? + H2O
-
79% of the activity with phenol
-
-
?
resorcinol + 4-aminoantipyrine + O2
? + H2O
-
73% of the activity with phenol
-
-
?
resorcinol + O2
?
-
-
-
-
?
resorcinol + O2
?
-
-
-
-
?
sinapic acid + O2
3-(3,5-dimethoxy-4-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
Coriolisimus fulvocinerea
-
-
-
-
?
sinapic acid + O2
3-(3,5-dimethoxy-4-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
sinapic acid + O2
3-(3,5-dimethoxy-4-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
sinapic acid + O2
3-(3,5-dimethoxy-4-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
sinapic acid + O2
3-(3,5-dimethoxy-4-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
sinapic acid + O2
3-(3,5-dimethoxy-4-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
sinapic acid + O2
3-(3,5-dimethoxy-4-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
sinapic acid + O2
3-(3,5-dimethoxy-4-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
sinapic acid + O2
?
-
-
-
-
?
sinapic acid + O2
?
-
-
-
?
sinapic acid + O2
?
-
-
-
?
sinapic acid + O2
?
-
-
-
-
?
sinapic acid + O2
? + H2O
-
-
-
-
?
sinapic acid + O2
? + H2O
-
-
-
-
?
sinapic acid + O2
? + H2O
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
90% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
90% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
i.e. 4-hydroxy-3,5-dimethoxybenzaldehyde azine
-
-
?
syringaldazine + O2
?
-
i.e. 4-hydroxy-3,5-dimethoxybenzaldehyde azine
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
0.5% compared to the activity with 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
Loweporus lividus
-
i.e. 2-hydroxy-3, 5-dimethoxybenaldehyde azine
-
-
?
syringaldazine + O2
?
Loweporus lividus MTCC-1178
-
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
Myrioconium sp.
-
-
-
-
?
syringaldazine + O2
?
Myrioconium sp. UHH 1-13-18-4
-
-
-
-
?
syringaldazine + O2
?
-
3% of the activity with 2,6-dimethoxyphenol
-
-
?
syringaldazine + O2
?
-
best substrate
-
-
?
syringaldazine + O2
?
-
best substrate
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
1% of the activity with 2,2-azino-bis-(3-ethylbenzthiazolin-6-sulfonate)
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
Sporothrix carnis
-
90% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
syringaldazine + O2
?
Sporothrix carnis CPF-05
-
90% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
the enzyme is able to rapidly decolourize the dye Indigo carmine in the presence of syringaldehyde as a redox mediator, at pH 9.0 and 45°C
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
?
-
best substrate
-
-
?
syringaldazine + O2
?
Thermochaetoides thermophila
-
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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?
syringaldazine + O2
?
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prefrred substrate
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syringaldazine + O2
?
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?
syringaldazine + O2
?
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148% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
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syringaldazine + O2
?
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148% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
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?
syringaldazine + O2
?
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about 17% of the activity with 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
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tannic acid + O2
?
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tannic acid + O2
?
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63.1 % of the activity with guaiacol
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tannic acid + O2
?
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63.1 % of the activity with guaiacol
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tannic acid + O2
?
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17.9% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
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tannic acid + O2
?
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17.9% of the activity compared to 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
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?
tannic acid + O2
?
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?
thioglycolic lignin + O2
?
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?
thioglycolic lignin + O2
?
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?
Turquoise blue HF6 + O2
?
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?
Turquoise blue HF6 + O2
?
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?
tyrosine + O2
?
the enzyme catalyzes oxidative cross-linking of tyrosine and potato patatin and lysozyme-derived peptides
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tyrosine + O2
?
the enzyme catalyzes oxidative cross-linking of tyrosine and potato patatin and lysozyme-derived peptides
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?
vanillic acid + O2
4-carboxy-2-methoxycyclohexa-2,4-dienone + H2O
Coriolisimus fulvocinerea
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?
vanillic acid + O2
4-carboxy-2-methoxycyclohexa-2,4-dienone + H2O
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?
vanillic acid + O2
4-carboxy-2-methoxycyclohexa-2,4-dienone + H2O
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?
vanillic acid + O2
4-carboxy-2-methoxycyclohexa-2,4-dienone + H2O
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?
vanillic acid + O2
4-carboxy-2-methoxycyclohexa-2,4-dienone + H2O
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-
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?
vanillic acid + O2
?
Fomes sclerodermeus
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?
vanillic acid + O2
?
Fomes sclerodermeus BAFC 2752
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?
vanillic acid + O2
?
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?
vanillic acid + O2
?
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?
vanillic acid + O2
?
Thermochaetoides thermophila
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?
vanillic acid + O2
?
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?
vanillin + O2
?
Coriolisimus fulvocinerea
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?
vanillin + O2
?
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-
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?
veratric acid + O2
?
Fomes sclerodermeus
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?
veratric acid + O2
?
Fomes sclerodermeus BAFC 2752
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?
additional information
?
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overview
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?
additional information
?
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overview
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?
additional information
?
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diphenols not substrates
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?
additional information
?
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CotA fails to oxidize coumaric acid, cinnamic acid, and vanillic acid
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?
additional information
?
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the enzyme mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2-naphthol is achieved with 77% conversion of 250 mg/l 2-naphtol in 15 min
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?
additional information
?
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the enzyme mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2-naphthol is achieved with 77% conversion of 250 mg/l 2-naphtol in 15 min
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?
additional information
?
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a 3D model shows potential binding affinities with ferulic acid, caffeic acid, and vanillin
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?
additional information
?
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a 3D model shows potential binding affinities with ferulic acid, caffeic acid, and vanillin
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?
additional information
?
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a 3D model shows potential binding affinities with ferulic acid, caffeic acid, and vanillin
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?
additional information
?
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no activity with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), syringaldazine, catechole, benzidine, 4-cresol, pyrogallol, caffeic acid and tyrosine. Decolorization of structurally different azo dyes using purified laccase: Methyl red, Reactive orange 16, Methyl orange, Sudan IV, Reactive red M5B, Direct brown MR, Reactive red 141, no decolorization of Congo red, Eriochrome black T, and Trypan blue
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?
additional information
?
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decolorization of azo dyes: the enzyme decolorizes sulphonyl green BLE up to 97% at pH 7.0 after 2 h incubation at 35°C, without any addition of mediators. No activity with resorcinol and tyrosine
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?
additional information
?
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no activity with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), syringaldazine, catechole, benzidine, 4-cresol, pyrogallol, caffeic acid and tyrosine. Decolorization of structurally different azo dyes using purified laccase: Methyl red, Reactive orange 16, Methyl orange, Sudan IV, Reactive red M5B, Direct brown MR, Reactive red 141, no decolorization of Congo red, Eriochrome black T, and Trypan blue
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?
additional information
?
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decolorization of azo dyes: the enzyme decolorizes sulphonyl green BLE up to 97% at pH 7.0 after 2 h incubation at 35°C, without any addition of mediators. No activity with resorcinol and tyrosine
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?
additional information
?
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reactive blue 19, reactive black 5 and indigo carmine cand be efficiently decolorized by the purified laccase in the presence of a mediator 2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
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?
additional information
?
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reactive blue 19, reactive black 5 and indigo carmine cand be efficiently decolorized by the purified laccase in the presence of a mediator 2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
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?
additional information
?
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two anthraquinonic dyes (reactive blue 4 and reactive yellow brown) and two azo dyes (reactive red 11 and reactive brilliant orange) can be partially decolorized by purified laccase in the absence of a mediator. The decolorization process is efficiently promoted when methylsyringate is present, with more than 90 % of color removal occurring in 3 h at pH 7.0 or 9.0
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?
additional information
?
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poorly oxidizes m-phenols (resorcinol) and shows no activity towards tyrosine
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?
additional information
?
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poorly oxidizes m-phenols (resorcinol) and shows no activity towards tyrosine
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?
additional information
?
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Malachite green is efficiently degraded by recombinant laccase, especially in combination with mediators
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?
additional information
?
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Malachite green is efficiently degraded by recombinant laccase, especially in combination with mediators
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?
additional information
?
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overview
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?
additional information
?
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the enzyme efficiently performs dye decoloration of anthraquinone dye RBBR
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?
additional information
?
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overview
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?
additional information
?
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2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), as a mediator, is necessary in decolorizing Malachite green
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?
additional information
?
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2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), as a mediator, is necessary in decolorizing Malachite green
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?
additional information
?
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the enzyme shows dye decolorization potential, overview
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?
additional information
?
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the enzyme shows dye decolorization potential, overview
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?
additional information
?
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the enzyme shows dye decolorization potential, overview
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?
additional information
?
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Lac3 exhibits higher decolorization efficiency than Lac4 for eleven out of thirteen different dyes. Mild synergistic decolorization by the laccases isoenzymes Lac 3 and Lac4 is observed for triphenylmethane dyes but not for anthraquinone and azo dyes
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?
additional information
?
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Lac3 exhibits higher decolorization efficiency than Lac4 for eleven out of thirteen different dyes. Mild synergistic decolorization by the laccases isoenzymes Lac 3 and Lac4 is observed for triphenylmethane dyes but not for anthraquinone and azo dyes
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?
additional information
?
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Lac3 exhibits higher decolorization efficiency than Lac4 for eleven out of thirteen different dyes. Mild synergistic decolorization by the laccases isoenzymes Lac 3 and Lac4 is observed for triphenylmethane dyes but not for anthraquinone and azo dyes
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?
additional information
?
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activities are below detection limits for veratryl alcohol, 2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) and ferulic acid
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?
additional information
?
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-
activities are below detection limits for veratryl alcohol, 2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) and ferulic acid
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?
additional information
?
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Coriolisimus fulvocinerea
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overview substrates, kinetics and stoichiometry
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?
additional information
?
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involved in production of oxygen free radicals
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?
additional information
?
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a high-molecular-weight kraft lignin iss effectively polymerized by the enzyme
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?
additional information
?
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the enzyme is capable of decolorizing between 50% and 100% of indigoid, triarylmethane, azoic and anthraquinonic synthetic dyes in the presence of the natural redox mediator acetosyringone within 2 h of incubation at pH 6 and 70°C
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?
additional information
?
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the enzyme is capable of decolorizing between 50% and 100% of indigoid, triarylmethane, azoic and anthraquinonic synthetic dyes in the presence of the natural redox mediator acetosyringone within 2 h of incubation at pH 6 and 70°C
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?
additional information
?
-
substrate specificity, overview, no activity with tyrosine, phenol, 2,4-dichlorophenol, and 5-sulphosalycylic acid
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?
additional information
?
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substrate specificity, overview, no activity with tyrosine, phenol, 2,4-dichlorophenol, and 5-sulphosalycylic acid
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?
additional information
?
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in the presence of metal ions (1 mM Cu2+ and 1 mM Mn2+), the enzyme form preheated at 6-90°C achieves 97% of Malachite green and 98.75% of Indigo blue (both at 2%, w/v) dye decolorization in 12 h. Activity with e.g. Alizarin red S, Congo red, Crystal violet, Eosin, Indigo blue, Lactophenol cotton blue, MG, Methylene blue, and Phenolphthalein, overview
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?
additional information
?
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involved in decomposition of lignin, discussion of physiological role
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?
additional information
?
-
presence of Fe2+ reduces the apparent phenoloxidase activity, Cu(II) enhances this activity six- to sevenfold
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-
additional information
?
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involved in decomposition of lignin, discussion of physiological role
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?
additional information
?
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LacG decolorizes 43% of Congo red and 14% of Malachite green, and the addition of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a redox mediator dramatically increases the dye decolorization efficiency
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-
additional information
?
-
-
substrate specificity, no activity with L-tyrosine, overview
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?
additional information
?
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-
substrate specificity, no activity with L-tyrosine, overview
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?
additional information
?
-
-
-
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?
additional information
?
-
-
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) acts as an effective mediator for amine oxidation by the enzyme. Higher concentrations of 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) achieve higher tyramine degradation percentages to nearly 100% with 5 mM
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?
additional information
?
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-
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) acts as an effective mediator for amine oxidation by the enzyme. Higher concentrations of 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) achieve higher tyramine degradation percentages to nearly 100% with 5 mM
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?
additional information
?
-
-
involved in melanin synthesis
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?
additional information
?
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-
no substrate: tyrosine, veratryl alcohol
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?
additional information
?
-
-
substrate specificity in descending order: syringaldazine, 4-phenylenediamine, 2,6-dimethoxyphenol, guaiacol, catechol, the purified enzyme decolorizes azo dyes, such as acid red 18, acid Black 1, and direct blue 71, up to 90, 87, and 72%, respectively, optimization, overview
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?
additional information
?
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-
substrate specificity, overview
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?
additional information
?
-
-
substrate specificity, overview
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-
?
additional information
?
-
-
no activity with L-tyrosine
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?
additional information
?
-
no activity with L-tyrosine
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?
additional information
?
-
-
no activity with L-tyrosine
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?
additional information
?
-
the enzyme shows broad substrate specificity. The recombinant His-tagged MmPPOA-695 shows kinetic properties on catechol higher than for known laccases. Laccase belongs to the group of blue, multicopper oxidases which couple the four-electron reduction of dioxygen to water with the oxidation of a broad range of substrates (including phenols, polyphenols, arylamines, anilines, hydroxyindols, and thiols)
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?
additional information
?
-
-
the enzyme shows broad substrate specificity. The recombinant His-tagged MmPPOA-695 shows kinetic properties on catechol higher than for known laccases. Laccase belongs to the group of blue, multicopper oxidases which couple the four-electron reduction of dioxygen to water with the oxidation of a broad range of substrates (including phenols, polyphenols, arylamines, anilines, hydroxyindols, and thiols)
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?
additional information
?
-
the enzyme shows broad substrate specificity. The recombinant His-tagged MmPPOA-695 shows kinetic properties on catechol higher than for known laccases. Laccase belongs to the group of blue, multicopper oxidases which couple the four-electron reduction of dioxygen to water with the oxidation of a broad range of substrates (including phenols, polyphenols, arylamines, anilines, hydroxyindols, and thiols)
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?
additional information
?
-
-
the enzyme decolorizes Congo red, Malachite green, Crystal violet, and Methylene green dyes at various decolorization rates of 63-90% without the addition of an expensive mediator
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?
additional information
?
-
FJ560721
substrate specificity of purified enzyme, overview. No activity with ferulic acid
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-
?
additional information
?
-
FJ560721
substrate specificity of purified enzyme, overview. No activity with ferulic acid
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?
additional information
?
-
Opuntia vulgaris
-
in the presence of metal ions (1 mM Cu2+ and 1 mM Mn2+), the enzyme form preheated at 6-90°C achieves 97% of Malachite green and 98.75% of Indigo blue (both at 2%, w/v) dye decolorization in 12 h. Activity with e.g. Alizarin red S, Congo red, Crystal violet, Eosin, Indigo blue, Lactophenol cotton blue, MG, Methylene blue, and Phenolphthalein, overview
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-
?
additional information
?
-
Acid Green 27, Acid Violet 7 and Indigo Carmine are used in a dye decolorization assay, overview
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?
additional information
?
-
Acid Green 27, Acid Violet 7 and Indigo Carmine are used in a dye decolorization assay, overview
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?
additional information
?
-
-
the enzyme possesses a catalytic His residue at the active site, substrate specificity, overview
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?
additional information
?
-
-
the enzyme possesses a catalytic His residue at the active site, substrate specificity, overview
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?
additional information
?
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-
the crude enzyme as well as the purified laccase is able to decolourize dyes from the textile industries, including remazol brilliant blue R, neolane blue and neolane pink
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?
additional information
?
-
guaiacol and tannic acid are poorly oxidized. Ferulic and or 3,4-dihydroxyphenylalanine (DOPA) are not oxidized at all. The industrially important dyes Acid Yellow, Bromo Cresol Purple, Nitrosulfonazo III, and Reactive Black 5 are more effciently decolorized by PsLac1 in the presence of the redox mediator 1-hydroxybenzotriazole
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-
-
additional information
?
-
guaiacol and tannic acid are poorly oxidized. Ferulic and or 3,4-dihydroxyphenylalanine (DOPA) are not oxidized at all. The industrially important dyes Acid Yellow, Bromo Cresol Purple, Nitrosulfonazo III, and Reactive Black 5 are more effciently decolorized by PsLac1 in the presence of the redox mediator 1-hydroxybenzotriazole
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-
-
additional information
?
-
-
the enzyme decolorizes fungal melanin and several other dye reagents, overview
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-
?
additional information
?
-
-
the enzyme decolorizes fungal melanin and several other dye reagents, overview
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-
?
additional information
?
-
laccases are able to oxidize a variety of substrates, ranging from mono- and polyphenols over aminophenols, methoxyphenols and aromatic amines to polycyclic aromatic hydrocarbons and certain lignin moieties
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-
?
additional information
?
-
-
laccases are able to oxidize a variety of substrates, ranging from mono- and polyphenols over aminophenols, methoxyphenols and aromatic amines to polycyclic aromatic hydrocarbons and certain lignin moieties
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-
?
additional information
?
-
laccases are able to oxidize a variety of substrates, ranging from mono- and polyphenols over aminophenols, methoxyphenols and aromatic amines to polycyclic aromatic hydrocarbons and certain lignin moieties
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-
?
additional information
?
-
-
the laccase exhibits an inhibitory activity toward HIV-1 reverse transcriptase with an IC50 of 0.0022 mM
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-
?
additional information
?
-
the genes encoding the laccacse isozymes are differently regulated, overview
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?
additional information
?
-
the genes encoding the laccacse isozymes are differently regulated, overview
-
-
?
additional information
?
-
the genes encoding the laccacse isozymes are differently regulated, overview
-
-
?
additional information
?
-
the genes encoding the laccacse isozymes are differently regulated, overview
-
-
?
additional information
?
-
-
the genes encoding the laccacse isozymes are differently regulated, overview
-
-
?
additional information
?
-
the genes encoding the laccacse isozymes are differently regulated, overview
-
-
?
additional information
?
-
the genes encoding the laccacse isozymes are differently regulated, overview
-
-
?
additional information
?
-
the genes encoding the laccacse isozymes are differently regulated, overview
-
-
?
additional information
?
-
the genes encoding the laccacse isozymes are differently regulated, overview
-
-
?
additional information
?
-
-
no significant enzymic activity with guaiacol
-
-
?
additional information
?
-
-
no activity with tyrosine and hydroquinone, the enzyme in absence of a mediator oxidizes anthracene to anthraquinone to 95%
-
-
?
additional information
?
-
-
no activity with ferulic acid and veratryl alcohol
-
-
?
additional information
?
-
-
the isolated enzyme from Pleurotus ostreatus mycelium has both bilirubin oxidase and laccase activities
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-
?
additional information
?
-
-
the enzyme catalyzes the oxidation of a wide range of compounds, including poly-phenols and anilines. The one electron oxidation of the reducing substrate occurs concomitantly with the four-electron reduction of molecular oxygen to water
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-
?
additional information
?
-
-
no activity with ferulic acid and veratryl alcohol
-
-
?
additional information
?
-
-
the isolated enzyme from Pleurotus ostreatus mycelium has both bilirubin oxidase and laccase activities
-
-
?
additional information
?
-
-
no activity with tyrosine and hydroquinone, the enzyme in absence of a mediator oxidizes anthracene to anthraquinone to 95%
-
-
?
additional information
?
-
-
no substrate: caffeic acid, ferulic acid, tyrosine
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
Lac1 decolorizes 0.02% (v/v) Remazol Brilliant Blue R and Bromophenol Blue more than 90% in 100 min. Lac1 completely decolorizes 0.002% (v/v) in 100 min. Reactive Orange 16 and Poly R-478 are not decolorized by Lac1 alone. In addition, Lac1 decolorized a wide range of substrates, such as the carcinogen, Poly R-478, in the presence of violuric acid as mediator
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-
?
additional information
?
-
-
Lac1 decolorizes 0.02% (v/v) Remazol Brilliant Blue R and Bromophenol Blue more than 90% in 100 min. Lac1 completely decolorizes 0.002% (v/v) in 100 min. Reactive Orange 16 and Poly R-478 are not decolorized by Lac1 alone. In addition, Lac1 decolorized a wide range of substrates, such as the carcinogen, Poly R-478, in the presence of violuric acid as mediator
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-
?
additional information
?
-
Lac1 does not oxidize L-tyrosine
-
-
?
additional information
?
-
-
Lac1 does not oxidize L-tyrosine
-
-
?
additional information
?
-
Lac1 decolorizes 0.02% (v/v) Remazol Brilliant Blue R and Bromophenol Blue more than 90% in 100 min. Lac1 completely decolorizes 0.002% (v/v) in 100 min. Reactive Orange 16 and Poly R-478 are not decolorized by Lac1 alone. In addition, Lac1 decolorized a wide range of substrates, such as the carcinogen, Poly R-478, in the presence of violuric acid as mediator
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?
additional information
?
-
Lac1 does not oxidize L-tyrosine
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-
?
additional information
?
-
-
the laccase can effectively decolorize two commercial wool dyes, weak acid blue AS and diamond black PV, up to 88% and 74.7%, respectively, within 2 h in the absence of any redox mediators
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-
?
additional information
?
-
-
the laccase can effectively decolorize two commercial wool dyes, weak acid blue AS and diamond black PV, up to 88% and 74.7%, respectively, within 2 h in the absence of any redox mediators
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-
?
additional information
?
-
-
overview
-
-
?
additional information
?
-
-
approximately 66% of the Acid Blue 129 at 100 mg/l is decolorized by 2.5 U of the purified laccase after a 120 min incubation at 50°C, Acid Red 1 at 20 mg/l and Reactive Black 5 at 50 mg/l are decolorized by the purified laccase after the addition of Acid Blue 129 at 100 mg/l.
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?
additional information
?
-
-
isozyme laccase II shows a higher activity and wider substrate specificity compared to the other isozymes, overview
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?
additional information
?
-
-
isozyme laccase II shows a higher activity and wider substrate specificity compared to the other isozymes, overview
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?
additional information
?
-
phenolic compounds are oxidized in the presence of the enzyme under alkaline but not acidic conditions. Conversely, nonphenolic compounds are oxidized at acidic but not alkaline pH. The enzyme catalyses oxidation of nonphenolic compounds more efficiently than that of phenols. The two-domain laccase displays a cytochrome c oxidase activity and exhibits no ferroxidase activity
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?
additional information
?
-
-
phenolic compounds are oxidized in the presence of the enzyme under alkaline but not acidic conditions. Conversely, nonphenolic compounds are oxidized at acidic but not alkaline pH. The enzyme catalyses oxidation of nonphenolic compounds more efficiently than that of phenols. The two-domain laccase displays a cytochrome c oxidase activity and exhibits no ferroxidase activity
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?
additional information
?
-
phenolic compounds are oxidized in the presence of the enzyme under alkaline but not acidic conditions. Conversely, nonphenolic compounds are oxidized at acidic but not alkaline pH. The enzyme catalyses oxidation of nonphenolic compounds more efficiently than that of phenols. The two-domain laccase displays a cytochrome c oxidase activity and exhibits no ferroxidase activity
-
-
?
additional information
?
-
-
the enzyme can efficiently decolourise Indigo Carmine, Coomassie Brilliant Blue R-250, Congo Red, Malachite Green and Alizarin in the presence of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a redox mediator
-
-
-
additional information
?
-
-
the enzyme possesses a catalytic His residue at the active site, substrate specificity, overview
-
-
?
additional information
?
-
Thermochaetoides thermophila
-
no activity with tyrosine
-
-
?
additional information
?
-
-
enzymatic synthesis of morpholine-substituted quinones with cytotoxic, antibacterial and antifungal activities, overview
-
-
?
additional information
?
-
-
the enzyme oxidizes a range of phenolic and nonphenolic compounds using molecular oxygen as an electron acceptor to produce water with a broad substrate specificity
-
-
?
additional information
?
-
the purified enzyme is able to decolourize Green Dye, Orange Dye and Acid Red Dye. The enzyme is unable to decolourize NBB, RBB, or Congo Red. However, with 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate) (5 mM) acting as redox mediator, the enzyme decolourizes NBB, RBB, or Congo Red
-
-
?
additional information
?
-
-
the purified enzyme is able to decolourize Green Dye, Orange Dye and Acid Red Dye. The enzyme is unable to decolourize NBB, RBB, or Congo Red. However, with 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate) (5 mM) acting as redox mediator, the enzyme decolourizes NBB, RBB, or Congo Red
-
-
?
additional information
?
-
broad substrate specificity
-
-
?
additional information
?
-
-
broad substrate specificity
-
-
?
additional information
?
-
broad substrate specificity
-
-
?
additional information
?
-
-
the enzyme transforms toluene and substituted toluenes to corresponding benzaldehyde and substituted benzaldehydes in the absence of mediator molecules with higher catalytic efficiency as compared to other known laccases
-
-
?
additional information
?
-
-
the enzyme transforms toluene and substituted toluenes to corresponding benzaldehyde and substituted benzaldehydes in the absence of mediator molecules with higher catalytic efficiency as compared to other known laccases
-
-
?
additional information
?
-
-
overview substrates, kinetics and stoichiometry
-
-
?
additional information
?
-
-
substrate specificities of a laccase chemically modified by attachment of PEG on soluble and cellulose-bound dye substrates, overview
-
-
?
additional information
?
-
-
polymerization of gliadins by laccase is observed only when a high enzyme dosage and prolonged incubation are used
-
-
?
additional information
?
-
-
no activity with veratryl alcohol, phenol, and L-tyrosine, substrate specificity, overview
-
-
?
additional information
?
-
Trametes hirsuta Ig-9 / CGMCC 2422
-
no activity with veratryl alcohol, phenol, and L-tyrosine, substrate specificity, overview
-
-
?
additional information
?
-
-
overview substrates, kinetics and stoichiometry
-
-
?
additional information
?
-
-
overview substrates, kinetics and stoichiometry
-
-
?
additional information
?
-
-
low decolourisation efficiency towards Azure B (1.78 %) and methylene blue (0.38 %)
-
-
-
additional information
?
-
-
low decolourisation efficiency towards Azure B (1.78 %) and methylene blue (0.38 %)
-
-
-
additional information
?
-
-
substrate specificity, overview. No activity with tyrosine. Dye decolorization capacity of an alkali-resistant and metal-tolerant laccase from Trametes pubescens, overview
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with tyrosine. Dye decolorization capacity of an alkali-resistant and metal-tolerant laccase from Trametes pubescens, overview
-
-
?
additional information
?
-
-
laccase couples catalytic oxidation of lignin with the four electron reduction of oxygen, the final product is water without any harmful intermediate making laccase the best candidate for the environmentally benign bleaching process
-
-
?
additional information
?
-
-
decolorization of an anthraquinone dye by the enzyme, best at pH 3.0 and 50°C, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, no activity with tyrosine, phenol, vanillin, and gallic acid
-
-
?
additional information
?
-
-
laccase couples catalytic oxidation of lignin with the four electron reduction of oxygen, the final product is water without any harmful intermediate making laccase the best candidate for the environmentally benign bleaching process
-
-
?
additional information
?
-
-
substrate specificity, overview, no activity with tyrosine, phenol, vanillin, and gallic acid
-
-
?
additional information
?
-
-
substrate specificity, overview. No or poor activity with caffeic acid, hydroquinone, veratryl alcohol, or ferulic acid
-
-
?
additional information
?
-
-
substrate specificity, overview. No or poor activity with caffeic acid, hydroquinone, veratryl alcohol, or ferulic acid
-
-
?
additional information
?
-
-
degradation of polychlorinated phenols and guaiacols
-
-
?
additional information
?
-
-
study on assays and conditions
-
-
?
additional information
?
-
the enzyme is involved in bioremdiation
-
-
?
additional information
?
-
-
the enzyme is involved in bioremdiation
-
-
?
additional information
?
-
-
purified recombinant laccase decolorizes more than 90% of Remazol Brilliant Blue R initially at 80 mg/l1 after 16 h at 45°C and pH 5 when 25 U laccase/ml is used. The purified recombinant laccase can efficiently decolorize Remazol Brilliant Blue R without additional redox mediators
-
-
?
additional information
?
-
the enzyme is involved in bioremdiation
-
-
?
additional information
?
-
-
free and immobilized laccase is employed for decolorization of three different synthetic dyes (malachite green, methylene blue and congo red). Approximately 100% of malachite green, 90% of methylene blue and 60% of congo red dyes at initial concentration of 200 mg/l are decolorized within 16, 18 and 20 h, respectively by laccase immobilized in sol-gel matrix in the presence of 1-hydroxybenzotriazole mediator
-
-
?
additional information
?
-
-
free and immobilized laccase is employed for decolorization of three different synthetic dyes (malachite green, methylene blue and congo red). Approximately 100% of malachite green, 90% of methylene blue and 60% of congo red dyes at initial concentration of 200 mg/l are decolorized within 16, 18 and 20 h, respectively by laccase immobilized in sol-gel matrix in the presence of 1-hydroxybenzotriazole mediator
-
-
?
additional information
?
-
-
in the presence of 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as the mediator, the enzyme transforms toluene, 3-nitrotoluene and 4-chlorotoluene to benzaldehyde, 3-nitrobenzaldehyde and 4-chlorobenzaldehyde, respectively
-
-
?
additional information
?
-
-
in the presence of 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as the mediator, the enzyme transforms toluene, 3-nitrotoluene and 4-chlorotoluene to benzaldehyde, 3-nitrobenzaldehyde and 4-chlorobenzaldehyde, respectively
-
-
?
additional information
?
-
the use of rlac1338 and lac2-9 alone had no degradation effect on the industrial dyes [indigo, amaranth, bromophenol blue, acid violet 7, Congo red, coomassie brilliant blue (G250)], however, adding small molecular mediators Ca2+ and 2,2'-azino-bis(3-ethylbenzothiazo-line)-6-sulfonic acid at the same time can significantly improve the degradation ability
-
-
-
additional information
?
-
-
poor substrates: guaiacol, catechol, no substrate: tyrosine, L-3,4-dimethoxyphenol, dihydroxyphenylalanine
-
-
?
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1,4-diethylenedioxide
-
complete inhibition at 50% or above
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
shows substrate inhibition at high concentrations above 6 mM
2,2-bipyridyl
-
1 mM, 61% residual activity
2,2-dipyridyl
1 mM, 13.4% loss of activity. 10 mM, 24.8% loss of activity
2,3-Dimercaptopropanol
-
-
2,4-dithio-6-pyrimidine
-
1 mM, 31% residual activity
2,6-dimethoxyphenol
substrate inhibition
2-mercaptobenzothiazole
Thermochaetoides thermophila
-
-
3,4,5-hydroxybenzoic acid propyl ester
-
-
4,5-methyl-o-phenylenediamine
-
50% inhibition at 5 mM
4-coumaric acid
32.5% residual activity at 1 mM
4-hydroxyphenylacetic acid
-
effects on enzyme kinetics with substrate N,N-dimethyl-4-phenylenediamine, overview
4-hydroxyphenylpropionic acid
-
effects on enzyme kinetics with substrate N,N-dimethyl-4-phenylenediamine, overview
4-nitrophenol
-
effects on enzyme kinetics with substrate N,N-dimethyl-4-phenylenediamine, overview
5,5 dithiobis(2-nitrobenzoate)
Acetylacetone
-
1 mM, 27% inhibition
Al2+
-
3 mM, 23% inhibition
-
AlCl3
-
10 mM, 40% inhibition
ascorbic acid
Thermochaetoides thermophila
-
-
BaCl2
5 mM, 10% inhibition
bathocuproinedisulfonic acid
-
1 mM, 39% residual activity
Benzene
-
1 h, 20% loss of activity by 20% (v/v), 40% loss of activity by 50% (v/v)
bipyridyl
-
90% inhibition
butanol
-
25%, 42% inhibition
Cationic detergents
-
-
-
CdCl2
-
1 mM, 24.6% inhibition
Cetylpyridinium bromide
-
-
cetyltrimethyl ammonium bromide
50% inhibition
cetyltrimethylammonium bromide
-
-
chitosan
-
conjugated to the enzyme, with 81-93% laccase being conjugated, a moderate activity loss of 16-28% occurs in conjugation solution, a second severe activity loss of 63-78% occurs during a cycle of phase change consisting of precipitation, centrifugation and re-dissolution of the enzymechitosan conjugates, the chitosan molecular size has little effect, overview
Co3+
20 mM, weak inhibitory effect
CoSO4
-
10 mM, 9% inhibition
Cr2+
-
10 mM, 5% inhibition
Dichloromethane
-
50% (v/v), 80% inhibition
diethyldithiocarbamic acid
-
-
Diethylenetriaminepentaacetic acid
-
10 mM, 76% loss of activity
dimethyldithiocarbamate trihydrate
-
1 mM, 13% residual activity
DL-dithiothreitol
0.01 mM, 9.5% loss of activity. 0.1 mM, complete loss of activity
FeCl2
MK290990.1
1 mM, 30 min, 84.47% residual activity
H2O2
significantly inhibits at above 4.85 mmol/l
hydroxylammonium chloride
-
-
isoascorbic acid
Thermochaetoides thermophila
-
-
KCN
competitive, complete inhibition
KI
-
5 mM, 25% inhibition
MgCl2
MK290990.1
1 mM, 30 min, 89.34% residual activity
MgSO4
-
10 mM, 6% inhibition
MnSO4
-
10 mM, 8% inhibition
Mo2+
-
100 mM, 82% inhibition
N,N-Dimethylformamide
-
1 h, 10% loss of activity by 20% (v/v), 40% loss of activity by 50% (v/v)
N-hydroxylglycine
-
0.1 mM, 87% inhibition
Na2SO4
-
100 mM, 7% inhibition
NaNO3
-
100 mM, 50% inhibition
Neocuprein
-
50% inhibition at 5 mM
NiCl2
MK290990.1
1 mM, 30 min, 80.65% residual activity
NiSO4
5 mM, 4% inhibition
oxalate
-
1 mM, 35% inhibition
p-coumarate
-
0.1 mM, complete inhibition
p-nitrophenol
-
50% inhibition at 5 mM
Phenanthroline
-
95% inhibition
Phenylthiourea
-
50% inhibition at 3 mM
potassium xanthogenate
Thermochaetoides thermophila
-
-
Propanol
-
25%, 17% inhibition
Salicylhydroxamic acid
-
0.08 mM, 85% inhibition
Semicarbazide
-
25% decrease in enzyme activity
Sn2+
4.6% residual activity at 1 mM
SnCl2
-
1 mM, 69% residual activity
Sodium bisulfite
Thermochaetoides thermophila
-
-
sodium bromide
-
50% inhibition at 195 mM
sodium chloride
-
50% inhibition at 52 mM
Sodium fluoride
-
50% inhibition at 0.08 mM
Sodium metabisulfite
Thermochaetoides thermophila
-
-
Sodium thioglycolate
-
45.3% residual activity at 10 mM
thiamine
-
50% inhibition at 0.95 mM
thiolglycolic acid
-
completely inhibited by 60 mM
Toluene
-
20% (v/v), 18% loss of activity
Triton X
-
2%, 61% inhibition
-
Triton X-100
Sporothrix carnis
-
1 mM, 35% inhibition
Tween 80
-
2%, 51% inhibition
Tween-80
1%, more than 50% loss of activity
1,10-phenanthroline
1 mM, 14.7% loss of activity. 10 mM, 89.1% loss of activity
1,10-phenanthroline
-
10 mM, complete loss of activity
1,10-phenanthroline
-
10 mM, complete loss of activity
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
200 mM, 80% inhibition
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
-
99.5% inhibition
1-Phenyl-2-thiourea
-
-
1-Phenyl-2-thiourea
Thermochaetoides thermophila
-
-
2-mercaptoethanol
-
0.05 mM, 29% loss of activity
2-mercaptoethanol
0.1 mM, 65.5% inhibition
2-mercaptoethanol
-
1 mM, complete inactivation
2-mercaptoethanol
competitive, complete inhibition
2-mercaptoethanol
-
1 mM, 68% inhibition
2-mercaptoethanol
-
1 mM, 97% inhibition
2-mercaptoethanol
-
complete inhibition of laccase activity at 0.1% concentration
2-mercaptoethanol
-
complete inhibition at 0.1 mM
2-mercaptoethanol
-
strong
2-mercaptoethanol
-
12.5 mM, complete inhibition
2-mercaptoethanol
Sporothrix carnis
-
1 mM, 23% inhibition
2-mercaptoethanol
Thermochaetoides thermophila
-
-
2-mercaptoethanol
-
93% inhibition at 1 mM
2-mercaptoethanol
-
5 mM, 15% loss of activity
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
5,5 dithiobis(2-nitrobenzoate)
-
-
5,5 dithiobis(2-nitrobenzoate)
-
-
5,5 dithiobis(2-nitrobenzoate)
-
-
8-hydroxyquinoline
-
-
8-hydroxyquinoline
-
70% inhibition at 1 mM
acetone
-
mutant enzyme V159E/N398D
acetone
-
50% (v/v), 90% inhibition
acetone
-
complete inhibition at 50% or above
acetone
31% (v/v) 50% inhibition
acetone
-
25%, 20% inhibition
acetone
-
20% (v/v), 42% loss of activity
acetonitrile
-
completely inhibits enzyme activity
acetonitrile
-
complete inhibition at 50% or above
acetonitrile
4.5% (v/v) 50% inhibition
Ag+
-
complete inhibition at 20 mM
Ag+
-
8.13% inhibition at 10 mM
Al3+
-
10 mM, 3% inhibition
Al3+
activating at 1 mM, inhibitory at 10 mM
Al3+
strongly inhibits at 10 mM
Al3+
-
5 mM, 44% inhibition
Al3+
-
1 mM, 43% inhibition
Al3+
-
100 mM, 92% inhibition
Al3+
-
10 mM, 43% loss of activity
Al3+
-
14% inhibition at 5 mM
Al3+
-
11.6% inhibition at 1 mM
Al3+
-
5 mM, 60% loss of activity
azide
-
-
azide
-
100% inhibition at 0.1 mM
azide
-
85% inhibition at 1 mM
azide
Phlebia fascicularia
-
complete inhibition
azide
-
100 inhibition at 0.1 mM
azide
-
55-70% inhibition at 0.5 mM
azide
Thermochaetoides thermophila
-
-
azide
-
complete inhibition at 0.02 mM
azide
-
0.1 mM, 100% inhibition
Ba2+
-
10 mM, 16% inhibition
Ba2+
partially inhibits laccase activity
Ba2+
-
1 mM, 11% loss of activity
Ba2+
activating at 1 mM, inhibitory at 10 mM
Ba2+
-
5 mM, 27% inhibition
Ba2+
-
10 mM, 59% inhibition
Ba2+
-
1 mM, 52% inhibition
Ba2+
Sporothrix carnis
-
1 mM, 39% inhibition
Ba2+
-
10 mM, 26% loss of activity
Ba2+
-
10% inhibition at 1 mM
Ca2+
-
10 mM, 6% inhibition
Ca2+
-
1.25 mM, 8% inhibition. 10 mM, 17% inhibition
Ca2+
activating at 1 mM, inhibitory at 10 mM
Ca2+
-
1% residual activity at 10 mM; 86.6% residual activity at 10 mM
Ca2+
-
5 mM, 17% inhibition
Ca2+
-
inhibits the enzyme activity at 100 mM but increases it at 12.5-50 mM
Ca2+
-
significantly inhibition
Ca2+
-
10 mM, 80% inhibition
Ca2+
-
100 mM, 43% inhibition
Ca2+
89.8% residual activity at 1 mM
Ca2+
-
10 mM, 35% loss of activity
Ca2+
Sporothrix carnis
-
1 mM, 37% inhibition
Ca2+
-
200 mM, 66.72% residual activity
Ca2+
-
30 mM, 85% loss of activity
CaCl2
-
10 mM, 31% inhibition
CaCl2
MK290990.1
1 mM, 30 min, 90.15% residual activity
Cd2+
-
10 mM, 81% inhibition
Cd2+
-
1.25 mM, 6% inhibition. 10 mM, 20% inhibition
Cd2+
-
1 mM, 28% of inhibition
Cd2+
-
96.2% residual activity at 10 mM
Cd2+
-
71.1% residual activity at 20 mM
Cd2+
-
inhibits the enzyme activity at 100 mM but increases it at 12.5-50 mM
Cd2+
-
21% inhibition at 1 mM
Cd2+
-
significantly inhibition
Cd2+
-
100 mM, 92% inhibition
Cd2+
88.0% residual activity at 1 mM
Cd2+
-
40% inhibition at 20 mM, almost complete inhibition at 80 mM
Cd2+
-
5 mM, 78% loss of activity
chloroform
-
1 h, 20% loss of activity by 20% (v/v), 65% loss of activity by 50% (v/v)
chloroform
-
25%, 25% inhibition
Citric acid
-
CN-
-
-
CN-
-
100% inhibition at 1 mM
CN-
-
40-65% inhibition at 0.5 mM
CN-
Thermochaetoides thermophila
-
-
Co2+
-
1 mM, 79%% inhibition
Co2+
-
1.25 mM, 3% inhibition. 10 mM, 17% inhibition
Co2+
-
1 mM, 51% of inhibition
Co2+
-
1 mM, complete inhibition
Co2+
-
61.9% residual activity at 20 mM
Co2+
-
inhibits the enzyme activity at 100 mM but increases it at 12.5-50 mM
Co2+
-
29% inhibition at 1 mM
Co2+
-
significantly inhibition
Co2+
-
1 mM, 63% inhibition
Co2+
-
10 mM, 55% inhibition
Co2+
-
100 mM, 51% inhibition
Co2+
75.3% residual activity at 01 mM
Co2+
-
28% inhibition at 5 mM
Co2+
-
10 mM, 99% loss of activity
Co2+
-
5 mM, 67% loss of activity
CoCl2
5 mM, 19% inhibition
CoCl2
-
1 mM, 20.8% inhibition
Cr3+
activating at 1 mM, inhibitory at 10 mM
Cr3+
-
46.2% residual activity at 20 mM
Cr3+
-
23% inhibition at 5 mM
Cr3+
-
inhibits 13.8% at 1 mM
Cu2+
-
10 mM, 4% inhibition
Cu2+
-
1.25 mM, 9% inhibition. 10 mM, 19% inhibition
Cu2+
-
10 mM, 25% inhibition
Cu2+
-
68.9% residual activity at 20 mM
Cu2+
-
10 mM, 61% inhibition
Cu2+
-
3 mM, 16% inhibition
Cu2+
Sporothrix carnis
-
1 mM, 48% inhibition
Cu2+
-
200 mM, 65.15% residual activity
Cu2+
-
19% inhibition at 5 mM
Cu2+
-
10 mM, 23% loss of activity
Cu2+
-
40% inhibition at 20 mM, almost complete inhibition at 80 mM
CuSO4
-
10 mM, 19% inhibition
CuSO4
MK290990.1
1 mM, 30 min, 90.81% residual activity
cyanide
Phlebia fascicularia
-
complete inhibition
cysteine
-
-
cysteine
-
5 mM, 92% loss of activity
cysteine
Thermochaetoides thermophila
-
-
cysteine
-
0.1 mM, 100% inhibition
cysteine-HCl
-
complete inhibition at 0.1 mM
cysteine-HCl
Opuntia vulgaris
-
complete inhibition at 0.1 mM
desferrioxamine mesylate
-
-
desferrioxamine mesylate
-
-
desferrioxamine mesylate
-
-
diethyldicarbonate
-
inactivation in simple linear pseudo-first order kinetics, recovery by 0.5 M hydroxylamine
diethyldicarbonate
-
inactivation in simple linear pseudo-first order kinetics, recovery by 0.5 M hydroxylamine
diethyldicarbonate
-
inactivation in simple linear pseudo-first order kinetics, recovery by 0.5 M hydroxylamine
diethyldithiocarbamate
-
50% inhibition at 1.2 mM
diethyldithiocarbamate
-
-
diethyldithiocarbamate
-
-
diethyldithiocarbamate
-
15% inhibition at 1 mM
diethyldithiocarbamate
-
35% inhibition at 1 mM
diethyldithiocarbamate
-
50% inhibition at 0.02 mM
diethyldithiocarbamate
-
-
dimethyl sulfoxide
-
50% (v/v), 85% inhibition
dimethyl sulfoxide
-
1 h, 10% loss of activity by 20% (v/v), 40% loss of activity by 50% (v/v)
dithiothreitol
-
dithiothreitol
-
1 mM, complete inactivation
dithiothreitol
0.1 mM, complete inhibition
dithiothreitol
-
5 mM, complete inactivation. 1 mM, 80% loss of activity
dithiothreitol
-
activates laccase at lower concentration (0.1 mM) while inhibits the enzyme at concentrations beyond 0.1 mM in a concentration-dependent manner with complete inhibition of activity at 10 mM
dithiothreitol
0.1 mM, activity is reduced to 5.9%
dithiothreitol
0.1 mM, complete inactivation; 0.1 mM, complete inactivation
dithiothreitol
-
0.1 mM, complete inhibition
dithiothreitol
-
0.1 mM, complete inhibition
dithiothreitol
-
complete inhibition at 0.1 mM
dithiothreitol
-
complete inhibition at 2 mM
dithiothreitol
-
1 mM, 61% inhibition
dithiothreitol
-
5 mM, 81% inhibition
dithiothreitol
-
1 mM, 100% inhibition
dithiothreitol
-
0.1 mM, 98% inhibition
dithiothreitol
completely inhibited by 1.0 mM dithiothreitol
dithiothreitol
-
1 mM, 10% loss of activity
dithiothreitol
-
strong inhibition at 1 mM
dithiothreitol
-
5 mM, 65% loss of activity
dithiothreitol
-
0.1 mM, 100% inhibition
DMSO
-
mutant enzyme V159E/N398D
DMSO
10%, 50% loss of the original activity
DMSO
-
10 mM, 34% inhibition
DMSO
40% (v/v) 50% inhibition
DTT
0.1 mM, complete inhibition
DTT
complete inhibition at 5 mM
DTT
1 mM, complete inhibition
DTT
-
complete inhibition at 0.1 mM
DTT
-
43% inhibition at 10 mM
DTT
-
complete inhibition at over 10 mM with substrate 3,6-dimethoxyphenol and at over 20 mM with substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
DTT
-
complete inhibition at 1 mM
EDTA
-
-
EDTA
5 mM or 20 mM, partially inhibits activity
EDTA
-
mutant enzyme V159E/N398D
EDTA
-
1 mM, 31% inhibition
EDTA
-
50% inhibition at about 300 mM
EDTA
-
0.5 mM, 29% loss of activity
EDTA
5 mM, 51.5% inhibition
EDTA
-
28% inhibition at 40 mM
EDTA
-
1 mM, 15.6% loss of activity
EDTA
-
10 mM, 77% loss of activity
EDTA
-
5 mM, 84-87% inhibition (depending on purification method)
EDTA
-
10 mM, 10% inhibition
EDTA
50 mM, 70% loss of activity, laccase 3; 50 mM, 80% loss of activity, laccase 4
EDTA
-
10 mM, 6% inhibition
EDTA
1 mM, 67% inhibition
EDTA
-
1 mM, 90% residual activity
EDTA
-
complete inhibition at 1 mM
EDTA
-
1 mM, 20% inhibition
EDTA
-
6.8% residual activity at 1 mM, complete inhibition at 10 mM
EDTA
-
20.8% residual activity at 20 mM
EDTA
-
1 mM, 21% inhibition
EDTA
-
87% inhibition at 1 mM, complete inhibition at 2 mM
EDTA
-
1 mM, 95% inhibition
EDTA
-
10 mM, 6% inhibition
EDTA
Opuntia vulgaris
-
complete inhibition at 1 mM
EDTA
-
10 mM, 36% inhibition
EDTA
-
0.1 mM, complete inhibition
EDTA
Phlebia fascicularia
-
partiall inhibition
EDTA
-
60% inhibition at 100 mM
EDTA
50% residual activity at 10 mM
EDTA
-
completely inhibited by 200 mM
EDTA
-
16% inhibition at 10 mM
EDTA
Sporothrix carnis
-
1 mM, 29% inhibition
EDTA
-
5 mM, complete inhibition
EDTA
-
1 mM, 62% loss of activity
EDTA
-
1 mM, 67% residual activity
EDTA
MK290990.1
100 mM, 93.1% residual activity
EDTA
Thermochaetoides thermophila
-
5 mM, 67% inhibition. 10 mM, 95% inhibition
EDTA
the reaction in the presence of 0.1 mM CuSO4 is completely inhibited by the addition of 1 mM EDTA
EDTA
-
10 mM, 35% inhibition
EDTA
un competitive inhibition
EDTA
-
1 mM, 74.2% inhibition
EDTA
-
45% inhibition at 10 mM, 10% at 1 mM
EDTA
-
5 mM, 70% loss of activity
EDTA
-
1 mM, 20% inhibition
EGTA
-
-
EGTA
-
22% inhibition at 10 mM
ethanol
-
mutant enzyme V159E/N398D
ethanol
-
50% inhibition at 36%
ethanol
-
50% (v/v), 80% inhibition
ethanol
-
1 h, 20% loss of activity by 20% (v/v), 45% loss of activity by 50% (v/v)
ethanol
52% (v/v) 50% inhibition
ethanol
-
25%, 28% inhibition
ethanol
-
20% (v/v), 15% loss of activity
F-
Polyporus versicolor
-
-
F-
-
complete inhibition at 1 equivalent F- per type 2 Cu2+
Fe2+
partially inhibits laccase activity
Fe2+
-
5 mM, 59% loss of activity
Fe2+
10 mM, 94% loss of activity
Fe2+
-
1.25 mM, 31% inhibition. 10 mM, 61% inhibition
Fe2+
activating at 1 mM, inhibitory at 10 mM
Fe2+
-
complete inhibition at 10 mM
Fe2+
-
8.47% residual activity at 10 mM
Fe2+
-
4.0% residual activity at 20 mM
Fe2+
-
1 mM, reduces LacG activity to 55%
Fe2+
-
significantly inhibition
Fe2+
-
1 mM, complete inhibition
Fe2+
FJ560721
inhibits laccase activity completely at 10 mM
Fe2+
Opuntia vulgaris
-
complete inhibition at 10 mM
Fe2+
-
complete inhibition at 1 mM
Fe2+
-
50% inhibition at 50 mM
Fe2+
-
10 mM, 72.4% loss of activity
Fe2+
-
complete inhibition at 10 mM
Fe2+
-
10 mM, about 75% inhibition
Fe2+
-
200 mM, no residual activity
Fe2+
-
95% inhibition at 5 mM
Fe2+
-
10 mM, 97% loss of activity
Fe2+
-
5 mM, 60% loss of activity
Fe3+
-
10 mM, 29% inhibition
Fe3+
partially inhibits laccase activity
Fe3+
-
1.25 mM, 46% inhibition. 10 mM, 93% inhibition
Fe3+
activating at 1 mM, inhibitory at 10 mM
Fe3+
strongly inhibits at 10 mM
Fe3+
-
complete inhibition at 20 mM
Fe3+
-
complete inhibition at 1 mM
Fe3+
-
50% inhibition at 10 mM
FeCl3
5 mM, 14% loss of activity
FeCl3
-
5 mM, complete inhibition
Ferrous sulfate
-
-
Ferrous sulfate
Thermochaetoides thermophila
-
-
FeSO4
5 mM, complete loss of activity
glutathione
-
1 mM, complete inhibition
Hg2+
-
10 mM, 79% inhibition
Hg2+
-
1 mM, 4% inhibition
Hg2+
-
1.0 mM, 48% loss of activity
Hg2+
-
concentration-dependent inhibition up to 1 mM
Hg2+
-
1 mM, 93% of inhibition
Hg2+
-
7.4% residual activity at 5 mM
Hg2+
-
14% inhibition at 1 mM
Hg2+
-
significantly inhibition
Hg2+
-
1 mM, 50% inhibition
Hg2+
-
strong inhibition at 1 mM
Hg2+
-
1 mM, 44% inhibition. 3 mM, 95% inhibition
Hg2+
Sporothrix carnis
-
1 mM, 46% inhibition
Hg2+
Thermochaetoides thermophila
-
-
Hg2+
-
200 mM, no residual activity
Hg2+
-
10 mM, 80% loss of activity
Hg2+
-
inhibits 17.2% at 1 mM
Hg2+
-
5 mM, 90% loss of activity
HgCl2
competitive, complete inhibition
HgCl2
-
1 mM, 67% residual activity
HgCl2
-
1 mM, 33.3% inhibition
HgCl2
-
46% inhibition at 51 mM
hydroxylamine
-
competitive
hydroxylamine
-
1 mM, 62% residual activity
Isopropanol
-
1 h, 40% loss of activity by 20% (v/v), 65% loss of activity by 50% (v/v)
Isopropanol
60% (v/v) 50% inhibition
Isopropanol
-
20% (v/v), 30% loss of activity
K+
-
10 mM, 26% inhibition
K+
-
10 mM, 4% inhibition
K+
activating at 1 mM, inhibitory at 10 mM
K+
-
1 mM, 4% inhibition, 10 mM, 15% inhibition
K+
-
inhibits the enzyme activity at 100 mM but increases it at 12.5-50 mM
K+
65.1% residual activity at 10 mM
K+
-
10 mM, 7% loss of activity
KCl
-
10 mM, 21% inhibition
KCl
MK290990.1
1 mM, 30 min, 80.25% residual activity
kojic acid
12.5 mM, about 50% loss of activity
kojic acid
5 mM, complete inhibition
kojic acid
-
1 mM, 57% residual activity
kojic acid
-
47% inhibition at 1 mM
kojic acid
27.7% residual activity at 1 mM
kojic acid
-
3 mM, 48% inhibition
L-cysteine
-
1 mM, 95% inhibition
L-cysteine
-
50% inhibition at 0.52 mM
L-cysteine
-
0.05 mM, 44% loss of activity
L-cysteine
0.5 mM, 67% inhibition
L-cysteine
-
1 mM, complete inactivation
L-cysteine
0.1 mM, complete inhibition
L-cysteine
-
1 mM, reduced 87% of its original activity
L-cysteine
-
0.1 mM, complete inhibition
L-cysteine
0.1 mM, activity is reduced to 5.5%
L-cysteine
0.1 mM, complete inhibition
L-cysteine
-
0.1 mM, complete inhibition
L-cysteine
-
1 mM, 100% inhibition
L-cysteine
0.1 mM, 17% loss of activity. 1 mM, complete loss of activity
L-cysteine
-
89% inhibition at 0.1 mM, complete inhibition at 1 mM
L-cysteine
-
1 mM, 100% inhibition
L-cysteine
-
0.1 mM, 95% inhibition
L-cysteine
-
5 mM, complete inhibition
L-cysteine
completely inhibited by 1.0 mM L-cysteine
L-cysteine
-
50 mM, 15% inhibition
L-cysteine
-
44% inhibition at 10 mM
L-cysteine
-
0.5 mM, 25% inhibition
L-cysteine
-
complete inhibition at 10 mM
L-cysteine
-
1 mM, 65.05% inhibition
L-cysteine
-
strong inhibition at 1 mM
L-cysteine
-
98% inhibition at 1 mM
L-cysteine
-
90% inhibition at 10 mM, 70% at 1 mM
L-cysteine
-
5 mM, 20% loss of activity
Li+
-
5 mM, 22% loss of activity
Li+
10 mM, 51% loss of activity
Li+
activating at 1 mM, inhibitory at 10 mM
Li+
-
1 mM, 19% inhibition
methanol
-
50% inhibition at 37%
methanol
-
50% (v/v), 70% inhibition
methanol
-
completely inhibits enzyme activity
methanol
-
1 h, 20% loss of activity by 20% (v/v), 60% loss of activity by 50% (v/v)
methanol
-
complete inhibition at 50% or above
methanol
52% (v/v) 50% inhibition
methanol
-
25%, 17% inhibition
methanol
-
20% (v/v), 20% loss of activity
Mg2+
-
1 mM, 88% inhibition
Mg2+
-
5 mM, 23% loss of activity
Mg2+
-
10 mM, 8% inhibition
Mg2+
activating at 1 mM, inhibitory at 10 mM
Mg2+
-
84.4% residual activity at 10 mM
Mg2+
-
5 mM, 34% inhibition
Mg2+
-
significantly inhibition
Mg2+
-
10 mM, 66% inhibition
Mg2+
-
100 mM, 33% inhibition
Mg2+
68.8% residual activity at 10 mM
Mg2+
-
10 mM, 38% loss of activity
Mg2+
-
3 mM, 11% inhibition
Mg2+
Sporothrix carnis
-
1 mM, 45% inhibition
Mg2+
-
200 mM, 81.32% residual activity
Mg2+
-
6% inhibition at 5 mM
Mg2+
-
10 mM, 23% loss of activity
Mg2+
-
2.5 mM 9% inhibition
Mn2+
-
5 mM, 21% loss of activity
Mn2+
activating at 1 mM, inhibitory at 10 mM
Mn2+
strongly inhibits at 10 mM
Mn2+
-
1 mM, 91% of inhibition
Mn2+
-
2% residual activity at 10 mM
Mn2+
-
5 mM, 20% inhibition
Mn2+
-
49.1% residual activity at 20 mM
Mn2+
-
inhibits the enzyme activity at 100 mM but increases it at 12.5-50 mM
Mn2+
-
22% inhibition at 1 mM
Mn2+
-
significantly inhibition
Mn2+
-
10 mM, 72% inhibition
Mn2+
-
1 mM, 51% inhibition
Mn2+
-
100 mM, 44% inhibition
Mn2+
82.3% residual activity at 10 mM
Mn2+
-
10 mM, 38% loss of activity
Mn2+
Sporothrix carnis
-
1 mM, 45% inhibition
Mn2+
-
10 mM, about 30% inhibition
Mn2+
-
50 mM, 100% loss of activity
MnCl2
5 mM, 90% loss of activity
MnCl2
-
1 mM, 83% residual activity
Na+
-
10 mM, 11% inhibition
Na+
-
exhibits activation of laccase up to 1 mM beyond which it exhibits inhibition of laccase activity
Na+
-
1.25 mM, 4% inhibition. 10 mM, 20% inhibition
Na+
activating at 1 mM, inhibitory at 10 mM
Na+
-
98% residual activity at 100 mM
Na+
-
1 mM, 4% inhibition
Na+
56.6% residual activity at 10 mM
Na2CO3
-
100 mM, 71% inhibition
NaCl
-
90% inhibition at 0.3 M, completely reversible
NaCl
-
mutant enzyme V159E/N398D
NaCl
10 mM, 20% inhibition. 500 mM, 63% inhibition. 1000 mM, complete loss of activity
NaCl
1000 mM, 24% inhibition
NaCl
-
500 mM, 52-59% inhibition (depending on purification method)
NaCl
-
10 mM, 17% inhibition
NaCl
-
100 mM, 51% inhibition
NaCl
-
80% inhibition at 50 mM
NaCl
-
50% inhibition at 20 mM, the inhibitory effect of chloride ions is reversible
NaCl
-
1 M, 90% inhibition
NaF
-
mutant enzyme V159E/N398D
NaF
-
0.1 mM, 75% inhibition
NaF
-
47% inhibition at 10 mM
NaF
-
complete inhibition at over 10 mM with substrates 3,6-dimethoxyphenol and 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
NaF
-
53% inhibition at 0.1 mM
NaN3
-
1 mM, 60% inhibition
NaN3
1 mM, 35% inhibition
NaN3
-
10 mM, 68% loss of activity
NaN3
complete inhibition at 5 mM
NaN3
-
0.1 mM, complete inhibition
NaN3
competitive, complete inhibition
NaN3
-
1% residual activity at 10 mM
NaN3
-
complete inhibition at 2 mM
NaN3
-
complete inhibition at 0.1 mM
NaN3
-
complete inhibition
NaN3
-
1 mM, 98% inhibition
NaN3
-
1 mM, complete loss of activity
NaN3
-
0.1 mM, complete inhibition
NaN3
8.9% residual activity at 1 mM
NaN3
-
completely inhibited by 50 mM
NaN3
-
7.86% inhibition at 10 mM
NaN3
-
1 mM, complete loss of activity
NaN3
-
22% inhibition at 10 mM, no inhibition by 1 mM NaN3
NaN3
10 mM, residual activity of wild-type enzyme is 23%, residual activity of mutant enzyme M199A is 13%, residual activity of mutant enzyme M199G is 20%, residual activity of mutant enzyme Y230A is 20%, residual activity of mutant enzyme H165A/M199G is 1116%, residual activity of mutant enzyme H165A/R240H is 78%, residual activity of mutant enzyme M199G/R240H is 25%
NaN3
-
1 mM, 5.5% loss of activity
NaN3
MK290990.1
100 mM, 96.28% residual activity
NaN3
-
0.5 mM, 85% inhibition
NaN3
-
complete inhibition at over 80 mM with substrate 3,6-dimethoxyphenol and at over 40 mM with substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
NaN3
competitive inhibition
NaN3
-
complete inhibition at 0.1 mM
NaN3
-
77% inhibition at 0.01 mM
NaN3
-
complete inhibition at 0.1 mM
Ni2+
20 mM, weak inhibitory effect
Ni2+
-
98.4% residual activity at 10 mM
Ni2+
-
5 mM, 25% inhibition
Ni2+
-
62% residual activity at 20 mM
Ni2+
-
32% inhibition at 1 mM
Ni2+
-
10 mM, 68% inhibition
Ni2+
-
1 mM, 57% inhibition
Ni2+
-
100 mM, 52% inhibition
Ni2+
-
3 mM, 33% inhibition
Ni2+
-
5 mM, 35% loss of activity
oxalic acid
-
p-coumaric acid
-
-
p-coumaric acid
5 mM, 60% inhibition
p-coumaric acid
-
1 mM, 25% inhibition
p-coumaric acid
-
1 mM, 48% inhibition
Pb2+
-
10 mM, 9% inhibition
Pb2+
-
97.2% residual activity at 20 mM
Pb2+
-
inhibits 50% at 10 mM
Pb2+
-
10 mM, 56% loss of activity
phenylmercuric acetate
-
-
phenylmercuric acetate
-
-
phenylmercuric acetate
-
-
potassium cyanide
-
90% at 1 mM
potassium cyanide
-
50% at 0.6 mM
potassium cyanide
-
87% at 0.1 mM
potassium cyanide
-
66-73% at 0.1 mM
SDS
-
SDS
-
mutant enzyme V159E/N398D
SDS
-
0.05 mM, 41% loss of activity
SDS
-
1 mM, 38.6% loss of activity
SDS
-
1 mM, 37-41% inhibition (depending on purification method)
SDS
0.1 mM, activity is reduced to 11.4%
SDS
-
5 mM, 46% inhibition
SDS
competitive, complete inhibition
SDS
-
93.8% residual activity at 20 mM
SDS
-
1.6fold activation at 1 mM, 89% inhibition at 10 mM
SDS
-
1 mM, 19% inhibition
SDS
-
10 mM, 89% inhibition
SDS
-
1 mM, 43% inhibition
SDS
-
10 mM, 21% inhibition
SDS
-
complete inhibition at 140 mM
SDS
-
3 mM, 85% inhibition
SDS
-
completely inhibited by 32 mM
SDS
-
10.2% inhibition at 10 mM
SDS
Sporothrix carnis
-
1 mM, 27% inhibition
SDS
-
1 mM, 20% loss of activity
SDS
MK290990.1
100 mM, 69.93% residual activity
SDS
-
10 mM, 15% inhibition
SDS
-
1 mM, 83.33% inhibition
SDS
-
40% inhibition at 10 mM, 10% at 1 mM
SDS
-
0.5%, 60% loss of activity
Sodium azide
-
Sodium azide
-
1 mM, 98% inhibition
Sodium azide
-
50% inhibition at 0.009 mM
Sodium azide
-
0.05 mM, 50% loss of activity
Sodium azide
-
completely inhibits enzyme activity
Sodium azide
0.1 mM, activity is reduced to 9.2%
Sodium azide
0.05 M, complete inhibition
Sodium azide
-
0.1 mM, complete inhibition
Sodium azide
strong inhibition
Sodium azide
-
1 mM, 12% inhibition
Sodium azide
1 mM, 33.8% loss of activity
Sodium azide
-
complete inhibition of laccase activity at 0.1% concentration
Sodium azide
-
0.1 mM, 97% inhibition
Sodium azide
-
0.5 mM, 94% inhibition
Sodium azide
-
30% inhibition
Sodium azide
Sporothrix carnis
-
1 mM, 27% inhibition
Sodium azide
-
5 mM, 40% inhibition
Sodium azide
-
1 mM, 68% residual activity
Sodium azide
Thermochaetoides thermophila
-
0.05 mM, 84% inhibition
Sodium azide
-
1 mM, 91.4% inhibition
Sodium azide
-
strong inhibition at 0.1 mM
Sodium azide
0.1 mM, strong
Sodium cyanide
-
1 mM, 0% residual activity
Sodium cyanide
-
1 mM, 81.18% inhibition
sodium dodecylsulfate
-
sodium dodecylsulfate
-
50% inhibition at 1 mM
sodium dodecylsulfate
-
50% inhibition at 1%
sodium dodecylsulfate
-
20-70% inhibition at 8 mM
sodium thiosulfate
-
sodium thiosulfate
1 mM, 98% inhibition
thioglycolic acid
-
1 mM, 82% inhibition
thioglycolic acid
-
50% inhibition at 0.5 mM
thioglycolic acid
-
2.5 mM, 50% loss of activity
thioglycolic acid
-
mixed competitive inhibition after a lag-phase
thioglycolic acid
strong inhibition
thioglycolic acid
-
93% inhibition at 0.1 mM, complete inhibition at 1 mM
thioglycolic acid
-
85% inhibition at 1 mM
thioglycolic acid
Thermochaetoides thermophila
-
0.1 mM, 91% inhibition
thioglycolic acid
-
inhibits 92.4% at 750 mM
thioglycolic acid
-
1 mM, 100% inhibition
Thiourea
-
1 mM, 60% inhibition
Thiourea
-
1 mM, complete inhibition
Thiourea
1 mM, 4.5% loss of activity. 10 mM, 90.4% loss of activity
Thiourea
-
73% inhibition at 5 mM
Thiourea
Thermochaetoides thermophila
-
-
tropolone
-
1 mM, 78% inhibition
tropolone
9.7% residual activity at 1 mM
Urea
-
Urea
Sporothrix carnis
-
1 mM, 21% inhibition
Urea
-
0.4 mM, complete inhibition
Urea
inactivation at 5 M, 50% inhibition at about 2 M
Zn2+
-
10 mM, 6% inhibition
Zn2+
partially inhibits laccase activity
Zn2+
-
10 mM, 13% inhibition
Zn2+
activating at 1 mM, inhibitory at 10 mM
Zn2+
strongly inhibits at 10 mM
Zn2+
-
75.6% residual activity at 10 mM
Zn2+
-
1 mM, reduces LacG activity to 48%
Zn2+
-
22% inhibition at 100 mM
Zn2+
-
10 mM, 88% inhibition
Zn2+
-
50% inhibition at 50 mM
Zn2+
65.7% residual activity at 1 mM
Zn2+
-
inhibits 40% at 10 mM
Zn2+
-
3 mM, 66% inhibition
Zn2+
-
10 mM, about 30% inhibition
Zn2+
-
200 mM, 85.8% residual activity
Zn2+
-
19% inhibition at 5 mM
Zn2+
-
50 mM, 97% loss of activity
ZnSO4
-
10 mM, 0.5% inhibition
ZnSO4
MK290990.1
1 mM, 30 min, 84.52% residual activity
additional information
Mn2+ even at 20 mM does not affect Atm activity
-
additional information
no inhibition: EDTA (10-50 mM), SDS (0.1-1 mM)
-
additional information
-
no inhibition: EDTA (10-50 mM), SDS (0.1-1 mM)
-
additional information
-
the enzyme can tolerate up to 600-800 mM NaCl. NaN3 (1 mM) has almost no effect on the laccase activity
-
additional information
no significant loss of activity loss at 10 mM EDTA
-
additional information
except for copper ions, most metal ions inhibit the laccase activity at a high concentration of about 10 mM, EDTA has no inhibitory effect on the laccase activity
-
additional information
-
except for copper ions, most metal ions inhibit the laccase activity at a high concentration of about 10 mM, EDTA has no inhibitory effect on the laccase activity
-
additional information
isoenzyme Lac4 is resistant to SDS, and retains 43.08% activity in the presence of 100 mM SDS; isoenzymes Lac3 is resistant to SDS, and retains 31.86% activity in the presence of 100 mM SDS
-
additional information
isoenzyme Lac4 is resistant to SDS, and retains 43.08% activity in the presence of 100 mM SDS; isoenzymes Lac3 is resistant to SDS, and retains 31.86% activity in the presence of 100 mM SDS
-
additional information
-
isoenzyme Lac4 is resistant to SDS, and retains 43.08% activity in the presence of 100 mM SDS; isoenzymes Lac3 is resistant to SDS, and retains 31.86% activity in the presence of 100 mM SDS
-
additional information
-
5 mM potassium cyanide shows no inhibitory effect on the laccase
-
additional information
no inhibition by EDTA
-
additional information
-
not inhibitory: EDTA. L-cysteine
-
additional information
-
no inhibition by 0.1 mM EDTA, laccase retains 100 % activity with 2,6-dimethoxyphenol as a substrate in the presence of clorgiline or pargyline (specific amine oxidase inhibitors)
-
additional information
the recombinant His-tagged MmPPOA-695 shows a strong resistance to NaCl, DMSO, and Tween-80
-
additional information
-
the recombinant His-tagged MmPPOA-695 shows a strong resistance to NaCl, DMSO, and Tween-80
-
additional information
FJ560721
poor inhibition by NaF and NaBr
-
additional information
-
no inhibition by iodoacetate and chloroacetamide
-
additional information
-
no inhibition by iodoacetate and chloroacetamide
-
additional information
-
no inhibition: SDS, NaBr
-
additional information
-
EDTA and DMSO have almost no inhibitory effect
-
additional information
-
no inhibition by EDTA at 1-10 mM
-
additional information
the enzyme is resistant to specific inhibitors of copper-containing oxidases, such as NaN3 and NaF
-
additional information
-
the enzyme is resistant to specific inhibitors of copper-containing oxidases, such as NaN3 and NaF
-
additional information
-
no inhibition by iodoacetate and chloroacetamide
-
additional information
Thermochaetoides thermophila
-
strongly inhibited by Cu-chelating agents
-
additional information
-
SDS and EDTA did not inhibit enzyme activity
-
additional information
-
no inhibition by DMSO up to 25 mM
-
additional information
-
study on inhibitors and inhibition
-
additional information
-
no or poor inhibition by Co2+, Zn2+, Sn2+, Mn2+, Mg2+, K+, Fe2+, Ba2+, and Na+
-
additional information
-
soluble laccase shows more than 80% relative activity in organic solvents like ethanol, methanol, toluene and acetonitrile
-
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34.1 - 47.7
1-hydroxybenzotriazole
0.008 - 2.027
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
0.0107 - 0.017
2,2'-azino-bis(3-ethylbenzathiazoline-6-sulfonate)
0.0065 - 0.27
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate)
0.0013 - 22.4
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
0.1049
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate)
Myrioconium sp.
-
25°C, pH 4
0.0023 - 7.611
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
0.00732 - 6.86
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
0.4
2,2'-azino-di(3-ethyl-benzthiazoline-6-sulfonate)
-
-
0.9 - 4.4
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate)
0.19
2,2'-azinobis(3-ethylbenz-thiazoline-6-sulfonic acid)
Thermochaetoides thermophila
-
pH 6.0, 50°C
0.00134 - 48.6
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
0.022 - 12
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
1.163 - 1.84
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)
0.0095
2,2,6,6-tetramethyl-piperidine-1-oxyl radical
-
pH 5.0, 25°C, recombinant enzyme
0.67
2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)
45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02
0.011 - 45
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
0.29
2,3-Dihydroxybenzoic acid
pH 5, 30°C
4.2 - 14
2,5-diaminotoluene
-
0.0161
2,5-xylidine
-
pH 7.0, 40°C
0.00086 - 64.4
2,6-dimethoxyphenol
1.374 - 7.131
2,6-dimethylphenol
0.015 - 0.044
2-dianisidine
0.66
3,4-dihydroxy L-phenylalanine
in McIlvaine buffer (pH 4.0), at 30°C
0.43
3,4-dihydroxybenzoic acid
pH 5, 30°C
0.0004 - 0.0315
3-(4-dimethylamino-1-phenylazo) benzene sulfonic acid sodium salt
6.9
3-dimethylaminobenzoic acid
-
pH 6.0, 25°C
0.69
3-hydroxyanthranilic acid
pH 5, 30°C
0.0024 - 0.092
4-hydroxy-3,5-dimethoxybenzaldehyde azine
1.41 - 1.96
4-hydroxybenzoic acid
0.223
4-hydroxyindole
-
pH 7.0, 30°C
1.56
4-methyl catechol
-
isoenzyme lac90
0.175
4-methyl-catechol
-
-
0.1 - 1.72
4-phenylenediamine
0.062 - 0.338
acetaminophen
0.284
anthraquinonic dye Acid Blue 62
pH 5.5, 65°C
1.22
beta-(3,4-dihydroxyphenyl)alanine
-
30°C, pH 4.0
0.236
bilirubin
45°C, pH 8.4, LccA protein isolated from Haloferax volcanii H26 strain US02
0.03
coniferaldehyde
-
isoenzyme lac90
0.002
coniferyl alcohol
-
isoenzyme lac90
0.0168
Diamond Black PV 200
-
25°C, pH 4.5
0.04
enterobactin
pH 5, 30°C
0.092 - 0.45
ferrocenemonocarboxylic acid
-
0.0514 - 0.13
gallic acid
0.001 - 11.33
hydroquinone
0.036
hydroxyquinone
Thermochaetoides thermophila
-
pH 6.0, 50°C
0.056
K4Fe(CN)6
-
pH 3, holoCotA
0.1
L-3,4-dihydroxyphenylalanine
Thermochaetoides thermophila
-
pH 6.0, 50°C
0.0518
L-tyrosine
-
pH 7.0, 40°C
0.038
methyl syringate
-
pH 5.5, 20°C
0.212 - 1.7
N,N-dimethyl-1,4-phenylenediamine
2.3 - 3.8
N,N-dimethyl-4-phenylenediamine
0.29 - 3.9
N,N-Dimethyl-p-phenylenediamine
0.42
N,N-dimethyl-p-phenylenediamine sulfate
-
pH 6.5, 40°C
0.43 - 0.63
N-acetyldopamine
0.47 - 1.9
N-beta-alanyldopamine
2.3
N-hydroxyacetanilide
-
pH 5.5, 20°C
3.65
o-benzenediol
-
pH 7.0, 25°C
0.045 - 0.647
o-Dianisidine
41
o-phenylenediamine
-
-
0.02
p-coumaryl alcohol
-
isoenzyme lac90
0.33
p-methoxy-phenol
-
-
2.21 - 375
p-phenylenediamine
0.013 - 0.11
Sinapic acid
0.007
sinapinic acid
Coriolisimus fulvocinerea
-
-
0.0018 - 39
syringaldazine
0.131
syringaldehyde
-
pH 5.0, 22°C
0.026 - 0.28
syringic acid
0.0251
Tannic acid
-
pH 7.0, 40°C
0.06 - 2.92
vanillic acid
3.9
Vanillin
Coriolisimus fulvocinerea
-
-
58
violuric acid
-
pH 5.5, 20°C
additional information
additional information
-
34.1
1-hydroxybenzotriazole
pH 5.0, temperature not specified in the publication
47.7
1-hydroxybenzotriazole
pH 5.0, temperature not specified in the publication, wild-type PM1 laccase
5.6
1-naphthol
pH and temperature not specified in the publication, wild-type enzyme
6.04
1-naphthol
pH and temperature not specified in the publication, mutant enzyme V281A/P309L/S318G/D232V
0.008
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 2.5, 65°C
0.07
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 3.0, 22°C, recombinant wild-type enzyme
0.07
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.8, 25°C
0.086
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C, recombinant wild-type enzyme
0.102
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 22°C, deglycosylated enzyme
0.106
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 22°C, native enzyme
0.11
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 3.0, 22°C, recombinant truncated mutant POXA1bDELTA16
0.11
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 3.0, 22°C, recombinant truncated mutant POXA1bDELTA4
0.112
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C, recombinant mutant WlacS
0.124
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C, wild-type CotA
0.129
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C, recombinant mutant WlacD
0.145
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C, mutant L386A
0.18
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.5, 35°C
0.26
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 22°C, recombinant enzyme expressed in Saccharomyces cerevisiae
0.28
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 25°C, recombinant enzyme expressed in Trichoderma reesei
0.29
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
-
0.32
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 3.0, 22°C, recombinant truncated mutant POXA1bD205R
0.4
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 25°C, recombinant wild-type enzyme
0.9
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae
2.027
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C, mutant I494A
0.0107
2,2'-azino-bis(3-ethylbenzathiazoline-6-sulfonate)
-
pH 3.0, 25°C, laccase Lac-3.5
0.017
2,2'-azino-bis(3-ethylbenzathiazoline-6-sulfonate)
-
pH 3.0, 25°C,laccase Lac-4.8
0.0065
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate)
-
pH 4.0
0.27
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate)
-
-
0.0013
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, temperature not specified in the publication
0.002
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, temperature not specified in the publication, wild-type PM1 laccase
0.0045
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3, temperature not specified in the publication, mutant enzyme V159E
0.0046
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3, temperature not specified in the publication, mutant enzyme V159E/N398D
0.00866
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 25°C
0.02
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, temperature not specified in the publication
0.0237
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
22°C, pH 5.0
0.024
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH not specified in the publication
0.0509
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 30°C
0.0595
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C
0.075
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 3.5, mutant enzyme H165A/R240H
0.075
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme H165A/R240H, 30°C, pH not specified in the publication
0.076
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH and temperature not specified in the publication, mutant enzyme V281A/P309L/S318G/D232V
0.09
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 3.5, mutant enzyme H165A/M199G
0.09
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme H165A/M199G, 30°C, pH not specified in the publication
0.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH not specified in the publication
0.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 3.5, mutant enzyme M199G/R240H
0.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme M199G/R240H, 30°C, pH not specified in the publication
0.17
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 3.5, mutant enzyme Y230A
0.17
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme Y230A, 30°C, pH not specified in the publication
0.2
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 4.0, mutant enzyme M199G
0.2
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme M199G, 30°C, pH not specified in the publication
0.21
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH and temperature not specified in the publication, wild-type enzyme
0.32
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 4.0, mutant enzyme M199A
0.32
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme M199A, 30°C, pH not specified in the publication
0.36
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild-type enzyme, 30°C, pH not specified in the publication
0.36
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 4.0, wild-type enzyme
0.394
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 5.0, 30°C, soluble enzyme
0.62
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
25°C, pH 5.6
0.747
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 5.0, 30°C, surface display laccase (SDL) biocatalyst (where the enzyme laccase is displayed on the surface of biological cells through synthetic biology)
0.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 30°C
2.12
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 40°C
3.99
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
70°C, pH 3.0
11.99
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 2.5, 55°C
20.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C
22.4
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 30°C
0.0023
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
in 67 mM sodium acetate buffer (pH 4.5), at 30°C
0.0033
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 50°C
0.014
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, recombinant Lac1
0.02
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
in McIlvaine buffer (pH 4.0), at 30°C
0.028
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
recombinant wild-type enzyme, pH 3.0, temperature not specified in the publication
0.034
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, recombinant Lac1
0.035
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
recombinant wild-type enzyme, pH 5.0, temperature not specified in the publication
0.036
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
FJ560721
pH 5.0, 22-25°C
0.041
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 5.0, 25°C
0.045
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 5.0, 25°C
0.0552
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 6.0, 25°C
0.058
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 25°C, mutant K532A
0.07
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
isoform POXA3a, pH 3.6, 25°C
0.074
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
isoform POXA3b, pH 3.6, 25°C
0.0794
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
0.08
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 4.0, 22°C, recombinant enzyme
0.084
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 25°C, mutant K532E
0.086
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 30°C
0.09
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
isoform POXA1w, pH 3.0, 25°C
0.104
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
recombinant enzyme, pH 3.0, 30°C
0.105
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 25°C, mutant P530A
0.12
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
isoform POXA2, pH 3.0, 25°C
0.13
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
0.15
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, temperature not specified in the publication
0.19
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 3.0, 50°C
0.203
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
in 100 mM citrate buffer, pH 4.5, at 37°C
0.28
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
0.28
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
isoform POXC, pH 3.0, 25°C
0.307
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 3.2, 37°C
0.37
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
isoform POXA1b, pH 3.0, 25°C
0.535
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
at 22°C, pH not specified in the publication
0.653
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 25°C, mutant K532A
0.7
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
40°C, pH 4.5
0.8158
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 2.5, 25°C
1.219
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 25°C, mutant P530A
1.278
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 25°C, mutant K532E
2.174
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 6.5, 25°C, mutant K532A
2.487
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 6.5, 25°C, mutant K532E
3.703
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 6.5, 25°C, mutant P530A
4.317
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, recombinant Lac1
7.611
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, recombinant Lac1
0.00732
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 4.0, 25°C
0.01
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH and temperature not specified in the publication
0.027
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 3.4, 70°C
0.0316
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
Sporothrix carnis
-
pH 7.5, 30°C
0.036
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
0.042
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH and temperature not specified in the publication
0.046
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 5.0, 25°C, recombinant enzyme
0.0934
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH and temperature not specified in the publication
0.11
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
21-23°C, pH not specified in the publication, wild-type enzyme
0.1107
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188R, in aqueous solution
0.1151
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188I, in aqueous solution
0.129
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188L, in aqueous solution
0.1327
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 22°C
0.1329
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 5.0, 30°C
0.1329
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188V, in aqueous solution
0.136
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, isoenzyme Lac3
0.1419
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, wild-type enzyme, in aqueous solution
0.149
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 37°C
0.1511
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188K, in aqueous solution
0.1714
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188A, in aqueous solution
0.205
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, isoenzyme Lac4
0.21
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 7.4, 37°C
0.2308
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 4.5
0.25
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4, 30°C
0.28
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 3.0, 30°C
0.303
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 3.0, 25°C
0.358
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
45°C, pH 5.0
0.366
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
0.43
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 55°C
0.5
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 6, 25°C, soluble enzyme
1.17
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I (variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions)
1.26
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
laccase DcLac2, pH 2.8, temperature not specified in the publication
1.4
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 8.0, 85°C
2
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 6, 25°C,laccase immobilized in solgel matrix
2.06
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I/V482G 2.06 (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)
3.9
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
laccase DcLac1, pH 2.8, temperature not specified in the publication
4.5
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, temperature not specified in the publication
5.33
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 4.0, 35°C
6.86
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 7.0 37°C
0.9
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate)
pH and temperature not specified in the publication
2.4
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate)
60°C, pH 6.0
3.8
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate)
55°C, pH 6.0
4.4
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate)
50°C, pH 6.0
0.00134
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 50°C, free enzyme
0.004
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
0.005
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 50°C, enzyme conjugated with 1.1 kDa PEG
0.00632
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 50°C, enzyme conjugated with 2 kDa PEG
0.00704
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 50°C, enzyme conjugated with 5 kDa PEG
0.01
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant mutant D206A
0.0113
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5
0.0123
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C
0.0128
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.0, 50°C
0.016
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant mutant D206N
0.025
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 4.5, 25°C
0.026
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant mutant D206E
0.03
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
isoenzyme lac90
0.03
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.0, 45°C
0.038
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 25°C
0.038
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 5.0, 22°C
0.041
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 4.5, 65°C
0.0423
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
free enzyme
0.045
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 5.5, 20°C
0.0452
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 505 kDa
0.049
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 7.6, 37°C, mutant M502F
0.0498
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 214 kDa
0.05
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant wild-type enzyme
0.058
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.2, 50°C
0.063
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 5.5
0.07
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
25°C, isozyme POXA3a
0.074
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
25°C, isozyme POXA3b
0.077
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.0, 25°C
0.0852
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 432 kDa
0.087
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 7.6, 37°C, wild-type enzyme
0.089
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 7.6, 37°C, mutant M502L
0.095
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 131 kDa
0.1
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 4.5, 37°C
0.11
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
0.11
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 7.0, 25°C
0.127
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
30°C, pH 3.0
0.177
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5
0.21
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
0.21
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 40°C
0.27
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5
0.41
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
Phlebia fascicularia
-
Lac II, 70°C, pH 2.2
0.42
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
Phlebia fascicularia
-
Lac I, 70°C, pH 2.2
0.652
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 7.0, 30°C
48.6
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.2, 45°C
0.022
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
pH 7.0, 25°C
0.124
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
-
pH 3, holoCotA
0.31
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant M455L, 30°C, pH 5
1.3
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant D439A/M510L, pH 5.5, temperature not specified in the publication
1.4
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant P444A/M510Q, pH 5.5, temperature not specified in the publication
1.58
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
wild-type, presence of 0.5 mM Cu2+, 30°C, pH 5
1.88
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant G304K, pH 5.5, 25°C
2.33
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant M456A, presence of 0.5 mM Cu2+, 30°C, pH 5
2.5
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
pH 5, 30°C
2.94
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
wild-type, 30°C, pH 5
3.79
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
wild-type, pH 5.5, 25°C
6.4
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
wild-type, presence of 1 mM Cu2+, pH 5.5, 25°C
6.5
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
wild-type, pH 5.5, 25°C
11
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
region Pro357-His406 deletion mutant, presence of 1 mM Cu2+, pH 5.5, 25°C
12
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
region Pro357-His406 deletion mutant, pH 5.5, 25°C
1.163
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)
recombinant His-tagged enzyme MmPPOA-695, pH 5.0, 25°C
1.263
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)
recombinant wild-type enzyme MmPPOA-695, pH 5.0, 25°C
1.84
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)
native wild-type enzyme, pH 5.0, 25°C
0.011
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
22°C, pH 5.0
0.0392
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 6.0, 40°C
0.04
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 7.5, 37°C
0.0536
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
25°C, pH 4.5
0.722
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, C-6His tagged laccase 3
0.835
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, deglycosylated enzyme
0.964
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA))
1.237
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)) and 6His tagged (C(DELTA)6H)
1.268
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)), 6His tagged (C(DELTA)6H) and hyper-glycosylated
2.042
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, wild-type enzyme
12
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 23°C
45
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 23°C
4.2
2,5-diaminotoluene
mutant M510L, pH 5.5, temperature not specified in the publication
-
5.5
2,5-diaminotoluene
mutant D439A/M510L, pH 5.5, temperature not specified in the publication
-
6.7
2,5-diaminotoluene
mutant D439A/P444A, pH 5.5, temperature not specified in the publication
-
9.3
2,5-diaminotoluene
mutant P444A, pH 5.5, temperature not specified in the publication
-
12
2,5-diaminotoluene
mutant D439A, pH 5.5, temperature not specified in the publication
-
12
2,5-diaminotoluene
wild-type, pH 5.5, temperature not specified in the publication
-
14
2,5-diaminotoluene
mutant P444A/M510Q, pH 5.5, temperature not specified in the publication
-
0.00086
2,6-dimethoxyphenol
Phlebia fascicularia
-
Lac II, 70°C, pH 3.0
0.00118
2,6-dimethoxyphenol
Phlebia fascicularia
-
Lac I, 70°C, pH 3.0
0.0052
2,6-dimethoxyphenol
-
pH 6.0
0.0082
2,6-dimethoxyphenol
-
pH 8.0, 40°C
0.0086
2,6-dimethoxyphenol
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
0.01
2,6-dimethoxyphenol
pH 5.0, temperature not specified in the publication, wild-type PM1 laccase
0.011
2,6-dimethoxyphenol
pH 4.5, 25°C, recombinant wild-type enzyme
0.012
2,6-dimethoxyphenol
-
pH 7.0, 30°C
0.016
2,6-dimethoxyphenol
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae
0.016
2,6-dimethoxyphenol
-
pH 5, temperature not specified in the publication, mutant enzyme V159E
0.02
2,6-dimethoxyphenol
30°C, pH not specified in the publication
0.0243
2,6-dimethoxyphenol
-
22°C, pH 5.0
0.0255
2,6-dimethoxyphenol
pH 4.5, 25°C
0.026
2,6-dimethoxyphenol
-
pH 4.5, 25°C
0.026
2,6-dimethoxyphenol
FJ560721
pH 5.0, 22-25°C
0.027
2,6-dimethoxyphenol
recombinant wild-type enzyme, pH 5.0, temperature not specified in the publication
0.032
2,6-dimethoxyphenol
wild-type enzyme, 30°C, pH not specified in the publication
0.035
2,6-dimethoxyphenol
-
pH 7.6, 37°C, mutant M502F
0.0351
2,6-dimethoxyphenol
pH 5.0, 30°C
0.038
2,6-dimethoxyphenol
-
-
0.048
2,6-dimethoxyphenol
-
pH 5.0, 22°C
0.05
2,6-dimethoxyphenol
pH 5.0, temperature not specified in the publication
0.053
2,6-dimethoxyphenol
-
at 22°C, pH not specified in the publication
0.0567
2,6-dimethoxyphenol
-
pH 7.0
0.06
2,6-dimethoxyphenol
-
pH 7.6, 37°C, wild-type enzyme
0.0678
2,6-dimethoxyphenol
Myrioconium sp.
-
25°C, pH 6
0.07
2,6-dimethoxyphenol
in McIlvaine buffer (pH 4.0), at 30°C
0.08
2,6-dimethoxyphenol
-
-
0.08
2,6-dimethoxyphenol
-
pH 4.5, 37°C
0.08
2,6-dimethoxyphenol
-
pH 5, temperature not specified in the publication, mutant enzyme V159E/N398D
0.084
2,6-dimethoxyphenol
-
pH 3.0, 25°C, laccase Lac-4.8
0.088
2,6-dimethoxyphenol
-
pH 3.0, 25°C, laccase Lac-3.5
0.09
2,6-dimethoxyphenol
-
-
0.096
2,6-dimethoxyphenol
Thermochaetoides thermophila
-
pH 6.0, 50°C
0.1
2,6-dimethoxyphenol
30°C, pH not specified in the publication
0.11
2,6-dimethoxyphenol
-
pH 4.5
0.14
2,6-dimethoxyphenol
pH 3.4, 30°C, recombinant mutant D206A
0.145
2,6-dimethoxyphenol
-
pH 7.6, 37°C, mutant M502L
0.15
2,6-dimethoxyphenol
30°C, pH 9.0, mutant enzyme H165A/R240H
0.15
2,6-dimethoxyphenol
mutant enzyme H165A/R240H, 30°C, pH not specified in the publication
0.16
2,6-dimethoxyphenol
-
pH and temperature not specified in the publication
0.172
2,6-dimethoxyphenol
recombinant wild-type enzyme MmPPOA-695, pH 5.0, 25°C
0.19
2,6-dimethoxyphenol
pH 3.4, 30°C, recombinant wild-type enzyme
0.2
2,6-dimethoxyphenol
-
pH 4.8, 25°C
0.2
2,6-dimethoxyphenol
pH and temperature not specified in the publication
0.203
2,6-dimethoxyphenol
-
pH 4.0, 25°C
0.216
2,6-dimethoxyphenol
-
pH 7, holoCotA
0.227
2,6-dimethoxyphenol
-
pH 7.0, 25°C, wild-type CotA
0.23
2,6-dimethoxyphenol
-
isoform POXC, pH 3.0-5.0, 25°C
0.25
2,6-dimethoxyphenol
30°C, pH 8.5, mutant enzyme M199G/R240H
0.25
2,6-dimethoxyphenol
mutant enzyme M199G/R240H, 30°C, pH not specified in the publication
0.26
2,6-dimethoxyphenol
-
isoform POXA1b, pH 4.0-5.0, 25°C
0.266
2,6-dimethoxyphenol
pH 4.0, 65°C
0.277
2,6-dimethoxyphenol
recombinant enzyme, pH 3.0, 30°C
0.28
2,6-dimethoxyphenol
30°C, pH 6.5, mutant enzyme H165A/M199G
0.28
2,6-dimethoxyphenol
mutant enzyme H165A/M199G, 30°C, pH not specified in the publication
0.293
2,6-dimethoxyphenol
recombinant His-tagged enzyme MmPPOA-695, pH 5.0, 25°C
0.302
2,6-dimethoxyphenol
-
pH 4.0, 25°C
0.32
2,6-dimethoxyphenol
30°C, pH 9.0, wild-type enzyme
0.324
2,6-dimethoxyphenol
recombinant wild-type enzyme, pH 3.0, temperature not specified in the publication
0.351
2,6-dimethoxyphenol
-
30°C, pH 3.0
0.37
2,6-dimethoxyphenol
-
pH 4.0, 50°C
0.38
2,6-dimethoxyphenol
pH 8.5, temperature not specified in the publication
0.393
2,6-dimethoxyphenol
pH 3.0, 50°C
0.41
2,6-dimethoxyphenol
21-23°C, pH not specified in the publication, wild-type enzyme
0.426
2,6-dimethoxyphenol
-
-
0.43
2,6-dimethoxyphenol
-
pH 7.0, 25°C
0.43
2,6-dimethoxyphenol
pH 5.3, 22°C, recombinant truncated mutant POXA1bDELTA16
0.43
2,6-dimethoxyphenol
pH 5.3, 22°C, recombinant truncated mutant POXA1bDELTA4
0.44
2,6-dimethoxyphenol
-
pH 4.5, 37°C
0.448
2,6-dimethoxyphenol
pH 3.0, 30°C
0.48
2,6-dimethoxyphenol
Loweporus lividus MTCC-1178
-
-
0.48
2,6-dimethoxyphenol
Loweporus lividus
-
in 50 mM sodium malonate buffer, pH 4.5 at 37°C
0.5
2,6-dimethoxyphenol
pH and temperature not specified in the publication
0.503
2,6-dimethoxyphenol
-
pH 5.0, temperature not specified in the publication
0.56
2,6-dimethoxyphenol
pH and temperature not specified in the publication, mutant enzyme V281A/P309L/S318G/D232V
0.57
2,6-dimethoxyphenol
-
pH 4.6, 45°C
0.57
2,6-dimethoxyphenol
pH 5.3, 22°C, recombinant wild-type enzyme
0.576
2,6-dimethoxyphenol
-
pH 7.0, 25°C, mutant L386A
0.602
2,6-dimethoxyphenol
-
pH and temperature not specified in the publication
0.654
2,6-dimethoxyphenol
pH and temperature not specified in the publication, wild-type enzyme
0.67
2,6-dimethoxyphenol
30°C, pH 8.0, mutant enzyme M199G
0.67
2,6-dimethoxyphenol
mutant enzyme M199G, 30°C, pH not specified in the publication
0.68
2,6-dimethoxyphenol
-
pH 7.0, 22°C, recombinant enzyme
0.74
2,6-dimethoxyphenol
-
isoform POXA2, pH 6.5, 25°C
0.76
2,6-dimethoxyphenol
30°C, pH 8.5, mutant enzyme Y230A
0.76
2,6-dimethoxyphenol
mutant enzyme Y230A, 30°C, pH not specified in the publication
0.83
2,6-dimethoxyphenol
30°C, pH 8.0, mutant enzyme M199A
0.83
2,6-dimethoxyphenol
mutant enzyme M199A, 30°C, pH not specified in the publication
0.84
2,6-dimethoxyphenol
-
pH 8.0, 85°C
1.026
2,6-dimethoxyphenol
-
pH 5.5
1.176
2,6-dimethoxyphenol
-
in 100 mM citrate buffer, pH 4.5, at 37°C
1.24
2,6-dimethoxyphenol
-
pH 8.0, 70°C
1.26
2,6-dimethoxyphenol
pH 5.3, 22°C, recombinant truncated mutant POXA1bD205R
1.295
2,6-dimethoxyphenol
-
pH 9.0, 25°C, mutant I494A
1.413
2,6-dimethoxyphenol
recombinant mutant enzyme MmPPOA-637, pH 5.0, 25°C
1.5 - 2
2,6-dimethoxyphenol
pH 3.0, 37°C
1.63
2,6-dimethoxyphenol
pH 3.4, 30°C, recombinant mutant D206N
1.67
2,6-dimethoxyphenol
-
pH 7.4, 37°C
1.8
2,6-dimethoxyphenol
region Pro357-His406 deletion mutant, presence of 1 mM Cu2+, pH 5.5, 25°C
1.83
2,6-dimethoxyphenol
21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I/V482G (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)
1.98
2,6-dimethoxyphenol
native wild-type enzyme, pH 5.0, 25°C
2.095
2,6-dimethoxyphenol
pH 4, 30°C
2.1
2,6-dimethoxyphenol
-
isoform POXA1w, pH 3.0-5.0, 25°C
2.12
2,6-dimethoxyphenol
pH 5, 30°C
2.16
2,6-dimethoxyphenol
21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I (variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions)
2.5
2,6-dimethoxyphenol
wild-type, presence of 1 mM Cu2+, pH 5.5, 25°C
3.28
2,6-dimethoxyphenol
pH 3.4, 30°C, recombinant mutant D206E
3.295
2,6-dimethoxyphenol
recombinant His-tagged mutant enzyme MmPPOA-637, pH 5.0, 25°C
3.53
2,6-dimethoxyphenol
-
70°C, pH 6.5
5.1
2,6-dimethoxyphenol
25°C, pH 5.6
6.82
2,6-dimethoxyphenol
pH 6.5, 30°C
7.3
2,6-dimethoxyphenol
-
-
8.01
2,6-dimethoxyphenol
pH 5.0, 30°C
8.8
2,6-dimethoxyphenol
-
25°C, isozyme POXA3b
8.8
2,6-dimethoxyphenol
-
isoform POXA3b, pH 5.5, 25°C
10
2,6-dimethoxyphenol
pH 3.0, 23°C
14
2,6-dimethoxyphenol
-
25°C, isozyme POXA3a
14
2,6-dimethoxyphenol
-
isoform POXA3a, pH 5.5, 25°C
47
2,6-dimethoxyphenol
pH 3.0, 23°C
56
2,6-dimethoxyphenol
pH 5.2, 45°C
64.4
2,6-dimethoxyphenol
pH 3.0, 30°C
1.374
2,6-dimethylphenol
pH 4.5, 40°C, isoenzyme Lac3
7.131
2,6-dimethylphenol
pH 4.5, 40°C, isoenzyme Lac4
0.015
2-dianisidine
pH 4.5, 22°C, deglycosylated enzyme
0.0172
2-dianisidine
-
pH 6.0, 25°C
0.044
2-dianisidine
pH 4.5, 22°C, native enzyme
0.0004
3-(4-dimethylamino-1-phenylazo) benzene sulfonic acid sodium salt
-
soluble enzyme in presence of 1-hydroxybenzotriazole
0.0007
3-(4-dimethylamino-1-phenylazo) benzene sulfonic acid sodium salt
-
immobilized enzyme in presence of 1-hydroxybenzotriazole
0.0082
3-(4-dimethylamino-1-phenylazo) benzene sulfonic acid sodium salt
-
soluble enzyme
0.0315
3-(4-dimethylamino-1-phenylazo) benzene sulfonic acid sodium salt
-
immobilized enzyme
0.0024
4-hydroxy-3,5-dimethoxybenzaldehyde azine
-
pH 5.0, 25°C
0.034
4-hydroxy-3,5-dimethoxybenzaldehyde azine
pH 5.0, 25°C
0.066
4-hydroxy-3,5-dimethoxybenzaldehyde azine
-
pH 5.0, 25°C
0.069
4-hydroxy-3,5-dimethoxybenzaldehyde azine
pH 5.0, 25°C
0.092
4-hydroxy-3,5-dimethoxybenzaldehyde azine
-
pH and temperature not specified in the publication
1.41
4-hydroxybenzoic acid
pH 5.0, temperature not specified in the publication
1.96
4-hydroxybenzoic acid
pH 5.0, temperature not specified in the publication, wild-type PM1 laccase
1
4-methylcatechol
-
-
0.1
4-phenylenediamine
-
-
0.27
4-phenylenediamine
in McIlvaine buffer (pH 5.0), at 30°C
1.72
4-phenylenediamine
-
30°C, pH 4.0
0.062
acetaminophen
-
pH 5.0, 30°C, surface display laccase (SDL) biocatalyst (where the enzyme laccase is displayed on the surface of biological cells through synthetic biology)
0.338
acetaminophen
-
pH 5.0, 30°C, soluble enzyme
0.011
catechol
native wild-type enzyme, pH 5.0, 25°C
0.018
catechol
recombinant His-tagged enzyme MmPPOA-695, pH 5.0, 25°C
0.022
catechol
recombinant wild-type enzyme MmPPOA-695, pH 5.0, 25°C
0.025
catechol
-
40°C, pH 4.5
0.031
catechol
-
pH 5.0, 25°C
0.0773
catechol
-
pH 9.0, 40°C
0.098
catechol
pH 5.0, 25°C
0.147
catechol
-
immobilized enzyme
0.16
catechol
pH 5.0, 25°C
0.23
catechol
Loweporus lividus MTCC-1178
-
-
0.23
catechol
Loweporus lividus
-
in 50 mM sodium malonate buffer, pH 4.5 at 37°C
0.261
catechol
-
immobilized enzyme in presence of 1-hydroxybenzotriazole
0.529
catechol
pH and temperature not specified in the publication
0.881
catechol
pH 3.0, 50°C
1.05
catechol
-
pH 7.0, 30°C
1.11
catechol
-
pH 5.0, 25°C
1.24
catechol
-
pH 7.0 37°C
1.478
catechol
recombinant mutant enzyme MmPPOA-637, pH 5.0, 25°C
1.48
catechol
-
pH 7.5, 37°C
1.72
catechol
-
30°C, pH 3.0
3.434
catechol
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
4.08
catechol
-
pH 5.0, temperature not specified in the publication
8.06
catechol
in McIlvaine buffer (pH 4.0), at 30°C
0.006
dopamine
-
pH 5.0, 25°C
0.17
dopamine
pH 5.0, 25°C
0.29
dopamine
pH 5.0, 25°C
2.1
dopamine
-
pH 5.0, 25°C
0.092
ferrocenemonocarboxylic acid
-
pH 5.0, 25°C
-
0.38
ferrocenemonocarboxylic acid
pH 5.0, 25°C
-
0.41
ferrocenemonocarboxylic acid
-
pH 5.0, 25°C
-
0.45
ferrocenemonocarboxylic acid
pH 5.0, 25°C
-
0.32
ferrocyanide
pH 5.0, 25°C
0.79
ferrocyanide
pH 5.0, 25°C
0.83
ferrocyanide
-
pH 5.0, 25°C
0.89
ferrocyanide
-
pH 5.0, 25°C
0.025
ferulic acid
Coriolisimus fulvocinerea
-
-
0.12
ferulic acid
in McIlvaine buffer (pH 5.0), at 30°C
0.27
ferulic acid
Thermochaetoides thermophila
-
pH 6.0, 50°C
1.39
ferulic acid
-
30°C, pH 5.0
14
ferulic acid
pH 5.2, 45°C
0.0514
gallic acid
-
pH 7.0, 40°C
0.13
gallic acid
Thermochaetoides thermophila
-
pH 6.0, 50°C
0.0154
guaiacol
-
pH 5.0, 25°C
0.016
guaiacol
-
pH 7.0, 30°C
0.06
guaiacol
-
pH 4.5, 35°C
0.091
guaiacol
Coriolisimus fulvocinerea
-
-
0.093
guaiacol
-
pH 5.0, 22°C
0.215
guaiacol
pH 6.0, 90°C, mutant enzyme D394M
0.24
guaiacol
22°C, pH 7.0, mutant enzyme L386Q/G417I (variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions)
0.24
guaiacol
pH 5.0, temperature not specified in the publication, wild-type PM1 laccase
0.243
guaiacol
pH 6.0, 90°C, mutant enzyme D394R
0.25
guaiacol
pH 4.5, 22°C, native enzyme
0.251
guaiacol
-
pH 6.0, 25°C
0.266
guaiacol
pH 6.0, 90°C, mutant enzyme D394E
0.3
guaiacol
pH and temperature not specified in the publication
0.3
guaiacol
pH 8.5, temperature not specified in the publication
0.325
guaiacol
pH 6.0, 90°C, mutant enzyme D396A
0.33
guaiacol
-
pH 5.0, 25°C
0.35
guaiacol
-
30°C, pH 4.0
0.356
guaiacol
pH 6.0, 90°C, mutant enzyme D396M
0.367
guaiacol
-
pH 8.0, 40°C
0.367
guaiacol
pH 4.5, 22°C, deglycosylated enzyme
0.37
guaiacol
-
pH 4.2, 50°C
0.38
guaiacol
-
pH 5.5, 50°C
0.382
guaiacol
pH 6.0, 90°C, mutant enzyme D396E
0.384
guaiacol
-
pH 6.0, 90°C, wild-type enzyme
0.391
guaiacol
-
pH 6.0, 90°C, mutant enzyme K428M
0.392
guaiacol
pH 6.0, 90°C, mutant enzyme D396N
0.4
guaiacol
Thermochaetoides thermophila
-
pH 6.0, 50°C
0.4
guaiacol
Phlebia fascicularia
-
Lac II, 70°C, pH 4.0
0.4
guaiacol
pH 5.0, temperature not specified in the publication
0.405
guaiacol
Phlebia fascicularia
-
Lac I, 70°C, pH 4.0
0.407
guaiacol
pH 6.0, 90°C, wild-type enzyme
0.42
guaiacol
pH 4.5, 25°C
0.439
guaiacol
pH 6.0, 90°C, mutant enzyme D394N
0.455
guaiacol
pH 4.5, 40°C, isoenzyme Lac4
0.473
guaiacol
-
pH 6.0, 90°C, mutant enzyme K428R
0.52
guaiacol
-
pH 6.0, 90°C, mutant enzyme K428E
0.55
guaiacol
-
pH 6.5, 40°C
0.552
guaiacol
-
pH 4.0, 25°C
0.575
guaiacol
-
pH 6.0, 90°C, mutant enzyme K428L
0.648
guaiacol
pH 5.5, 65°C
0.7
guaiacol
-
pH and temperature not specified in the publication
0.849
guaiacol
pH 3.0, 50°C
0.891
guaiacol
pH 5.0, 30°C
1.04
guaiacol
pH 5.0, temperature not specified in the publication
1.05
guaiacol
-
pH 5.0, 25°C
1.05
guaiacol
22°C, pH 7.0, wild-type enzyme
1.095
guaiacol
-
pH 3.0, 25°C, laccase Lac-3.5
1.1077
guaiacol
-
pH 7.5, 37°C
1.114
guaiacol
-
in 100 mM citrate buffer, pH 4.5, at 37°C
1.114
guaiacol
pH 4.5, 40°C, isoenzyme Lac3
1.2
guaiacol
-
isoform POXC, pH 6.0, 25°C
1.263
guaiacol
recombinant enzyme, pH 3.0, 30°C
1.39
guaiacol
22°C, pH 7.0, mutant enzyme L386Q/G417I/V482G (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)
1.406
guaiacol
-
pH 3.0, 25°C, laccase Lac-4.8
1.89
guaiacol
-
pH 5.0, temperature not specified in the publication
2.14
guaiacol
pH 3.0, 30°C
2.23
guaiacol
pH and temperature not specified in the publication
2.5
guaiacol
-
pH 4.5, 40°C
2.657
guaiacol
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
2.772
guaiacol
-
pH and temperature not specified in the publication
2.8
guaiacol
-
isoenzyme L2
3.1
guaiacol
-
isoform POXA2, pH 6.0, 25°C
3.26
guaiacol
-
pH 8.0, 85°C
4
guaiacol
-
pH 6.0, 25°C
4.23
guaiacol
-
70°C, pH 6.0
4.3
guaiacol
pH and temperature not specified in the publication, mutant enzyme V281A/P309L/S318G/D232V
4.9
guaiacol
pH and temperature not specified in the publication, wild-type enzyme
10.7
guaiacol
in McIlvaine buffer (pH 4.0), at 30°C
17.6
guaiacol
pH 3.0, 30°C
918
guaiacol
pH 5.0, 30°C
1790
guaiacol
pH 3.0, 30°C
0.001
hydroquinone
-
isoenzyme lac90
0.0686
hydroquinone
-
pH 7.0, 40°C
0.086
hydroquinone
Coriolisimus fulvocinerea
-
-
0.123
hydroquinone
-
pH 7.0, 30°C
1.92
hydroquinone
-
pH 7.0 37°C
2.93
hydroquinone
pH 6.5, 30°C
11.33
hydroquinone
-
pH 7.5, 37°C
0.027
K4(FeCN6)
-
pH 7.6, 37°C, mutant M502L
0.067
K4(FeCN6)
-
pH 7.6, 37°C, mutant M502F
0.069
K4(FeCN6)
-
pH 7.6, 37°C, wild-type enzyme
0.1
K4[Fe(CN)6]
30°C, pH 4.0, wild-type enzyme
0.17
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme M199G/R240H
0.18
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme H165A/R240H
0.24
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme H165A/M199G
0.25
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme M199G
0.31
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme Y230A
0.35
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme M199A
9.9
K4[Fe(CN)6]
pH 4.0, temperature not specified in the publication
0.102
L-Dopa
-
pH 7.0, 40°C
0.84
L-Dopa
-
enzyme has a higher affinity for syringaldazine than for L-dopa
6.28
L-Dopa
-
pH 5.0, temperature not specified in the publication
0.21
m-cresol
Loweporus lividus MTCC-1178
-
-
0.21
m-cresol
Loweporus lividus
-
in 50 mM sodium malonate buffer, pH 4.5 at 37°C
0.212
N,N-dimethyl-1,4-phenylenediamine
-
pH 7.0, 30°C
0.53
N,N-dimethyl-1,4-phenylenediamine
-
pH 4, temperature not specified in the publication, mutant enzyme V159E
1.7
N,N-dimethyl-1,4-phenylenediamine
-
pH 4, temperature not specified in the publication, mutant enzyme V159E/N398D
2.3 - 2.5
N,N-dimethyl-4-phenylenediamine
-
pH 7.0, 20°C
3.3 - 3.8
N,N-dimethyl-4-phenylenediamine
-
pH 7.0, 25°C
0.29
N,N-Dimethyl-p-phenylenediamine
pH 4.0, temperature not specified in the publication
1.06
N,N-Dimethyl-p-phenylenediamine
pH 4.0, temperature not specified in the publication, wild-type PM1 laccase
3.9
N,N-Dimethyl-p-phenylenediamine
-
-
0.43
N-acetyldopamine
pH 5.0-5.5, recombinant N-terminally truncated enzyme
0.46
N-acetyldopamine
pH 5.0-5.5, recombinant full-length enzyme
0.63
N-acetyldopamine
pH 5.0-5.5, native enzyme
0.47
N-beta-alanyldopamine
pH 5.0-5.5, native enzyme
1.9
N-beta-alanyldopamine
pH 5.0-5.5, recombinant full-length enzyme
0.045
o-Dianisidine
-
isoenzyme L2
0.144
o-Dianisidine
30°C, pH not specified in the publication
0.647
o-Dianisidine
30°C, pH not specified in the publication
0.01
O2
25°C, pH 5.6
0.25
O2
-
extracellular enzyme
0.37
O2
-
intracellular enzyme
2.21
p-phenylenediamine
presence of 0.25 mM Cu2+, pH 5, 30°C
3.2
p-phenylenediamine
pH 5, 30°C
3.31
p-phenylenediamine
presence of 0.1 mM Cu2+, pH 5, 30°C
6.6
p-phenylenediamine
-
-
7.25
p-phenylenediamine
presence of 0.01 mM Cu2+, pH 5, 30°C
90
p-phenylenediamine
region Pro357-His406 deletion mutant, pH 5.5, 25°C
375
p-phenylenediamine
wild-type, pH 5.5, 25°C
0.0145
pyrogallol
-
pH 8.0, 40°C
0.023
pyrogallol
-
pH 7.0, 30°C
0.32
pyrogallol
Loweporus lividus MTCC-1178
-
-
0.32
pyrogallol
Loweporus lividus
-
in 50 mM sodium malonate buffer, pH 4.5 at 37°C
0.56
pyrogallol
in McIlvaine buffer (pH 4.0), at 30°C
24.6
pyrogallol
-
30°C, pH 3.0
1.25
quinol
-
-
0.013
Sinapic acid
recombinant wild-type enzyme, pH 5.0, temperature not specified in the publication
0.085
Sinapic acid
recombinant wild-type enzyme, pH 3.0, temperature not specified in the publication
0.0018
syringaldazine
-
pH 6.0
0.0028
syringaldazine
-
pH 3.0, 25°C, laccase Lac-4.8
0.0037
syringaldazine
-
pH 8.0, 22°C
0.004
syringaldazine
-
pH 5.5
0.0042
syringaldazine
-
pH 4.5
0.0042
syringaldazine
Myrioconium sp.
-
25°C, pH 6
0.0043
syringaldazine
-
pH 7.0
0.005
syringaldazine
-
at 22°C, pH not specified in the publication
0.00673
syringaldazine
-
pH 4.0, 25°C
0.0072
syringaldazine
30°C, pH 6.0, C-6His tagged laccase 3
0.008
syringaldazine
-
pH 4.5, 25°C
0.008
syringaldazine
-
pH 7.6, 37°C, mutant M502F
0.008
syringaldazine
-
mutant enzyme M502F
0.0081
syringaldazine
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)) and 6His tagged (C(DELTA)6H)
0.0083
syringaldazine
-
pH 4.2, 50°C
0.0087
syringaldazine
-
pH 7.0, 25°C
0.009
syringaldazine
-
pH 7.0, 30°C
0.009
syringaldazine
-
pH 7.6, 37°C, mutant M502L
0.009
syringaldazine
-
mutant enzyme M502L
0.0093
syringaldazine
30°C, pH 6.0, deglycosylated enzyme
0.01
syringaldazine
-
wild-type enzyme
0.01
syringaldazine
-
pH 7.6, 37°C, wild-type enzyme
0.01
syringaldazine
-
pH 5.6, 45°C
0.0109
syringaldazine
-
pH 6.2, 37°C
0.0116
syringaldazine
30°C, pH 6.0, wild-type enzyme
0.012
syringaldazine
-
pH 6.5, 40°C
0.0126
syringaldazine
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)) and 6His tagged (C(DELTA)6H) and hyper-glycosylated
0.0153
syringaldazine
40°C, pH 6.0
0.0161
syringaldazine
-
pH 7.0, 40°C
0.018
syringaldazine
-
pH 7, holoCotA
0.018
syringaldazine
-
pH 7.0, 25°C, wild-type CotA
0.0196
syringaldazine
pH 6.5, 37°C, recombinant enzyme
0.02
syringaldazine
pH 5, 30°C
0.02
syringaldazine
pH 5.0, 65°C
0.02
syringaldazine
-
isoform POXC, pH 6.0, 25°C
0.0237
syringaldazine
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA))
0.027
syringaldazine
-
pH 3.0, 25°C, laccase Lac-3.5
0.028
syringaldazine
-
pH 4.5
0.03
syringaldazine
pH 6.0, 22°C, recombinant truncated mutant POXA1bDELTA16
0.03
syringaldazine
pH 6.0, 22°C, recombinant truncated mutant POXA1bDELTA4
0.031
syringaldazine
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae
0.033
syringaldazine
-
pH 7.0, 25°C, mutant L386A
0.034
syringaldazine
Thermochaetoides thermophila
-
pH 6.0, 50°C
0.035
syringaldazine
45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02
0.036
syringaldazine
-
25°C, isozyme POXA3a
0.036
syringaldazine
-
isoform POXA3a, pH 6.0, 25°C
0.037
syringaldazine
pH 4.5, 25°C, recombinant wild-type enzyme
0.04
syringaldazine
-
pH 6.0, 50°C
0.04
syringaldazine
pH 6.0, 22°C, recombinant wild-type enzyme
0.04
syringaldazine
30°C, pH not specified in the publication
0.05
syringaldazine
-
40°C, pH 4.5
0.052
syringaldazine
-
pH 8.0, 25°C, mutant I494A
0.079
syringaldazine
-
25°C, isozyme POXA3b
0.079
syringaldazine
-
isoform POXA3b, pH 6.0, 25°C
0.087
syringaldazine
-
pH 6.0, 50°C
0.087
syringaldazine
pH 4.5, 40°C, isoenzyme Lac3
0.091
syringaldazine
-
pH 5.0, 25°C
0.101
syringaldazine
30°C, pH not specified in the publication
0.102
syringaldazine
pH 4.5, 22°C, native enzyme
0.11
syringaldazine
-
enzyme has a higher affinity for syringaldazine than for L-dopa
0.13
syringaldazine
-
isoform POXA1w, pH 6.0, 25°C
0.14
syringaldazine
-
isoform POXA2, pH 6.0, 25°C
0.156
syringaldazine
pH 4.5, 22°C, deglycosylated enzyme
0.167
syringaldazine
35°C, pH 6.0
0.204
syringaldazine
pH 4.5, 40°C, isoenzyme Lac4
0.22
syringaldazine
-
isoform POXA1b, pH 6.0, 25°C
0.226
syringaldazine
-
pH 6.0, 50°C
0.256
syringaldazine
30°C, pH 6.0
0.35
syringaldazine
Loweporus lividus MTCC-1178
-
-
0.35
syringaldazine
Loweporus lividus
-
in 50 mM sodium malonate buffer, pH 4.5 at 37°C
0.379
syringaldazine
-
45°C, pH 7.4
1.88
syringaldazine
pH and temperature not specified in the publication
2.5
syringaldazine
-
pH 4.5, 40°C
3.77
syringaldazine
pH and temperature not specified in the publication
17
syringaldazine
pH 5.0, 23°C
39
syringaldazine
pH 5.0, 23°C
0.026
syringic acid
-
pH 4.5, 25°C
0.03
syringic acid
-
immobilized enzyme
0.055
syringic acid
-
immobilized enzyme
0.06
vanillic acid
-
immobilized enzyme
0.15
vanillic acid
Thermochaetoides thermophila
-
pH 6.0, 50°C
0.165
vanillic acid
Coriolisimus fulvocinerea
-
-
0.97
vanillic acid
-
immobilized enzyme
additional information
additional information
-
kinetics
-
additional information
additional information
-
comparison of values for free and immobilized laccase
-
additional information
additional information
-
study on kinetics, stoichiometries
-
additional information
additional information
-
study on kinetics, stoichiometries
-
additional information
additional information
-
study on kinetics, stoichiometries
-
additional information
additional information
Coriolisimus fulvocinerea
-
study on kinetics, stoichiometries
-
additional information
additional information
-
kinetic studies of electron transfer
-
additional information
additional information
-
dependency on source of enzyme, pH, inhibition by F-
-
additional information
additional information
-
dependency on source of enzyme, pH, inhibition by F-
-
additional information
additional information
-
dependency on source of enzyme, pH, inhibition by F-
-
additional information
additional information
-
dependency on source of enzyme, pH, inhibition by F-
-
additional information
additional information
-
dependency on source of enzyme, pH, inhibition by F-
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
kinetics of mutant enzymes, overview
-
additional information
additional information
-
kinetics of mutant enzymes, overview
-
additional information
additional information
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
Fomes sclerodermeus
-
both isozymes show Michaelis-Menten kinetics, overview
-
additional information
additional information
-
kinetics in absence and presence of acidic and halophenols, overview
-
additional information
additional information
-
kinetics of isozymes, overview
-
additional information
additional information
-
kinetics with Michaelis-Menten constants obtained from amperometric measurements, kinetics of coupled reaction with catechol and 1-hydroxybenzotriazole, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, laccases copper type I redox potential
-
additional information
additional information
-
MichaelisMenten kinetics, laccases copper type I redox potential
-
additional information
additional information
-
MichaelisMenten kinetics, laccases copper type I redox potential
-
additional information
additional information
-
MichaelisMenten kinetics, laccases copper type I redox potential
-
additional information
additional information
-
thermodynamics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
transient/stopped-flow and steady-state kinetics, modeling
-
additional information
additional information
FJ560721
steady-state kinetics, overview
-
additional information
additional information
-
analysis of enzyme dynamics and catalytic, spectral properties. Analysis of the structural state of the purified native laccase in solution at the phase transition before freezing, at freezing, and subsequent thawing of enzyme solution, processes in the active site on environmental temperature changes, overview
-
additional information
additional information
construction of enzymesubstrate complexes and molecular dynamics simulations, complex of mutant D205R with 2,5-xylidine, molecular dynamics simulations, overview
-
additional information
additional information
the enzyme shows typical MichaelisMenten kinetics, overview
-
additional information
additional information
-
the enzyme shows typical MichaelisMenten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics, overview
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics, overview
-
additional information
additional information
Michaelis-Menten steady-state kinetics, overview
-
additional information
additional information
Michaelis-Menten steady-state kinetics, overview
-
additional information
additional information
-
kinetics do not fit a Michaelis-Menten equation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.6 - 28.8
1-hydroxybenzotriazole
6.57 - 322
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
286 - 409
2,2'-azino-bis(3-ethylbenzathiazoline-6-sulfonate)
83 - 208
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate)
0.0046 - 409
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
0.29
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate)
Myrioconium sp.
-
25°C, pH 4
0.14 - 7109
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
0.012988 - 2468
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
1.58 - 24.6
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate)
0.064 - 158300
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
0.15 - 322
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
2 - 4.5
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)
7.8
2,2,6,6-tetramethylpiperidin-N-oxide radical
-
pH 3.8, 55°C
10
2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)
45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02
0.00403 - 2150
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
0.038
2,3-Dihydroxybenzoate
pH 7.0, 25°C
3 - 832
2,5-diaminotoluene
-
284.4
2,5-xylidine
-
pH 7.0, 40°C
0.01 - 23800
2,6-dimethoxyphenol
0.307 - 1.468
2,6-dimethylphenol
22.8
2-methoxyphenol
-
pH 3.8, 55°C
368
3-dimethylaminobenzoic acid
-
pH 6.0, 25°C
0.32 - 140
4-hydroxy-3,5-dimethoxybenzaldehyde azine
3.02 - 8.6
4-hydroxybenzoic acid
128
4-hydroxyindole
-
pH 7.0, 30°C
36.3
4-methoxyphenol
-
pH 3.8, 55°C
93.9
4-methyl catechol
-
pH 3.8, 55°C
32.2
anthraquinonic dye Acid Blue 62
pH 5.5, 65°C
29
bilirubin
45°C, pH 8.4, LccA protein isolated from Haloferax volcanii H26 strain US02
80.4
Diamond Black PV 200
-
25°C, pH 4.5
428
eugenol
-
pH 4.5, 55°C
0.92 - 137
ferrocenemonocarboxylic acid
-
5.2
ferulic acid
pH 5.2, 45°C
675
gallic acid
-
pH 7.0, 40°C
408
homovanillic acid
-
pH 4.5, 55°C
529
K4Fe(CN)6
-
pH 3, holoCotA
404
K4[Fe(CN)]6
-
pH 4.5, 55°C
462.5
L-tyrosine
-
pH 7.0, 40°C
5.5
methyl syringate
-
pH 5.5, 20°C
1.7 - 56
N,N-dimethyl-1,4-phenylenediamine
181 - 443
N,N-dimethyl-4-phenylenediamine
108.6 - 938
N,N-Dimethyl-p-phenylenediamine
1.33 - 4.83
N-acetyldopamine
3 - 3.33
N-beta-alanyldopamine
18.3
N-hydroxyacetanilide
-
pH 5.5, 20°C
0.057 - 0.748
o-Dianisidine
0.01 - 11670
syringaldazine
10.1
syringic acid
-
pH 4.5, 25°C
1471.9
Tannic acid
-
pH 7.0, 40°C
102
vanillic acid
-
pH 4.5, 55°C
352
vanillic alcohol
-
pH 4.5, 55°C
2.6
1-hydroxybenzotriazole
-
pH 3.8, 55°C
15.5
1-hydroxybenzotriazole
pH 5.0, temperature not specified in the publication, wild-type PM1 laccase
28.8
1-hydroxybenzotriazole
pH 5.0, temperature not specified in the publication, engineered enzyme 7D5
3.56
1-naphthol
pH and temperature not specified in the publication, wild-type enzyme
3.89
1-naphthol
pH and temperature not specified in the publication, mutant enzyme V281A/P309L/S318G/D232V
6.57
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae
7.2
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C, mutant I494A
10.6
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 2.5, 65°C
18.2
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C, recombinant wild-type enzyme
28.1
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 25°C, recombinant wild-type enzyme
36.5
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C, recombinant mutant WlacS
48.6
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 22°C, deglycosylated enzyme
50.9
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C, recombinant mutant WlacD
52
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C, mutant L386A
59.3
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 22°C, native enzyme
197
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.8, 25°C
322
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C, wild-type CotA
286
2,2'-azino-bis(3-ethylbenzathiazoline-6-sulfonate)
-
pH 3.0, 25°C, laccase Lac-3.5
409
2,2'-azino-bis(3-ethylbenzathiazoline-6-sulfonate)
-
pH 3.0, 25°C, laccase Lac-4.8
83
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate)
-
pH 4.0
208
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate)
-
-
0.0046
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3, temperature not specified in the publication, mutant enzyme V159E/N398D
0.3
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
70°C, pH 3.0
0.431
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH not specified in the publication
0.696
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH not specified in the publication
4.14
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
22°C, pH 5.0
6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 3.5, mutant enzyme H165A/R240H
6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme H165A/R240H, 30°C, pH not specified in the publication
9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 3.5, mutant enzyme H165A/M199G
9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme H165A/M199G, 30°C, pH not specified in the publication
15
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild-type enzyme, 30°C, pH not specified in the publication
15
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 4.0, wild-type enzyme
20
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 3.5, mutant enzyme M199G/R240H
20
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme M199G/R240H, 30°C, pH not specified in the publication
23.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 30°C
29
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 3.5, mutant enzyme Y230A
29
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme Y230A, 30°C, pH not specified in the publication
33
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 4.0, mutant enzyme M199A
33
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme M199A, 30°C, pH not specified in the publication
33
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3, temperature not specified in the publication, mutant enzyme V159E
34.39
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH and temperature not specified in the publication, wild-type enzyme
42.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 30°C
44.4
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, temperature not specified in the publication, wild-type PM1 laccase
45
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 4.0, mutant enzyme M199G
45
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme M199G, 30°C, pH not specified in the publication
46.94
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH and temperature not specified in the publication, mutant enzyme V281A/P309L/S318G/D232V
198.29
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, temperature not specified in the publication
240
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, temperature not specified in the publication, engineered enzyme 7D5
315
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C
409
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C
0.14
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
FJ560721
pH 5.0, 22-25°C
0.6
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, recombinant Lac1
1.15
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, recombinant Lac1
4.22
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 30°C
4.26
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 6.5, 25°C, mutant K532A
4.58
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 6.5, 25°C, mutant P530A
5.51
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 6.5, 25°C, mutant K532E
7.67
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, recombinant Lac1
10.1
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 5.0, 25°C
15.93
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, recombinant Lac1
20
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 6.0, 25°C
38
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
recombinant wild-type enzyme, pH 5.0, temperature not specified in the publication
60.6
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 25°C, mutant P530A
65.6
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
recombinant enzyme, pH 3.0, 30°C
70.02
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 25°C, mutant K532A
70.6
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 25°C, mutant P530A
74.67
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 25°C, mutant K532E
97.85
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 25°C, mutant K532E
100.7
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 25°C, mutant K532A
107.1
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
109
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
127
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
at 22°C, pH not specified in the publication
130
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
144.6
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
recombinant wild-type enzyme, pH 3.0, temperature not specified in the publication
196
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 5.0, 25°C
291
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 4.0, 22°C, recombinant enzyme
594
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, temperature not specified in the publication
934.6
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 50°C
1372
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 3.2, 37°C
1480
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
in 67 mM sodium acetate buffer (pH 4.5), at 30°C
7109
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 3.0, 50°C
0.012988
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
laccase DcLac1, pH 2.8, temperature not specified in the publication
0.018534
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
laccase DcLac2, pH 2.8, temperature not specified in the publication
0.058
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 7.0 37°C
1.02
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 4.0, 35°C
1.467
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, isoenzyme Lac4
1.9
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, temperature not specified in the publication
2.54
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
3.485
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, isoenzyme Lac3
6.45
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
6.85
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH and temperature not specified in the publication
7.7
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
25°C, pH 4.0
15.7
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I/V482G (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)
21.2
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188A, in aqueous solution
23
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 5.0, 25°C, recombinant enzyme
31.11
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188K, in aqueous solution
32.03
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 37°C
32.8
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 4.5
42.2
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
21-23°C, pH not specified in the publication, wild-type enzyme
45.8
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, wild-type enzyme, in aqueous solution
67.04
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 8.0, 85°C
69.7
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I (variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions)
72
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 3.4, 70°C
86.4
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188L, in aqueous solution
98.2
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188R, in aqueous solution
99.5
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188V, in aqueous solution
102.8
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188I, in aqueous solution
260
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 4.0, 25°C
286.5
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 3.0, 25°C
309
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 22°C
377
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 5.0, 30°C
399
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4, 30°C
2468
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH and temperature not specified in the publication
1.58
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate)
50°C, pH 6.0
3.33
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate)
55°C, pH 6.0
4.77
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate)
60°C, pH 6.0
24.6
2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate)
pH and temperature not specified in the publication
0.064
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 505 kDa
0.08
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 214 kDa
0.101
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 432 kDa
0.168
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 131 kDa
0.252
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
free enzyme
0.26
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 7.6, 37°C, mutant M502F
1.3
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant wild-type enzyme
1.6
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant mutant D206A
3.3
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant mutant D206E
4.3
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant mutant D206N
10.3
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 5.5, 20°C
10.6
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 7.6, 37°C, mutant M502L
11.7
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 7.0, 25°C
21
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 5.5
22.4
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 7.6, 37°C, wild-type enzyme
26
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 7.0, 30°C
68.87
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.0, 25°C
78.3
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5
182
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
Fomes sclerodermeus
-
pH 5.0, isozyme Lac II
199
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
Fomes sclerodermeus
-
pH 5.0, isozyme Lac I
204
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.2, 45°C
272
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 4.5, 65°C
692
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 4.5, 25°C
778
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.0, 25°C
1520
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 40°C
2277
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5
73300
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
25°C, isozyme POXA3a
158300
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
25°C, isozyme POXA3b
0.15
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant M456A, presence of 0.5 mM Cu2+, 30°C, pH 5
0.16
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant M455L, 30°C, pH 5
0.25
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
wild-type, 30°C, pH 5
0.58
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
pH 7.0, 25°C
0.69
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
wild-type, presence of 0.5 mM Cu2+, 30°C, pH 5
0.98
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
wild-type, pH 5.5, 25°C
1.1
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant P444A/M510Q, pH 5.5, temperature not specified in the publication
5.7
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant P444I, pH 5.5, 25°C
8.7
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant P444A, pH 5.5, 25°C
10
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant P444L, pH 5.5, 25°C
15
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
region Pro357-His406 deletion plus D439A/P444A mutant, pH 5.5, 25°C
17
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant D439A, pH 5.5, 25°C
17
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
region Pro357-His406 deletion plus P444A mutant, pH 5.5, 25°C
23
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
region Pro357-His406 deletion plus P444A mutant, pH 5.5, 25°C
38
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
region Pro357-His406 deletion mutant, pH 5.5, 25°C
40
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant D439A/P444A, pH 5.5, 25°C
50
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
region Pro357-His406 deletion plus P444G mutant, pH 5.5, 25°C
137
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant D439A/M510L, pH 5.5, temperature not specified in the publication
147
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
region Pro357-His406 deletion plus D439A mutant, pH 5.5, 25°C
322
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
-
pH 3, holoCotA
2
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)
recombinant His-tagged enzyme MmPPOA-695, pH 5.0, 25°C
2.5
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)
recombinant wild-type enzyme MmPPOA-695, pH 5.0, 25°C
4.5
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)
native wild-type enzyme, pH 5.0, 25°C
0.00403
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 7.5, 37°C
67
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA))
170
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, C-6His tagged laccase 3
299
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)) and 6His tagged (C(DELTA)6H)
328
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)), 6His tagged (C(DELTA)6H) and hyper-glycosylated
445
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, deglycosylated enzyme
549
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, wild-type enzyme
2150
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 6.0, 40°C
3 - 6
2,5-diaminotoluene
mutant M510L, pH 5.5, temperature not specified in the publication
-
3.2
2,5-diaminotoluene
mutant D439A/M510Q, pH 5.5, temperature not specified in the publication
-
11
2,5-diaminotoluene
mutant P444A/M510Q, pH 5.5, temperature not specified in the publication
-
16
2,5-diaminotoluene
mutant D439A/P444A/M510Q, pH 5.5, temperature not specified in the publication
-
19
2,5-diaminotoluene
wild-type, pH 5.5, temperature not specified in the publication
-
25
2,5-diaminotoluene
mutant P444A/M510Q, pH 5.5, temperature not specified in the publication
-
105
2,5-diaminotoluene
mutant P444A, pH 5.5, temperature not specified in the publication
-
233
2,5-diaminotoluene
mutant D439A/P444A, pH 5.5, temperature not specified in the publication
-
366
2,5-diaminotoluene
mutant D439A, pH 5.5, temperature not specified in the publication
-
832
2,5-diaminotoluene
mutant D439A/M510L, pH 5.5, temperature not specified in the publication
-
0.01
2,6-dimethoxyphenol
-
pH 7.6, 37°C, mutant M502F
0.04 - 1.97
2,6-dimethoxyphenol
-
pH 7.0, 25°C
0.058
2,6-dimethoxyphenol
-
25°C, pH 9.0
0.08
2,6-dimethoxyphenol
-
pH 5, temperature not specified in the publication, mutant enzyme V159E/N398D
0.1
2,6-dimethoxyphenol
recombinant mutant enzyme MmPPOA-637, pH 5.0, 25°C
0.11
2,6-dimethoxyphenol
30°C, pH 9.0, mutant enzyme H165A/R240H
0.11
2,6-dimethoxyphenol
mutant enzyme H165A/R240H, 30°C, pH not specified in the publication
0.178
2,6-dimethoxyphenol
30°C, pH not specified in the publication
0.21
2,6-dimethoxyphenol
recombinant His-tagged mutant enzyme MmPPOA-637, pH 5.0, 25°C
0.29
2,6-dimethoxyphenol
pH 3.4, 30°C, recombinant mutant D206E
0.31
2,6-dimethoxyphenol
30°C, pH 6.5, mutant enzyme H165A/M199G
0.31
2,6-dimethoxyphenol
mutant enzyme H165A/M199G, 30°C, pH not specified in the publication
0.35
2,6-dimethoxyphenol
FJ560721
pH 5.0, 22-25°C
0.35
2,6-dimethoxyphenol
wild-type enzyme, 30°C, pH not specified in the publication
0.35
2,6-dimethoxyphenol
30°C, pH 9.0, wild-type enzyme
0.42
2,6-dimethoxyphenol
pH 3.4, 30°C, recombinant mutant D206A
0.51
2,6-dimethoxyphenol
pH 3.4, 30°C, recombinant wild-type enzyme
0.66
2,6-dimethoxyphenol
pH 3.4, 30°C, recombinant mutant D206N
0.92
2,6-dimethoxyphenol
recombinant wild-type enzyme MmPPOA-695, pH 5.0, 25°C
1.3
2,6-dimethoxyphenol
30°C, pH 8.0, mutant enzyme M199A
1.3
2,6-dimethoxyphenol
mutant enzyme M199A, 30°C, pH not specified in the publication
1.55
2,6-dimethoxyphenol
-
pH 7.6, 37°C, mutant M502L
1.68
2,6-dimethoxyphenol
30°C, pH 8.5, mutant enzyme Y230A
1.68
2,6-dimethoxyphenol
mutant enzyme Y230A, 30°C, pH not specified in the publication
1.74
2,6-dimethoxyphenol
recombinant His-tagged enzyme MmPPOA-695, pH 5.0, 25°C
1.98
2,6-dimethoxyphenol
native wild-type enzyme, pH 5.0, 25°C
2 - 8
2,6-dimethoxyphenol
-
pH 7.0
2.3
2,6-dimethoxyphenol
pH 3.0, 37°C
2.441
2,6-dimethoxyphenol
30°C, pH not specified in the publication
2.54
2,6-dimethoxyphenol
-
pH 4.5, 37°C
2.93
2,6-dimethoxyphenol
-
pH 8.0, 70°C
3 - 6
2,6-dimethoxyphenol
-
pH 7.0, 25°C, wild-type CotA
3
2,6-dimethoxyphenol
-
at 22°C, pH not specified in the publication
3.18
2,6-dimethoxyphenol
Myrioconium sp.
-
25°C, pH 6
3.39
2,6-dimethoxyphenol
30°C, pH 8.0, mutant enzyme M199G
3.39
2,6-dimethoxyphenol
mutant enzyme M199G, 30°C, pH not specified in the publication
3.46
2,6-dimethoxyphenol
-
22°C, pH 5.0
4.18
2,6-dimethoxyphenol
30°C, pH 8.5, mutant enzyme M199G/R240H
4.18
2,6-dimethoxyphenol
mutant enzyme M199G/R240H, 30°C, pH not specified in the publication
4.3
2,6-dimethoxyphenol
pH 4.0, 65°C
4.5
2,6-dimethoxyphenol
-
pH 9.0, 25°C, mutant I494A
6
2,6-dimethoxyphenol
-
pH 5, temperature not specified in the publication, mutant enzyme V159E
6.45
2,6-dimethoxyphenol
-
pH 4.5, 37°C
6.65
2,6-dimethoxyphenol
-
pH 7.6, 37°C, wild-type enzyme
6.85
2,6-dimethoxyphenol
-
pH and temperature not specified in the publication
6.91
2,6-dimethoxyphenol
-
pH 4.0, 25°C
7.89
2,6-dimethoxyphenol
pH 5.0, 30°C
8.94
2,6-dimethoxyphenol
-
pH 7.0, 25°C
9.08
2,6-dimethoxyphenol
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae
9.43
2,6-dimethoxyphenol
pH and temperature not specified in the publication, wild-type enzyme
10.2
2,6-dimethoxyphenol
pH 4.5, 25°C, recombinant wild-type enzyme
11
2,6-dimethoxyphenol
-
pH 7.0, 22°C, recombinant enzyme
11.23
2,6-dimethoxyphenol
pH and temperature not specified in the publication, mutant enzyme V281A/P309L/S318G/D232V
13.2
2,6-dimethoxyphenol
pH 5.0, temperature not specified in the publication, wild-type PM1 laccase
14.8
2,6-dimethoxyphenol
pH 5.0, 30°C
15
2,6-dimethoxyphenol
-
pH 5.5
16.3
2,6-dimethoxyphenol
recombinant wild-type enzyme, pH 5.0, temperature not specified in the publication
17
2,6-dimethoxyphenol
-
pH 7.0, 25°C, mutant L386A
17.7
2,6-dimethoxyphenol
-
pH 3.8, 55°C
23.2
2,6-dimethoxyphenol
21-23°C, pH not specified in the publication, wild-type enzyme
26.4
2,6-dimethoxyphenol
recombinant wild-type enzyme, pH 3.0, temperature not specified in the publication
29
2,6-dimethoxyphenol
-
pH 7, holoCotA
34
2,6-dimethoxyphenol
-
pH 7.0, 30°C
34.4
2,6-dimethoxyphenol
pH 8.5, temperature not specified in the publication
38.2
2,6-dimethoxyphenol
-
pH 5.0, temperature not specified in the publication
38.5
2,6-dimethoxyphenol
recombinant enzyme, pH 3.0, 30°C
38.8
2,6-dimethoxyphenol
21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I/V482G (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)
38.81
2,6-dimethoxyphenol
-
70°C, pH 6.5
45.3
2,6-dimethoxyphenol
pH 5.0, temperature not specified in the publication, engineered enzyme 7D5
50
2,6-dimethoxyphenol
-
pH 4.8, 25°C
50.3
2,6-dimethoxyphenol
-
pH 4.0, 25°C
67
2,6-dimethoxyphenol
-
pH 6.0
68
2,6-dimethoxyphenol
-
pH and temperature not specified in the publication
73.15
2,6-dimethoxyphenol
-
pH 8.0, 85°C
80.4
2,6-dimethoxyphenol
21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I (variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions)
81
2,6-dimethoxyphenol
pH 4.5, 25°C
102
2,6-dimethoxyphenol
pH 3.0, 30°C
103
2,6-dimethoxyphenol
-
-
109.2
2,6-dimethoxyphenol
pH 3.0, 50°C
121
2,6-dimethoxyphenol
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
155
2,6-dimethoxyphenol
pH 3.0, 30°C
180
2,6-dimethoxyphenol
pH 5.2, 45°C
189
2,6-dimethoxyphenol
-
pH 4.5
206
2,6-dimethoxyphenol
Fomes sclerodermeus
-
pH 5.0, isozyme Lac I
218
2,6-dimethoxyphenol
Fomes sclerodermeus
-
pH 5.0, isozyme Lac II
329
2,6-dimethoxyphenol
pH 4, 30°C
347
2,6-dimethoxyphenol
-
pH 3.0, 25°C, laccase Lac-3.5
365.6
2,6-dimethoxyphenol
-
pH 3.8, 55°C
481
2,6-dimethoxyphenol
-
pH 3.0, 25°C, laccase Lac-4.8
703.7
2,6-dimethoxyphenol
pH and temperature not specified in the publication
1009.4
2,6-dimethoxyphenol
-
pH 8.0, 40°C
1476
2,6-dimethoxyphenol
-
pH 4.0, 50°C
20000
2,6-dimethoxyphenol
-
25°C, isozyme POXA3b
23800
2,6-dimethoxyphenol
-
25°C, isozyme POXA3a
0.307
2,6-dimethylphenol
pH 4.5, 40°C, isoenzyme Lac3
1.468
2,6-dimethylphenol
pH 4.5, 40°C, isoenzyme Lac4
4.9
2-dianisidine
pH 4.5, 22°C, deglycosylated enzyme
9.4
2-dianisidine
pH 4.5, 22°C, native enzyme
20.7
2-dianisidine
-
pH 6.0, 25°C
0.32
4-hydroxy-3,5-dimethoxybenzaldehyde azine
pH 5.0, 25°C
6.85
4-hydroxy-3,5-dimethoxybenzaldehyde azine
-
pH and temperature not specified in the publication
77
4-hydroxy-3,5-dimethoxybenzaldehyde azine
-
pH 5.0, 25°C
122
4-hydroxy-3,5-dimethoxybenzaldehyde azine
pH 5.0, 25°C
140
4-hydroxy-3,5-dimethoxybenzaldehyde azine
-
pH 5.0, 25°C
3.02
4-hydroxybenzoic acid
pH 5.0, temperature not specified in the publication, wild-type PM1 laccase
8.6
4-hydroxybenzoic acid
pH 5.0, temperature not specified in the publication, engineered enzyme 7D5
0.0165
catechol
-
pH 7.5, 37°C
0.042
catechol
-
pH 7.0 37°C
0.084
catechol
recombinant mutant enzyme MmPPOA-637, pH 5.0, 25°C
1.53
catechol
recombinant wild-type enzyme MmPPOA-695, pH 5.0, 25°C
2.18
catechol
recombinant His-tagged enzyme MmPPOA-695, pH 5.0, 25°C
2.6
catechol
pH 5.0, 25°C
4.2
catechol
native wild-type enzyme, pH 5.0, 25°C
34.4
catechol
-
pH 3.8, 55°C
44.9
catechol
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
46
catechol
-
pH 7.0, 30°C
88
catechol
-
pH 5.0, 25°C
115
catechol
-
pH 5.0, 25°C
115.5
catechol
pH 3.0, 50°C
125
catechol
-
pH 5.0, temperature not specified in the publication
202
catechol
pH 5.0, 25°C
412.5
catechol
-
pH 9.0, 40°C
626
catechol
pH and temperature not specified in the publication
4.4
dopamine
pH 5.0, 25°C
116
dopamine
-
pH 5.0, 25°C
184
dopamine
pH 5.0, 25°C
186
dopamine
-
pH 5.0, 25°C
0.92
ferrocenemonocarboxylic acid
pH 5.0, 25°C
-
75
ferrocenemonocarboxylic acid
-
pH 5.0, 25°C
-
83
ferrocenemonocarboxylic acid
-
pH 5.0, 25°C
-
137
ferrocenemonocarboxylic acid
pH 5.0, 25°C
-
0.1
ferrocyanide
pH 5.0, 25°C
64
ferrocyanide
-
pH 5.0, 25°C
108
ferrocyanide
pH 5.0, 25°C
215
ferrocyanide
-
pH 5.0, 25°C
0.196
guaiacol
pH 4.5, 40°C, isoenzyme Lac4
0.211
guaiacol
pH 3.0, 30°C
0.418
guaiacol
pH 4.5, 40°C, isoenzyme Lac3
0.8
guaiacol
pH 6.0, 90°C, mutant enzyme D394R
1.34
guaiacol
pH and temperature not specified in the publication, wild-type enzyme
1.57
guaiacol
pH and temperature not specified in the publication, mutant enzyme V281A/P309L/S318G/D232V
1.7
guaiacol
pH 6.0, 90°C, mutant enzyme D394M
2.05
guaiacol
pH 4.5, 22°C, native enzyme
2.53
guaiacol
-
pH 5.0, 25°C
2.85
guaiacol
pH 5.0, temperature not specified in the publication, wild-type PM1 laccase
3 - 6
guaiacol
-
pH 7.0, 30°C
3
guaiacol
pH 4.5, 22°C, deglycosylated enzyme
3.3
guaiacol
pH 6.0, 90°C, mutant enzyme D394E
3.9
guaiacol
-
pH 6.0, 25°C
4.6
guaiacol
pH 5.5, 65°C
5
guaiacol
recombinant enzyme, pH 3.0, 30°C
5.5
guaiacol
pH 5.2, 45°C
5.7
guaiacol
-
pH 6.0, 90°C, mutant enzyme K428R
5.8
guaiacol
-
pH 6.0, 90°C, mutant enzyme K428L
6.1
guaiacol
-
pH 6.0, 90°C, wild-type enzyme
6.2
guaiacol
-
pH 6.0, 90°C, mutant enzyme K428E
6.7
guaiacol
pH 6.0, 90°C, mutant enzyme D396N
6.9
guaiacol
pH 6.0, 90°C, wild-type enzyme
7.1
guaiacol
pH 6.0, 90°C, mutant enzyme D396A
7.3
guaiacol
pH 6.0, 90°C, mutant enzyme D396M
7.4
guaiacol
pH 6.0, 90°C, mutant enzyme D394N
7.4
guaiacol
pH 6.0, 90°C, mutant enzyme D396E
8
guaiacol
pH 8.5, temperature not specified in the publication
8.4
guaiacol
-
pH 6.0, 90°C, mutant enzyme K428M
10.5
guaiacol
pH 5.0, temperature not specified in the publication, engineered enzyme 7D5
11.9
guaiacol
22°C, pH 7.0, wild-type enzyme
13.2
guaiacol
pH 5.0, 30°C
16.7
guaiacol
pH 5.0, 30°C
21.1
guaiacol
-
pH 4.0, 25°C
28.4
guaiacol
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
30.44
guaiacol
-
pH 5.5, 50°C
39.5
guaiacol
22°C, pH 7.0, mutant enzyme L386Q/G417I/V482G (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)
42.1
guaiacol
-
pH 6.0, 25°C
45.17
guaiacol
-
70°C, pH 6.0
56.3
guaiacol
-
pH 8.0, 40°C
62.96
guaiacol
-
pH 8.0, 85°C
64.9
guaiacol
22°C, pH 7.0, mutant enzyme L386Q/G417I (variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions)
71
guaiacol
-
pH 3.0, 25°C, laccase Lac-3.5
80.2
guaiacol
pH 5.0, temperature not specified in the publication
82
guaiacol
-
pH 3.0, 25°C, laccase Lac-4.8
85.1
guaiacol
pH 3.0, 30°C
92.2
guaiacol
-
pH 5.0, temperature not specified in the publication
95.6
guaiacol
pH 5.2, 45°C
128.1
guaiacol
pH and temperature not specified in the publication
147.9
guaiacol
pH 3.0, 50°C
226
guaiacol
-
pH and temperature not specified in the publication
310
guaiacol
-
pH 6.5, 40°C
424
guaiacol
-
pH 4.5, 55°C
0.051
hydroquinone
-
pH 7.5, 37°C
0.23
hydroquinone
-
pH 7.0 37°C
55
hydroquinone
-
pH 7.0, 30°C
443.8
hydroquinone
-
pH 7.0, 40°C
455
hydroquinone
-
pH 4.5, 55°C
5.5
K4(FeCN6)
-
pH 7.6, 37°C, mutant M502F
20.9
K4(FeCN6)
-
pH 7.6, 37°C, mutant M502L
54.5
K4(FeCN6)
-
pH 7.6, 37°C, wild-type enzyme
0.2
K4[Fe(CN)6]
pH 4.0, temperature not specified in the publication
29
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme H165A/R240H
35
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme H165A/M199G
38
K4[Fe(CN)6]
30°C, pH 4.0, wild-type enzyme
48
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme M199G/R240H
54
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme M199A
66
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme M199G
86
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme Y230A
83.2
L-Dopa
-
pH 5.0, temperature not specified in the publication
318.8
L-Dopa
-
pH 7.0, 40°C
1.7
N,N-dimethyl-1,4-phenylenediamine
-
pH 4, temperature not specified in the publication, mutant enzyme V159E/N398D
18
N,N-dimethyl-1,4-phenylenediamine
-
pH 7.0, 30°C
56
N,N-dimethyl-1,4-phenylenediamine
-
pH 4, temperature not specified in the publication, mutant enzyme V159E
181 - 186
N,N-dimethyl-4-phenylenediamine
-
pH 7.0, 20°C
350 - 443
N,N-dimethyl-4-phenylenediamine
-
pH 7.0, 25°C
108.6
N,N-Dimethyl-p-phenylenediamine
pH 4.0, temperature not specified in the publication, wild-type PM1 laccase
938
N,N-Dimethyl-p-phenylenediamine
pH 4.0, temperature not specified in the publication, engineered enzyme 7D5
1.33
N-acetyldopamine
pH 5.0-5.5, recombinant N-terminally truncated enzyme
1.67
N-acetyldopamine
pH 5.0-5.5, recombinant full-length enzyme
4.83
N-acetyldopamine
pH 5.0-5.5, native enzyme
3
N-beta-alanyldopamine
pH 5.0-5.5, native enzyme
3.33
N-beta-alanyldopamine
pH 5.0-5.5, recombinant full-length enzyme
2 - 8
o-benzenediol
-
pH 7.0, 25°C
21.98
o-benzenediol
-
pH 7.0, 25°C
403
o-benzenediol
-
pH 4.5, 55°C
0.057
o-Dianisidine
30°C, pH not specified in the publication
0.748
o-Dianisidine
30°C, pH not specified in the publication
10
pyrogallol
-
pH 7.0, 30°C
1231.3
pyrogallol
-
pH 8.0, 40°C
21.6
Sinapic acid
recombinant wild-type enzyme, pH 5.0, temperature not specified in the publication
52.8
Sinapic acid
recombinant wild-type enzyme, pH 3.0, temperature not specified in the publication
578
Sinapic acid
-
pH 4.5, 55°C
0.01
syringaldazine
-
pH 7.6, 37°C, mutant M502F
0.01
syringaldazine
-
mutant enzyme M502F
0.26
syringaldazine
-
pH 5.0, 25°C
0.337
syringaldazine
-
25°C, pH 8.0
0.365
syringaldazine
30°C, pH not specified in the publication
0.573
syringaldazine
30°C, pH not specified in the publication
1.29
syringaldazine
-
pH 6.2, 37°C
1.5
syringaldazine
pH 5.0, 65°C
2.54
syringaldazine
-
pH 6.0, 50°C
2.96
syringaldazine
Myrioconium sp.
-
25°C, pH 6
3.66
syringaldazine
30°C, pH 6.0
4
syringaldazine
-
pH 7.0, 30°C
4.9
syringaldazine
-
pH 6.5, 22°C, recombinant enzyme, with 0.8% v/v DMSO
5
syringaldazine
-
pH 5.5
5.33
syringaldazine
35°C, pH 6.0
6.1
syringaldazine
-
pH 7.0, 25°C
6.45
syringaldazine
-
pH 6.0, 50°C
6.47
syringaldazine
pH and temperature not specified in the publication
7.4
syringaldazine
-
pH 7.6, 37°C, mutant M502L
7.4
syringaldazine
-
mutant enzyme M502L
9
syringaldazine
-
pH 8.0, 25°C, mutant I494A
10.3
syringaldazine
40°C, pH 6.0
13
syringaldazine
-
pH 7.0, 25°C, mutant L386A
18.4
syringaldazine
-
wild-type enzyme
18.4
syringaldazine
-
pH 7.6, 37°C, wild-type enzyme
20
syringaldazine
-
at 22°C, pH not specified in the publication
21.05
syringaldazine
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae
22
syringaldazine
45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02
24
syringaldazine
pH 6.5, 37°C, recombinant enzyme
31.96
syringaldazine
pH 4.5, 40°C, isoenzyme Lac3
35.9
syringaldazine
-
pH 4.0, 25°C
39.9
syringaldazine
pH 4.5, 22°C, native enzyme
40.17
syringaldazine
pH 4.5, 25°C, recombinant wild-type enzyme
44.71
syringaldazine
pH 4.5, 40°C, isoenzyme Lac4
51
syringaldazine
-
pH 5.0, 22°C
51.52
syringaldazine
-
pH 5.0, 25°C
65.8
syringaldazine
pH 4.5, 22°C, deglycosylated enzyme
66
syringaldazine
-
pH 7.0, 22°C, recombinant enzyme, with 25% v/v DMSO
71
syringaldazine
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA))
80
syringaldazine
-
pH 7, holoCotA
80
syringaldazine
-
pH 7.0, 25°C, wild-type CotA
92
syringaldazine
-
pH 6.0
100
syringaldazine
-
pH 7.0
113
syringaldazine
30°C, pH 6.0, C-6His tagged laccase 3
124
syringaldazine
-
pH 3.0, 25°C, laccase Lac-4.8
188
syringaldazine
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)) and 6His tagged (C(DELTA)6H)
246
syringaldazine
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)) and 6His tagged (C(DELTA)6H) and hyper-glycosylated
282
syringaldazine
-
pH 3.0, 25°C, laccase Lac-3.5
290
syringaldazine
30°C, pH 6.0, deglycosylated enzyme
386
syringaldazine
30°C, pH 6.0, wild-type enzyme
600
syringaldazine
-
pH 4.5
654
syringaldazine
-
pH 6.5, 40°C
918.8
syringaldazine
-
pH 7.0, 40°C
938.1
syringaldazine
-
pH 6.0, 50°C
2830
syringaldazine
-
25°C, isozyme POXA3a
11670
syringaldazine
-
25°C, isozyme POXA3b
8.4
violuric acid
-
pH 3.8, 55°C
10
violuric acid
-
pH 5.5, 20°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.33 - 0.84
1-hydroxybenzotriazole
0.076 - 184500
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
0.0552 - 643500
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
0.00333 - 35519
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
63000
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4, 25°C
0.065 - 0.521
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
15
2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)
45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02
0.1 - 530
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
0.74 - 14000
2,6-dimethoxyphenol
4.737
2,6-dimethylphthalate
pH and temperature not specified in the publication
-
0.0172
2-dianisidine
-
pH 6.0, 25°C
53
3-dimethylaminobenzoic acid
-
pH 6.0, 25°C
4.3 - 58330
4-hydroxy-3,5-dimethoxybenzaldehyde azine
1.54 - 6.1
4-hydroxybenzoic acid
123
bilirubin
45°C, pH 8.4, LccA protein isolated from Haloferax volcanii H26 strain US02
2.3 - 956
ferrocenemonocarboxylic acid
-
0.0045 - 0.12
hydroquinone
13.3
L-Dopa
-
pH 5.0, temperature not specified in the publication
107 - 388
N,N-dimethyl-1,4-phenylenediamine
102 - 3253
N,N-Dimethyl-p-phenylenediamine
0.089 - 5.187
o-Dianisidine
5.672 - 33000
syringaldazine
388
syringic acid
-
pH 4.5, 25°C
0.33
1-hydroxybenzotriazole
pH 5.0, temperature not specified in the publication, wild-type PM1 laccase
0.84
1-hydroxybenzotriazole
pH 5.0, temperature not specified in the publication
0.64
1-naphthol
pH and temperature not specified in the publication, wild-type enzyme
0.64
1-naphthol
pH and temperature not specified in the publication, mutant enzyme V281A/P309L/S318G/D232V
0.076
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
70°C, pH 3.0
1.72
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH and temperature not specified in the publication
4.331
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH not specified in the publication
15.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C
19.03
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 30°C
29.245
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH not specified in the publication
42
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild-type enzyme, 30°C, pH not specified in the publication
42
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 4.0, wild-type enzyme
74
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 3.5, mutant enzyme H165A/R240H
74
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme H165A/R240H, 30°C, pH not specified in the publication
95
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 3.5, mutant enzyme H165A/M199G
95
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme H165A/M199G, 30°C, pH not specified in the publication
102
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 4.0, mutant enzyme M199A
102
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme M199A, 30°C, pH not specified in the publication
157.86
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH and temperature not specified in the publication
160
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH and temperature not specified in the publication, wild-type enzyme
169
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 3.5, mutant enzyme Y230A
169
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme Y230A, 30°C, pH not specified in the publication
203
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 3.5, mutant enzyme M199G/R240H
203
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme M199G/R240H, 30°C, pH not specified in the publication
226
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
30°C, pH 4.0, mutant enzyme M199G
226
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme M199G, 30°C, pH not specified in the publication
455
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 30°C
620
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH and temperature not specified in the publication, mutant enzyme V281A/P309L/S318G/D232V
6880
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C
7391
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3, temperature not specified in the publication, mutant enzyme V159E
9914.5
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, temperature not specified in the publication
26106
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, temperature not specified in the publication, wild-type PM1 laccase
75500
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3, temperature not specified in the publication, mutant enzyme V159E/N398D
184500
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, temperature not specified in the publication
0.0552
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 6.0, 25°C
0.074
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 6.5, 25°C, mutant P530A
0.133
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 6.5, 25°C, mutant K532E
0.15
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, recombinant Lac1
0.154
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 6.5, 25°C, mutant K532A
0.672
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 25°C, mutant P530A
1.165
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 25°C, mutant K532E
1.73
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 25°C, mutant K532A
1.78
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, recombinant Lac1
2.981
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 25°C, mutant P530A
3.505
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 25°C, mutant K532E
5.05
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
FJ560721
pH 5.0, 22-25°C
6.434
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 25°C, mutant K532A
42.55
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, recombinant Lac1
49.1
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 30°C
222
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 5.0, 25°C
380
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
465.8
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, recombinant Lac1
630
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
recombinant enzyme, pH 3.0, 30°C
1024
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
1085
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
recombinant wild-type enzyme, pH 5.0, temperature not specified in the publication
1300
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
3960
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, temperature not specified in the publication
4780
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 5.0, 25°C
5164
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
recombinant wild-type enzyme, pH 3.0, temperature not specified in the publication
8340
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 50°C
643500
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
in 67 mM sodium acetate buffer (pH 4.5), at 30°C
0.00333
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
laccase DcLac1, pH 2.8, temperature not specified in the publication
0.01477
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
laccase DcLac2, pH 2.8, temperature not specified in the publication
0.19
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 4.0, 35°C
0.42
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, temperature not specified in the publication
7.167
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, isoenzyme Lac4
7.61
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I/V482G (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)
17.6
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
25.625
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 40°C, isoenzyme Lac3
47.82
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 8.0, 85°C
59.6
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I (variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions)
70.5
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
118.28
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 7.0 37°C
120
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188A, in aqueous solution
142.1
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 4.5
163.1
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH and temperature not specified in the publication
210
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188K, in aqueous solution
322
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, wild-type enzyme, in aqueous solution
383
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
21-23°C, pH not specified in the publication, wild-type enzyme
670
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188L, in aqueous solution
750
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188V, in aqueous solution
890
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188I, in aqueous solution
900
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.0, 22°C, mutant enzyme E188R, in aqueous solution
946
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 3.0, 25°C
1596
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4, 30°C
2328
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 22°C
2609
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 3.4, 70°C
2642
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH and temperature not specified in the publication
35519
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 4.0, 25°C
0.065
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant M456A, presence of 0.5 mM Cu2+, 30°C, pH 5
0.085
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
wild-type, 30°C, pH 5
0.437
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
wild-type, presence of 0.5 mM Cu2+, 30°C, pH 5
0.521
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)
mutant M455L, 30°C, pH 5
0.1
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 7.5, 37°C
70
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA))
240
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)) and 6His tagged (C(DELTA)6H)
240
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, deglycosylated enzyme
260
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)), 6His tagged (C(DELTA)6H) and hyper-glycosylated
270
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, wild-type enzyme
530
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
30°C, pH 6.0, C-6His tagged laccase 3
0.74
2,6-dimethoxyphenol
30°C, pH 9.0, mutant enzyme H165A/R240H
0.74
2,6-dimethoxyphenol
mutant enzyme H165A/R240H, 30°C, pH not specified in the publication
1.09
2,6-dimethoxyphenol
wild-type enzyme, 30°C, pH not specified in the publication
1.09
2,6-dimethoxyphenol
30°C, pH 9.0, wild-type enzyme
1.11
2,6-dimethoxyphenol
30°C, pH 6.5, mutant enzyme H165A/M199G
1.11
2,6-dimethoxyphenol
mutant enzyme H165A/M199G, 30°C, pH not specified in the publication
1.375
2,6-dimethoxyphenol
FJ560721
pH 5.0, 22-25°C
1.55
2,6-dimethoxyphenol
30°C, pH 8.0, mutant enzyme M199A
1.55
2,6-dimethoxyphenol
mutant enzyme M199A, 30°C, pH not specified in the publication
2.22
2,6-dimethoxyphenol
30°C, pH 8.5, mutant enzyme Y230A
2.22
2,6-dimethoxyphenol
mutant enzyme Y230A, 30°C, pH not specified in the publication
2.36
2,6-dimethoxyphenol
-
pH 8.0, 70°C
5.07
2,6-dimethoxyphenol
30°C, pH 8.0, mutant enzyme M199G
5.07
2,6-dimethoxyphenol
mutant enzyme M199G, 30°C, pH not specified in the publication
9.102
2,6-dimethoxyphenol
30°C, pH not specified in the publication
10.99
2,6-dimethoxyphenol
-
70°C, pH 6.5
14.4
2,6-dimethoxyphenol
pH and temperature not specified in the publication, wild-type enzyme
14.7
2,6-dimethoxyphenol
-
pH 4.5, 37°C
16.51
2,6-dimethoxyphenol
30°C, pH 8.5, mutant enzyme M199G/R240H
16.51
2,6-dimethoxyphenol
mutant enzyme M199G/R240H, 30°C, pH not specified in the publication
18.5
2,6-dimethoxyphenol
pH 5.0, 30°C
20
2,6-dimethoxyphenol
pH and temperature not specified in the publication, mutant enzyme V281A/P309L/S318G/D232V
21.2
2,6-dimethoxyphenol
21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I/V482G (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)
24.02
2,6-dimethoxyphenol
pH 3.0, 30°C
24.532
2,6-dimethoxyphenol
30°C, pH not specified in the publication
31.7
2,6-dimethoxyphenol
-
pH 4.5, 37°C
37.2
2,6-dimethoxyphenol
21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I (variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions)
42.8
2,6-dimethoxyphenol
-
pH and temperature not specified in the publication
57
2,6-dimethoxyphenol
21-23°C, pH not specified in the publication, wild-type enzyme
75.9
2,6-dimethoxyphenol
-
pH 5.0, temperature not specified in the publication
81
2,6-dimethoxyphenol
recombinant wild-type enzyme, pH 3.0, temperature not specified in the publication
87.05
2,6-dimethoxyphenol
-
pH 8.0, 85°C
90.5
2,6-dimethoxyphenol
pH 8.5, temperature not specified in the publication
113
2,6-dimethoxyphenol
-
pH and temperature not specified in the publication
140
2,6-dimethoxyphenol
recombinant enzyme, pH 3.0, 30°C
157
2,6-dimethoxyphenol
pH 4, 30°C
170
2,6-dimethoxyphenol
-
pH 4.0, 25°C
225
2,6-dimethoxyphenol
pH 5.0, 30°C
228
2,6-dimethoxyphenol
pH 3.0, 30°C
371
2,6-dimethoxyphenol
-
pH 5, temperature not specified in the publication, mutant enzyme V159E
581
2,6-dimethoxyphenol
recombinant wild-type enzyme, pH 5.0, temperature not specified in the publication
905
2,6-dimethoxyphenol
pH 5.0, temperature not specified in the publication
1325
2,6-dimethoxyphenol
pH 5.0, temperature not specified in the publication, wild-type PM1 laccase
1490
2,6-dimethoxyphenol
-
pH 5, temperature not specified in the publication, mutant enzyme V159E/N398D
3500
2,6-dimethoxyphenol
pH and temperature not specified in the publication
14000
2,6-dimethoxyphenol
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
4.3
4-hydroxy-3,5-dimethoxybenzaldehyde azine
pH 5.0, 25°C
74.4
4-hydroxy-3,5-dimethoxybenzaldehyde azine
-
pH and temperature not specified in the publication
1167
4-hydroxy-3,5-dimethoxybenzaldehyde azine
-
pH 5.0, 25°C
3288
4-hydroxy-3,5-dimethoxybenzaldehyde azine
pH 5.0, 25°C
58330
4-hydroxy-3,5-dimethoxybenzaldehyde azine
-
pH 5.0, 25°C
1.54
4-hydroxybenzoic acid
pH 5.0, temperature not specified in the publication, wild-type PM1 laccase
6.1
4-hydroxybenzoic acid
pH 5.0, temperature not specified in the publication
0.011
catechol
-
pH 7.5, 37°C
0.034
catechol
-
pH 7.0 37°C
13
catechol
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
26.5
catechol
pH 5.0, 25°C
30.6
catechol
-
pH 5.0, temperature not specified in the publication
103
catechol
-
pH 5.0, 25°C
1200
catechol
pH and temperature not specified in the publication
1232
catechol
pH 5.0, 25°C
2838
catechol
-
pH 5.0, 25°C
25.1
dopamine
pH 5.0, 25°C
88
dopamine
-
pH 5.0, 25°C
643
dopamine
pH 5.0, 25°C
1208
dopamine
-
pH 5.0, 25°C
2.3
ferrocenemonocarboxylic acid
pH 5.0, 25°C
-
185
ferrocenemonocarboxylic acid
-
pH 5.0, 25°C
-
306
ferrocenemonocarboxylic acid
pH 5.0, 25°C
-
956
ferrocenemonocarboxylic acid
-
pH 5.0, 25°C
-
0.13
ferrocyanide
pH 5.0, 25°C
72
ferrocyanide
-
pH 5.0, 25°C
259
ferrocyanide
-
pH 5.0, 25°C
334
ferrocyanide
pH 5.0, 25°C
0.012
guaiacol
pH 3.0, 30°C
0.181
guaiacol
pH 5.0, 30°C
0.268
guaiacol
pH 3.0, 30°C
0.27
guaiacol
pH and temperature not specified in the publication, wild-type enzyme
0.37
guaiacol
pH and temperature not specified in the publication, mutant enzyme V281A/P309L/S318G/D232V
0.375
guaiacol
pH 4.5, 40°C, isoenzyme Lac3
0.503
guaiacol
pH 4.5, 40°C, isoenzyme Lac4
2.4
guaiacol
-
pH 5.0, 25°C
3.3
guaiacol
pH 6.0, 90°C, mutant enzyme D394R
3.9
guaiacol
recombinant enzyme, pH 3.0, 30°C
4
guaiacol
-
pH 6.0, 25°C
5.17
guaiacol
pH and temperature not specified in the publication
7.9
guaiacol
pH 6.0, 90°C, mutant enzyme D394M
10
guaiacol
-
pH 6.0, 90°C, mutant enzyme K428L
10.1
guaiacol
pH 5.0, temperature not specified in the publication
10.68
guaiacol
-
70°C, pH 6.0
11
guaiacol
-
at 30°C in 100 mM sodium tartrate buffer (pH 4.5)
11.3
guaiacol
22°C, pH 7.0, wild-type enzyme
11.9
guaiacol
pH 5.0, temperature not specified in the publication, wild-type PM1 laccase
12
guaiacol
-
pH 6.0, 90°C, mutant enzyme K428E
12
guaiacol
-
pH 6.0, 90°C, mutant enzyme K428R
12.4
guaiacol
pH 6.0, 90°C, mutant enzyme D394E
14.8
guaiacol
pH 5.0, 30°C
16
guaiacol
-
pH 6.0, 90°C, wild-type enzyme
16.8
guaiacol
pH 6.0, 90°C, mutant enzyme D394N
16.9
guaiacol
pH 6.0, 90°C, wild-type enzyme
17.1
guaiacol
pH 6.0, 90°C, mutant enzyme D396N
19.34
guaiacol
-
pH 8.0, 85°C
19.4
guaiacol
pH 6.0, 90°C, mutant enzyme D396E
20.5
guaiacol
pH 6.0, 90°C, mutant enzyme D396M
21.8
guaiacol
pH 6.0, 90°C, mutant enzyme D396A
22
guaiacol
-
pH 6.0, 90°C, mutant enzyme K428M
26.6
guaiacol
pH 8.5, temperature not specified in the publication
28.5
guaiacol
22°C, pH 7.0, mutant enzyme L386Q/G417I/V482G (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)
38
guaiacol
-
pH 4.0, 25°C
41.3
guaiacol
pH 3.0, 30°C
48.7
guaiacol
-
pH 5.0, temperature not specified in the publication
81
guaiacol
-
pH and temperature not specified in the publication
168
guaiacol
-
pH 6.0, 25°C
200.51
guaiacol
pH 5.0, temperature not specified in the publication
271
guaiacol
22°C, pH 7.0, mutant enzyme L386Q/G417I (variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions)
400
guaiacol
pH and temperature not specified in the publication
0.0045
hydroquinone
-
pH 7.5, 37°C
0.12
hydroquinone
-
pH 7.0 37°C
0.02
K4[Fe(CN)6]
pH 4.0, temperature not specified in the publication
144
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme H165A/M199G
155
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme M199A
160
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme H165A/R240H
261
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme M199G
278
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme Y230A
279
K4[Fe(CN)6]
30°C, pH 4.0, mutant enzyme M199G/R240H
383
K4[Fe(CN)6]
30°C, pH 4.0, wild-type enzyme
107
N,N-dimethyl-1,4-phenylenediamine
-
pH 4, temperature not specified in the publication, mutant enzyme V159E
388
N,N-dimethyl-1,4-phenylenediamine
-
pH 4, temperature not specified in the publication, mutant enzyme V159E/N398D
102
N,N-Dimethyl-p-phenylenediamine
pH 4.0, temperature not specified in the publication, wild-type PM1 laccase
3253
N,N-Dimethyl-p-phenylenediamine
pH 4.0, temperature not specified in the publication
0.089
o-Dianisidine
30°C, pH not specified in the publication
5.187
o-Dianisidine
30°C, pH not specified in the publication
621
Sinapic acid
recombinant wild-type enzyme, pH 3.0, temperature not specified in the publication
1662
Sinapic acid
recombinant wild-type enzyme, pH 5.0, temperature not specified in the publication
5.672
syringaldazine
30°C, pH not specified in the publication
28.5
syringaldazine
-
pH 6.0, 50°C
29.2
syringaldazine
-
pH 6.0, 50°C
82.936
syringaldazine
30°C, pH not specified in the publication
219.6
syringaldazine
pH 4.5, 40°C, isoenzyme Lac4
367.36
syringaldazine
pH 4.5, 40°C, isoenzyme Lac3
628
syringaldazine
45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02
3000
syringaldazine
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA))
5360
syringaldazine
-
pH 4.0, 25°C
13783
syringaldazine
-
pH 8.0, 22°C
16000
syringaldazine
30°C, pH 6.0, deglycosylated enzyme
20000
syringaldazine
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)) and 6His tagged (C(DELTA)6H) and hyper-glycosylated
23000
syringaldazine
30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)) and 6His tagged (C(DELTA)6H)
31000
syringaldazine
30°C, pH 6.0, C-6His tagged laccase 3
33000
syringaldazine
30°C, pH 6.0, wild-type enzyme
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N398D
-
twice better activity at pH 6 and 1.2fold improvement at pH 3
V159E
-
two-fold improvement in the laccase activity detected at pH 3 and 6. Lower thermotolerance than native enzyme
V159E/N398D
-
1.4fold higher activity than mutant enzyme V159E and 2.6fold higher activity than mutant enzyme N398D with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as substrate. Lower thermotolerance than native enzyme
V159E/N398D/I453F/M454L
-
parental-like activity at both pH values. Lower thermotolerance than native enzyme
V159E/N398D/I453L/M454L
-
1.3fold TAI at pH 3 and lower activity (0.8fold) than mutant enzyme V159E/N398D. Lower thermotolerance than native enzyme
N398D
-
twice better activity at pH 6 and 1.2fold improvement at pH 3
-
V159E
-
two-fold improvement in the laccase activity detected at pH 3 and 6. Lower thermotolerance than native enzyme
-
V159E/N398D
-
1.4fold higher activity than mutant enzyme V159E and 2.6fold higher activity than mutant enzyme N398D with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as substrate. Lower thermotolerance than native enzyme
-
V159E/N398D/I453F/M454L
-
parental-like activity at both pH values. Lower thermotolerance than native enzyme
-
V159E/N398D/I453L/M454L
-
1.3fold TAI at pH 3 and lower activity (0.8fold) than mutant enzyme V159E/N398D. Lower thermotolerance than native enzyme
-
D501G
-
better stability and catalytic efficiency than wild-type enzyme
D500G
in Pichia pastoris 9.3folds higher expression than wild-type enzyme
K316N
11.4-fold higher expression level. High dimerization of phenolic and decolorization of industrial dyes
L386Q/G417I
variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions. The mutant enzyme exhibits 9-fold higher guaiacol oxidation rates in the lysate compared to the strain expressing the wild-type enzyme
L386Q/G417I/V482G
variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions. The mutant enzyme exhibits 14-fold higher guaiacol oxidation rates in the lysate compared to the strain expressing the wild-type enzyme. The decline in relative activity from the maximum at pH 4 towards more alkaline pH values is sharper for the mutant enzyme compared to the wild-type with 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid). The mutant enzyme has an increased activity towards the lignin-like model compound guaiacol while retaining the very good thermostability and activity at neutral-to-basic pH of the wild-type enzyme
E188A
in comparison with the wild type, the mutant enzyme shows an increase in Km value and a decrease in kcat. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol)
E188I
in comparison with the wild type, the mutant enzyme shows an increase in kcat and catalytic efficiency values and a decrease in Km. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol)
E188K
in comparison with the wild type, the mutant enzyme shows an increase in Km value and a decrease in kcat. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol)
E188L
in comparison with the wild type, the mutant enzyme shows an increase in kcat and catalytic efficiency values and a decrease in Km. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol)
E188R
in comparison with the wild type, the mutant enzyme shows an increase in kcat and catalytic efficiency values and a decrease in Km, In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol)
E188V
in comparison with the wild type, the mutant enzyme shows an increase in kcat and catalytic efficiency values and a decrease in Km. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol)
E188A
-
in comparison with the wild type, the mutant enzyme shows an increase in Km value and a decrease in kcat. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol)
-
E188I
-
in comparison with the wild type, the mutant enzyme shows an increase in kcat and catalytic efficiency values and a decrease in Km. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol)
-
E188L
-
in comparison with the wild type, the mutant enzyme shows an increase in kcat and catalytic efficiency values and a decrease in Km. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol)
-
E188R
-
in comparison with the wild type, the mutant enzyme shows an increase in kcat and catalytic efficiency values and a decrease in Km, In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol)
-
E188V
-
in comparison with the wild type, the mutant enzyme shows an increase in kcat and catalytic efficiency values and a decrease in Km. In comparison with the wild type, the mutant enzyme shows increased stability to organis solvents (ethanol, methanol, 1-propanol)
-
H497A
-
copper center, no significant changes
I494A
-
site-directed mutagenesis at a hydrophobic residue in the vicinity of the type 1 copper site, the replacement of Ile494 by an alanine residue leads to significant changes in the enzyme, the mutant shows differences in the type 1 as well as in the type 2 copper centre compared to the wild-type enzyme
L386A
-
the site-directed mutation of Leu386, a hydrophobic residue in the vicinity of the type 1 copper site, to an alanine residue appears to cause only very subtle alterations in the properties of the enzyme indicating minimal changes in the structure of the copper centres
degradation
-
the highest biodegradation of the toxic organochlorine pesticide pentachlorophenol (PCP) is of 23% at pollutant concentration of 100 mg/l, which evidences that the thermostable enzyme acts directly in degradation of pentachlorophenol and may be a useful asset to remediate this pollutant
environmental protection
-
the highest biodegradation of the toxic organochlorine pesticide pentachlorophenol (PCP) is of 23% at pollutant concentration of 100 mg/l, which evidences that the thermostable enzyme acts directly in degradation of pentachlorophenol and may be a useful asset to remediate this pollutant
degradation
-
the highest biodegradation of the toxic organochlorine pesticide pentachlorophenol (PCP) is of 23% at pollutant concentration of 100 mg/l, which evidences that the thermostable enzyme acts directly in degradation of pentachlorophenol and may be a useful asset to remediate this pollutant
-
environmental protection
-
the highest biodegradation of the toxic organochlorine pesticide pentachlorophenol (PCP) is of 23% at pollutant concentration of 100 mg/l, which evidences that the thermostable enzyme acts directly in degradation of pentachlorophenol and may be a useful asset to remediate this pollutant
-
D360M
mutation at sites Cu5
D439A/M510L
140fold and 44fold increases in the kcat values for ABTS and 2,5-diaminotoluene, redox potential is 0.39 V
D439A/M510Q
redox potential of the mutant s 0.21 V
D439A/P444A
40fold increase in the ABTS-oxidizing activity, redox potential is 0.46 V
D439A/P444A/M510L
T1 copper in the triple mutant cannot be fully oxidized resulting in loss of enzymatic activities
D439A/P444A/M510Q
redox potential of the mutant was 0.26 V and high enzymatic activities are not attained
D507A
about 10% increase in specific activity activity
D507N
about 80% increase in specific activity activity
E506A
mutation results in the formation of a compensatory hydrogen bond network with one or two extra water molecules
E506D
about 20% decrease in specific activity activity
E506I
mutation results in the complete shutdown of the hydrogen bond network leading to loss of enzymatic activities
E506Q
mutation results in the hydrogen bond network without the proton transport function
G304K
mutant shows about 2.7fold increased the laccase activity. Movements of the regulatory loop combined with the changes of the methionine-rich region may uncover the T1 Cu site allowing greater access of the substrate
M355L/D360N
mutation at sites Cu5
M358S/M362S
mutation at sites Cu6
M358S/M362S/M364S/M368S
mutations at sites Cu6,7
M364S/M368S
mutation at sites Cu7
M510L
3.8-4.2 copper atoms per protein molecule, similar to wild-type, redox potential is 0.40 V
M510Q
3.8-4.2 copper atoms per protein molecule, similar to wild-type, redox potential is 0.23 V
P444A/D439A
mutation leads to a synergetic effect of the positive shift in the redox potential of the type I copper center and the increase in enzyme activity
P444A/M510L
enzymatic activities similar to wild-type
P444A/M510Q
3.4 copper atoms per protein molecule, similar to wild-type, redox potential is 0.21 V, no oxidizing activity of ABTS is observed
P444G
mutation results in positive shifts in the redox potential of this copper center and enhanced oxidase activity in CueO and in the region Pro357-His406 deletion mutant lacking a methionine-rich helical segment that covers the substrate-binding site
P444I
positive shift in the redox potential of this copper center and enhanced oxidase activity
P444L
positive shift in the redox potential of this copper center and enhanced oxidase activity
Q106F
-
mutation enhanced CueO oxidation activity
L559A
the C-terminal mutation affects the trinuclear site geometry of the mutant enzyme, which also shows 3-4fold reduced activity compared to the wild-type enzyme
K532A
site-directed mutagenesis, the mutant shows increased catalytic efficiency and altered substrate specificity compared to the wild-type enzyme
K532E
site-directed mutagenesis, the mutant shows increased catalytic efficiency and altered substrate specificity compared to the wild-type enzyme
K532R
site-directed mutagenesis, inactive mutant
P530A
site-directed mutagenesis, the mutant shows increased catalytic efficiency and altered substrate specificity compared to the wild-type enzyme
D205R
site-directed mutagenesis, the mutation in a highly conserved region perturbs the structural local environment in POXA1b, leading to a large rearrangement of the enzyme structure. The mutant shows highly reduced activity compared to the wild-type enzyme and is inactive with substrate syringaldazine
L466V/E467S/A468G
-
triple mutation: changes in pH optimum, redox potential, Km, kcat and fluoride inhibition
L470F
-
no significant changes
Y108A
Tyr108 does form an integral part of the active site and affects enzyme kinetics
Y108F
Tyr108 does form an integral part of the active site and affects enzyme kinetics
Y229A
over 10fold increase in activity
Y108A
-
Tyr108 does form an integral part of the active site and affects enzyme kinetics
-
Y108F
-
Tyr108 does form an integral part of the active site and affects enzyme kinetics
-
Y229A
-
over 10fold increase in activity
-
H165A/M199G
2.3fold increase in kcat/Km towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
M199G/H165A
2.3fold increase in kcat/Km for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid). kcat/Km for 2,6-dimethoxyphenol is identical to kcat/Km of wilde-type enzyme. 2.7fold decrease in kcat/Km for K4[Fe(CN)6]. Drastic shift in the optimal pH of 2,6-dimethoxyphenol oxidation
M199G
-
5.4fold increase in kcat/Km for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid). 4.7fold increase in kcat/Km for 2,6-dimethoxyphenol. 1.5fold decrease in kcat/Km for K4[Fe(CN)6]
-
L513F
-
no significant changes
V509L/S510E/G511A
-
triple mutation: changes in pH optimum, redox potential, Km, kcat and fluoride inhibition
D394E
mutant with the lower laccase activity displays a decreased decolorization efficiency as compared to the wild-type enzyme. Expressed in a lower level, about 50%, of the wild type enzyme. Optimum pH shifts towards the acidic value (0.5-1 units) relative to the wild type enzyme which has an optimal pH 6.0
D394M
mutant with the lower laccase activity displays a decreased decolorization efficiency as compared to the wild-type enzyme. Expressed in a lower level, about 50%, of the wild type enzyme. Optimum pH shifts towards the acidic value (0.5-1 units) relative to the wild type enzyme which has an optimal pH 6.0
D394R
mutant with the lower laccase activity displays a decreased decolorization efficiency as compared to the wild-type enzyme. Expressed in a lower level, about 16%, of the wild type enzyme. Optimum pH shifts towards the acidic value (0.5-1 units) relative to the wild type enzyme which has an optimal pH 6.0
D396A
mutant enzyme with higher catalytic efficiency decolorizes the synthetic dye more efficiently than the wild-type enzyme
D396E
mutant enzyme with higher catalytic efficiency decolorizes the synthetic dye more efficiently than the wild-type enzyme
D396M
mutant enzyme with higher catalytic efficiency decolorizes the synthetic dye more efficiently than the wild-type enzyme
K428E
-
1.3fold decrease in kcat/Km for the substrate guaiacol
K428L
-
1.6fold decrease in kcat/Km for the substrate guaiacol. 70% decrease in activity of mutant enzyme after 4 h at 80°C. 30% decrease in activity of wild-type enzyme after 4 h at 80°C
K428M
-
1.4fold increase in kcat/Km for the substrate guaiacol
K428R
-
1.3fold decrease in kcat/Km for the substrate guaiacol
M455L
mutation in T1 Cu site, incorporation of 3-4 copper atoms, similar to wild-type. Mutation results in an increase of 100 mV in the O2 reduction potential, while the enzymatic activity for ABTS oxidation is decreased
M456A
mutation in T1 Cu site, incorporation of 3-4 copper atoms, similar to wild-type
D394E
-
mutant with the lower laccase activity displays a decreased decolorization efficiency as compared to the wild-type enzyme. Expressed in a lower level, about 50%, of the wild type enzyme. Optimum pH shifts towards the acidic value (0.5-1 units) relative to the wild type enzyme which has an optimal pH 6.0
-
D394M
-
mutant with the lower laccase activity displays a decreased decolorization efficiency as compared to the wild-type enzyme. Expressed in a lower level, about 50%, of the wild type enzyme. Optimum pH shifts towards the acidic value (0.5-1 units) relative to the wild type enzyme which has an optimal pH 6.0
-
D394R
-
mutant with the lower laccase activity displays a decreased decolorization efficiency as compared to the wild-type enzyme. Expressed in a lower level, about 16%, of the wild type enzyme. Optimum pH shifts towards the acidic value (0.5-1 units) relative to the wild type enzyme which has an optimal pH 6.0
-
D396A
-
mutant enzyme with higher catalytic efficiency decolorizes the synthetic dye more efficiently than the wild-type enzyme
-
D396M
-
mutant enzyme with higher catalytic efficiency decolorizes the synthetic dye more efficiently than the wild-type enzyme
-
K428E
-
1.3fold decrease in kcat/Km for the substrate guaiacol
-
K428L
-
1.6fold decrease in kcat/Km for the substrate guaiacol. 70% decrease in activity of mutant enzyme after 4 h at 80°C. 30% decrease in activity of wild-type enzyme after 4 h at 80°C
-
K428M
-
1.4fold increase in kcat/Km for the substrate guaiacol
-
K428R
-
1.3fold decrease in kcat/Km for the substrate guaiacol
-
A240P
site-directed mutagenesis
D341N
site-directed mutagenesis the D3 domain coil, surface, the mutant shows H bonding with surrounding residue N340 in contrast to the wild-type enzyme
N208S |
site-directed mutagenesis in the D2 domain beta sheet, near D206 (responsible for binding phenolic substrates at the T1 site), the mutant shows increased H bonding with surrounding residues
N331D
site-directed mutagenesis the D3 domain beta sheet substrate binding loop, contiguous to F332 key residue of the binding pocket, the mutant shows increased H bonding with surrounding residues
R280H |
site-directed mutagenesis in the D2 domain end of distal beta sheet, surface, the mutant shows reduced H bonding with surrounding residues
A240P
-
site-directed mutagenesis
-
D341N
-
site-directed mutagenesis the D3 domain coil, surface, the mutant shows H bonding with surrounding residue N340 in contrast to the wild-type enzyme
-
D206A
site-directed mutagenesis, the Asn mutation leads to a significant shift of pH optimum for activity with 2,6-dimethoxyphenol, the mutant shows several fold increased activity compared to the wild-type enzyme
D206E
site-directed mutagenesis, the Asn mutation leads to a significant shift of pH optimum for activity with 2,6-dimethoxyphenol, the mutant shows several fold increased activity compared to the wild-type enzyme
D206N
site-directed mutagenesis, the Asn mutation leads to a significant shift of pH optimum for activity with 2,6-dimethoxyphenol, the mutant shows several fold increased activity compared to the wild-type enzyme
V281A/P309L/S318G/D232V
the expression of the optimized mutant enzyme increases by 22% compared to the unoptimized enzyme and the optimal reaction temperature of the mutant enzyme is 5°C higher than that of the recombinant wild-type enzyme rlac1338, and the optimal pH increases by 0.5 units. The thermal stability and pH stability of the mutant enzyme lac2-9 are improved. 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) is the most suitable substrate for the recombinant enzyme and mutant enzyme. In addition, the Km of the mutant strain lac2-9 (76 mM) is significantly lower, but the kcat/Km (0.618 /s*M) is significantly higher, and the specific enzyme activity (79.8 U/mg) increases by 3.5 times compared with the recombinant laccase (22.8 U/mg). Compared to the rlac1338, the degradation rates with the simultaneous addition of Ca2+ and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) of mutant enzyme lac2-9 for acid violet 7, bromophenol blue and coomassie brilliant blue significantly improved by 8.3, 3.4 and 3.4 times
M502F
-
site-directed mutagenesis, the mutation of the weak so-called axial ligand of the T1 copper site leads to an increase in the redox potential by approximately 100 mV relative to that of the wild-type enzyme, the mutant shows 10% and 0.15-0.05% activity for the non-phenolic substrates and for the phenolic substrates, respectively, compared with the wild-type enzyme
M502F
-
mutations leads to an increase in the redox potential by approx. 100 mV, decrease in the catalytic efficiency, decrease in thermodynamic stability
M502F
-
replacement of Met502, which is weakly co-ordinating to the T1 copper, in CotA laccase by the non-co-ordinating residues leucine and phenylalanine allows the maintenance of the T1 copper geometry while causing an increase in the redox potential
M502L
-
copper center, no significant changes
M502L
-
site-directed mutagenesis, the mutation of the weak so-called axial ligand of the T1 copper site leads to an increase in the redox potential by approximately 100 mV relative to that of the wild-type enzyme, the mutant exhibits a twofold to fourfold decrease in the kcat
M502L
-
mutations leads to an increase in the redox potential by approx. 100 mV, decrease in the catalytic efficiency, decrease in thermodynamic stability
M502L
-
replacement of Met502, which is weakly co-ordinating to the T1 copper, in CotA laccase by the non-co-ordinating residues leucine and phenylalanine allows the maintenance of the T1 copper geometry while causing an increase in the redox potential
D439A
3.8-4.2 copper atoms per protein molecule, similar to wild-type, redox potential is 0.43 V compared to 0.36 for wild-type
D439A
positive shift in the redox potential of this copper center and enhanced oxidase activity
P444A
3.8-4.2 copper atoms per protein molecule, similar to wild-type, redox potential is 0.43 V
P444A
positive shift in the redox potential of this copper center and enhanced oxidase activity
E106F
-
site-directed mutagenesis with additional deletion of residues L351-G378, the mutant WlacD shows 3.5fold increased activity and enhanced thermal stability compared to the wild-type enzyme
E106F
-
site-directed mutagenesis, the mutant WlacS shows 2.2fold increased activity compared to the wild-type enzyme
E106F
-
mutation promotes both enzymatic activity and thermostability
H165A/R240H
1.8 fold increase in kcat/Km towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
H165A/R240H
4.8fold increase in kcat/Km for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid). 15.1fold increase in kcat/Km for 2,6-dimethoxyphenol. 1.4fold decrease in kcat/Km for K4[Fe(CN)6]
M199A
2.4fold increase in kcat/Km for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid). 1.4fold increase in kcat/Km for 2,6-dimethoxyphenol. 2.5fold decrease in kcat/Km for K4[Fe(CN)6]
M199A
2.4fold increase in kcat/Km towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
M199G
5.4fold increase in kcat/Km for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid). 4.7fold increase in kcat/Km for 2,6-dimethoxyphenol. 1.5fold decrease in kcat/Km for K4[Fe(CN)6]
M199G
5.4fold increase in kcat/Km towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
M199G/R240H
1.8fold increase in kcat/Km for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid). 1.5fold decrease in kcat/Km for 2,6-dimethoxyphenol. 2.4fold decrease in kcat/Km for K4[Fe(CN)6]. Combination of substitutions in the substrate-binding pocket and in the tunnel leading to Cu2+ ion increases the catalytic activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) by 5fold, and towards 2,6-dimethoxyphenol by 16fold
M199G/R240H
mutation increases catalytic activity of the enzyme towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) by 5fold, and towards 2,6-dimethoxyphenol by 16fold. Prospective 2D laccase variant with the highest activity under alkaline conditions
Y230A
4.02fold increase in kcat/Km for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid). 2fold increase in kcat/Km for 2,6-dimethoxyphenol. 1.4fold decrease in kcat/Km for K4[Fe(CN)6]
Y230A
4.0fold increase in kcat/Km towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
M199A
-
2.4fold increase in kcat/Km for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid). 1.4fold increase in kcat/Km for 2,6-dimethoxyphenol. 2.5fold decrease in kcat/Km for K4[Fe(CN)6]
-
M199A
-
2.4fold increase in kcat/Km towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
Y230A
-
4.02fold increase in kcat/Km for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid). 2fold increase in kcat/Km for 2,6-dimethoxyphenol. 1.4fold decrease in kcat/Km for K4[Fe(CN)6]
-
Y230A
-
4.0fold increase in kcat/Km towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
P394H
site-directed mutagenesis
P394H
site-directed mutagenesis the D3 domain coil substrate binding loop, contiguous to H395, T1 Cu ligand, the mutant shows H bonding with surrounding residue S427 in contrast to the wild-type enzyme
P394H
-
site-directed mutagenesis
-
P394H
-
site-directed mutagenesis the D3 domain coil substrate binding loop, contiguous to H395, T1 Cu ligand, the mutant shows H bonding with surrounding residue S427 in contrast to the wild-type enzyme
-
additional information
deletion of the region Pro357-His406 comprising a methionine-rich helical segment that covers the substrate-binding site and replacement with a Gly-Gly linker. The scaffold of the CueO molecule and metal-binding sites are reserved in the mutant. The high thermostability of the protein molecule and its spectroscopic and magnetic properties are also conserved after truncation. The cuprous oxidase activity of the mutant is reduced to about 10% that of recombinant CueO due to the decrease in the affinity of the labile Cu site for Cu(I) ions
additional information
-
deletion of the region Pro357-His406 comprising a methionine-rich helical segment that covers the substrate-binding site and replacement with a Gly-Gly linker. The scaffold of the CueO molecule and metal-binding sites are reserved in the mutant. The high thermostability of the protein molecule and its spectroscopic and magnetic properties are also conserved after truncation. The cuprous oxidase activity of the mutant is reduced to about 10% that of recombinant CueO due to the decrease in the affinity of the labile Cu site for Cu(I) ions
additional information
mutations at Pro444 to construct a second NH-S hydrogen bond between the backbone amide and coordinating Cys500 thiolate of the type I copper result in positive shifts in the redox potential of this copper center and enhanced oxidase activity in CueO. Pro444 mutations limit the incorporation of copper ions into the trinuclear copper center. The activities of both CueO and the region Pro357-His406 deletion mutant are also enhanced by mutations to break down the hydrogen bond between the imidazole group of His443 that is coordinated to the type I copper and the beta-carboxy group of Asp439 that is located in the outer sphere of the type I copper center. The characteristics of the Cu(II)-S(Cys) bond are only minimally perturbed by mutations involving formation or disruption of a hydrogen bond from the coordinating groups to the type I copper
additional information
-
mutations at Pro444 to construct a second NH-S hydrogen bond between the backbone amide and coordinating Cys500 thiolate of the type I copper result in positive shifts in the redox potential of this copper center and enhanced oxidase activity in CueO. Pro444 mutations limit the incorporation of copper ions into the trinuclear copper center. The activities of both CueO and the region Pro357-His406 deletion mutant are also enhanced by mutations to break down the hydrogen bond between the imidazole group of His443 that is coordinated to the type I copper and the beta-carboxy group of Asp439 that is located in the outer sphere of the type I copper center. The characteristics of the Cu(II)-S(Cys) bond are only minimally perturbed by mutations involving formation or disruption of a hydrogen bond from the coordinating groups to the type I copper
additional information
construction of a chimeric form of lcc1, CaMV35Sp:clcc1
additional information
-
construction of a chimeric form of lcc1, CaMV35Sp:clcc1
additional information
-
laccase Lcc4/1, composed of the N-terminus of the Lcc4 and the C-terminus of the Lcc1 laccases
additional information
laccase Lcc4/1, composed of the N-terminus of the Lcc4 and the C-terminus of the Lcc1 laccases
additional information
-
laccase Lcc4/1, composed of the N-terminus of the Lcc4 and the C-terminus of the Lcc1 laccases. The fusion enzyme is more efficient, compared to Lcc1, in decolorizing RBBR and poly-R478, even if the latter is only in the presence of a redox mediator
additional information
laccase Lcc4/1, composed of the N-terminus of the Lcc4 and the C-terminus of the Lcc1 laccases. The fusion enzyme is more efficient, compared to Lcc1, in decolorizing RBBR and poly-R478, even if the latter is only in the presence of a redox mediator
additional information
-
construction of a chimeric form of lcc1, CaMV35Sp:clcc1
-
additional information
elimination of the N-terminal sequence in mutant rMmPPOA-637 decreases the specific activity 15fold, which is partially restored in the presence of 1 M NaCl, and alters the secondary and tertiary structures and the pH dependence of optimal stability
additional information
-
elimination of the N-terminal sequence in mutant rMmPPOA-637 decreases the specific activity 15fold, which is partially restored in the presence of 1 M NaCl, and alters the secondary and tertiary structures and the pH dependence of optimal stability
additional information
-
elimination of the N-terminal sequence in mutant rMmPPOA-637 decreases the specific activity 15fold, which is partially restored in the presence of 1 M NaCl, and alters the secondary and tertiary structures and the pH dependence of optimal stability
-
additional information
deletion of the last four amino acids dramatically affected the activity of the enzyme, as the deletion mutant delDSGL559 is practically inactive
additional information
-
deletion of the last four amino acids dramatically affected the activity of the enzyme, as the deletion mutant delDSGL559 is practically inactive
additional information
construction and generation of C-terminal truncation mutants lacking 1, 2, 5, 8, 11, 14 or 18 amino acid residues
additional information
-
construction and generation of C-terminal truncation mutants lacking 1, 2, 5, 8, 11, 14 or 18 amino acid residues
additional information
deletion of the C-terminal extension of 4 or 16 amino acids leads to truncated mutants which lose the high stability at pH 10, while they show an increased stability at pH 5.0, the thermostability is unaltered compared to the wild-type enzyme
additional information
-
generation of a truncation mutant lacking the first 31 amino acid residues, the mutant protein displays a better thermostability, with a half life of over 400 min at 37°C, is less sensitive to chloride and more stable at pH 7.0 compared to the wild--type enzyme
additional information
-
an alkaline laccase mutant form is chosen and further evolved for the synthesis of the C-N polydye at basic pHs. Over 11500 clones derived form 3 rounds of directed and focused evolution are screened through a high-throughput colorimetric assay, and a variant with 3.5-fold improved activity relative to that of the wild type is selected
additional information
-
construction of a two-type domain laccase from a three-type domain laccase by eliminating the signal sequence domain
additional information
replacement of the native PcL signal peptide by the alpha-factor preproleader, and subjected to six rounds of evolution coupled to a multiscreening assay based on the oxidation of natural and synthetic redox mediators at more neutral pHs. The sequence encoding the evolved alpha-factor preproleader of 7A9 for secretion in Sacchaaromyces cerevisiae is replaced by the 24-amino-acid glucoamylase preprosequence from Aspergillus niger, under the Emericella nidulans gpd promoter and trpC terminator. Total laccase activity is enhanced 8000fold, the evolved alpha-factor preproleader improves secretion levels 40fold, and several mutations in mature laccase provide a 13.7fold increase in kcat. While the pH activity profile is shifted to more neutral values, the thermostability and the broad substrate specificity of PcL are retained. Mutational effect on laccase secretion, overview
additional information
-
replacement of the native PcL signal peptide by the alpha-factor preproleader, and subjected to six rounds of evolution coupled to a multiscreening assay based on the oxidation of natural and synthetic redox mediators at more neutral pHs. The sequence encoding the evolved alpha-factor preproleader of 7A9 for secretion in Sacchaaromyces cerevisiae is replaced by the 24-amino-acid glucoamylase preprosequence from Aspergillus niger, under the Emericella nidulans gpd promoter and trpC terminator. Total laccase activity is enhanced 8000fold, the evolved alpha-factor preproleader improves secretion levels 40fold, and several mutations in mature laccase provide a 13.7fold increase in kcat. While the pH activity profile is shifted to more neutral values, the thermostability and the broad substrate specificity of PcL are retained. Mutational effect on laccase secretion, overview
additional information
-
replacement of the native PcL signal peptide by the alpha-factor preproleader, and subjected to six rounds of evolution coupled to a multiscreening assay based on the oxidation of natural and synthetic redox mediators at more neutral pHs. The sequence encoding the evolved alpha-factor preproleader of 7A9 for secretion in Sacchaaromyces cerevisiae is replaced by the 24-amino-acid glucoamylase preprosequence from Aspergillus niger, under the Emericella nidulans gpd promoter and trpC terminator. Total laccase activity is enhanced 8000fold, the evolved alpha-factor preproleader improves secretion levels 40fold, and several mutations in mature laccase provide a 13.7fold increase in kcat. While the pH activity profile is shifted to more neutral values, the thermostability and the broad substrate specificity of PcL are retained. Mutational effect on laccase secretion, overview
-
additional information
-
enzyme adsorption to cellulose fibers from cotton and denim, attachment of PEG of 1.1-5.0 kDa to the purified enzyme, overview
additional information
a variant deleted of the last 13 residues (C(DELTA)) and its 6His tagged counterpart (C(DELTA)6H) are active enzymes. The production of C(DELTA)6H results in the synthesis of a unusually high proportion of highly glycosylated forms of the enzyme therefore allowing the additional purification of a hyper-glycosylated form of C(DELTA)6H noted C(DELTA)6Hh. Properties of (C(DELTA)), C(DELTA)6H and C(DELTA)6Hh are compared. Catalytic efficiency of C(DELTA) (kcat/KM) decreases 4fold (with syringaldazine as substrate) and 10fold (with 2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as substrate) respectively. The catalytic parameters kcat and KM of C(DELTA)6H and C(DELTA)6Hh are strictly comparable revealing that over-glycosylation does not affect the enzyme catalytic efficiency. To the contrary, in vitro deglycosylation of laccase drastically reduces its activity
additional information
-
a variant deleted of the last 13 residues (C(DELTA)) and its 6His tagged counterpart (C(DELTA)6H) are active enzymes. The production of C(DELTA)6H results in the synthesis of a unusually high proportion of highly glycosylated forms of the enzyme therefore allowing the additional purification of a hyper-glycosylated form of C(DELTA)6H noted C(DELTA)6Hh. Properties of (C(DELTA)), C(DELTA)6H and C(DELTA)6Hh are compared. Catalytic efficiency of C(DELTA) (kcat/KM) decreases 4fold (with syringaldazine as substrate) and 10fold (with 2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as substrate) respectively. The catalytic parameters kcat and KM of C(DELTA)6H and C(DELTA)6Hh are strictly comparable revealing that over-glycosylation does not affect the enzyme catalytic efficiency. To the contrary, in vitro deglycosylation of laccase drastically reduces its activity
additional information
-
a variant deleted of the last 13 residues (C(DELTA)) and its 6His tagged counterpart (C(DELTA)6H) are active enzymes. The production of C(DELTA)6H results in the synthesis of a unusually high proportion of highly glycosylated forms of the enzyme therefore allowing the additional purification of a hyper-glycosylated form of C(DELTA)6H noted C(DELTA)6Hh. Properties of (C(DELTA)), C(DELTA)6H and C(DELTA)6Hh are compared. Catalytic efficiency of C(DELTA) (kcat/KM) decreases 4fold (with syringaldazine as substrate) and 10fold (with 2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as substrate) respectively. The catalytic parameters kcat and KM of C(DELTA)6H and C(DELTA)6Hh are strictly comparable revealing that over-glycosylation does not affect the enzyme catalytic efficiency. To the contrary, in vitro deglycosylation of laccase drastically reduces its activity
-
additional information
-
evaluation of the oxidation and decolorization of azo dyes by the enzyme through co-immobilization of enzyme and dye on an electrode, mechanism of electron transfer, overview
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0 - 25
-
purified recombinant enzyme, stable
0 - 50
-
purified enzyme, stable
10
-
1 h, 5% loss of activity
10 - 30
-
at pH 6, the rate of inactivation increases as the temperature is elevated from 10 to 60°C, with good stability observed in the range of 10 to 30°C
20 - 30
16 h, less than 5% loss of activity
20 - 50
-
purified enzyme, 90 min, completely stable
20 - 70
temperature stability profiles of native and deglycosylated enzymes, overview
20 - 80
stable from 20°C-80°C
22
-
50 h, about 55% loss of activity
25 - 35
-
2 h, residual enzyme activities are more than 90%
25 - 65
-
half-life of 81 min at 25°C, 77 min at 35°C, 64 min at 45°C, 36 min at 55°C, and 21 min at 65°C
25 - 70
stable at, inactivation above
30 - 60
-
stability between 30°C and 60°C with a maximum at 50°C
4 - 45
the enzyme is most stable between 4°C and room temperature. After 288 h, the recovered activities correspond to approximately 51% at 4°C, 57% at 15°C and 49% at room temperature of the initial activity. The laccase is nearly completely inactivated at 35°C after 288 h and at 45°C after 24 h
4 - 70
-
after 24 h incubation at pH 4.8 and 4°C, 80% of the initial activity remains. After 1 h incubation, the enzyme shows about 100% activity at 4°C, about 90% activity at 30°C, about 75% activity at 40°C, about 50% activity at 50°C, about 5% activity at 60°C, and no activity at 70°C
40 - 50
-
most stable at a temperature range of 40-50°C
45 - 50
the enzyme retains 35 to 60% of its activity at 45°C to 50°C after incubation for 2.5 days
45 - 52
-
melting temperature in presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol
45 - 55
-
2 h, the enzyme retains more than 60% of its activity
45 - 70
-
the enzyme is activated by 10 min of preincubation at 45-70°C, but higher temperatures promote inactivation
50 - 70
-
the enzyme retains activity after incubation at 50°C for 1 h, but the activity sharply decreases when the temperature is increased to 60°C and almost no activity is detected at 70°C. The laccase can still oxidize 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) when incubated at 70°C for 5 min, but when the enzyme is incubated under the same condition without substrate, it loses almost all its activity
50 - 80
the Lac activity of Lac1 remains 80% after incubation at 50°C for 30 min. However, incubated at 60°C, the remaining activity declines in less than 80%. The enzyme is inactive at 70-80°C
61.7
-
T50-value, mutant enzyme V159E/N398D/I453F/M454L
62.5
-
T50-value, mutant enzyme V159E/N398D/I453L/M454L
65 - 75
-
2 h, the enzyme loses nearly 80% of its activity
68.8
-
T50-value, mutant enzyme N398D
69.9
-
T50-value, wild-type enzyme
70 - 80
-
with syringaldazine as the substrate, the activity is increased 3fold after 50 min preincubation at 70°C and 2.4fold after 10 min preincubation at 80°C. Preincubation of the enzyme in 70°C for 30 min raises the activity 4fold with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) as the substrate
95
-
half-life: 2 h, recombinant enzyme
100
-
1 h, 80% loss of activity
100
-
purified native enzyme, 10 min, inactivation
100
inactivation through protein unfolding. The enzyme is refolded at 25°C but rests catalytically inactive
100
-
half-life is 8.7 min
100
MK290990.1
after 90 min enzyme activity increases to 138.76% and subsequently decreases, displaying residual activity of 69.90% at 270 min
20
-
purified laccase is stable at 20°C, pH 7.0 and pH 3.0
20
-
1 h, 4% loss of activity
25
-
purified native enzyme, half-life is 116 min
25
-
purified isozymes Lacc I and Lacc II are stable
25
-
150h, 50% residaul activity
30
-
60 min, enzyme retains 100% of its activity
30
24 h, 10% loss of activity
30
-
1 h, 8% loss of activity
30
-
40 h, 70% loss of activity
30
-
24h, 100% residual activity, increase in activity by 80% after shift from room temperature to 30°C
30
-
pH 6.0, stable for 16 h
30
-
purified enzyme, highly stable at
30
-
stable over a broad range of temperatures and are most stable at 30°C
30
Sporothrix carnis
-
the enzyme retains 94% of its initial activity after 180 min of incubation with 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as substrate
30
-
8 h, 40% loss of activity
30
-
the enzyme shows 1.3fold thermal activation within 360 min of incubation
35
-
purified native enzyme, half-life is 104 min
35
-
1 h, about 20% loss of activity
35
-
purified recombinant enzyme, 2 h, loss of 30% activity
35
-
1 h, about 50% loss of activity
35
-
purified enzyme, 24 h, stable
37
2.5 d, the enzyme retains nearly all of its original activity
37
30 days, the enzyme retains 80% of its activity
40
-
purified laccase rapidly loses its activity at 40°C
40
half-life time (t1/s): more than 12 h
40
-
60 min, enzyme retains 97% of its activity
40
-
1 h, 1% loss of activity
40
-
20h, 50% residual activity
40
-
80 h, about 50% loss of activity
40
-
24h, 100% residual activity, increase in activity by 100% after shift from room temperature to 40°C
40
-
stable for at least 12 h
40
half-life of recombinant, expressed in Saccharomyces cerevisiae, wild-type enzyme is over 50 h, and of the L559A mutant is 24 h
40
-
pH 3, 1 h, about 15% loss of activity
40
Phlebia fascicularia
-
stable below
40
-
POXA3a, 50% residual activity after 6 h, POXA3b, 50% residual activity after 14h
40
-
1 h, 50% loss of activity
40
-
3 h, at temperatures below 40°C, there is almost no change in enzymatic activity
40
Sporothrix carnis
-
the enzyme retains 98% of its initial activity after 180 min of incubation with 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as substrate
40
-
30 min, 52% loss of activity
40
-
8 h, 60% loss of activity
40
Thermochaetoides thermophila
-
half-life: 24 h
40
-
the enzyme shows 1.3fold thermal activation within 90 min of incubation
40
16 h, about 65% loss of activity
40
-
30 min, about 20% loss of activity
40
-
purified native enzyme, 60 min, completely stable up to
40
-
purified enzyme, stable up to
40 - 60
recombinant enzyme, pH 5.0 for 9 h, stable
40 - 60
-
isoform POXA1b shows a inactivation half-period of 3 h at 60°C, isoform POXA1w shows a inactivation half-period of 3.3 h at 60°C, isoform POXA2 shows a inactivation half-period of 0.2 h at 60°C, isoform POXA3a shows a inactivation half-period of 6 h at 40°C, isoform POXA3b shows a inactivation half-period of 14 h at 40°C, isoform POXC shows a inactivation half-period of 30 min at 40°C
45
-
purified native enzyme, half-life is 67 min
45
-
2 h, 20% loss of actuvity
45
-
purified recombinant enzyme, 1 h, loss of 30% activity
45
-
the enzyme is most stable at 45°C when exposed for 1 h
50
-
half-life 3 h
50
-
60 min, more than 80% residual activity
50
-
30 min, enzyme retains 85.4% of its activity. 90 min, enzyme retains 80% of its activity
50
6 h, 50% loss of activity
50
-
a significant increase in activity is observed until 60 min, in which the relative activity reaches to 150%
50
-
1 h, no loss of activity
50
10 h, no loss of activity
50
t1/2: 40.3 h (wild-type PM1 laccase), t1/2: 21.7 h (mutant 7D5 laccase)
50
-
1 h, 25% loss of activity
50
-
laccase Lac-4.8 shows thermal activation at 50°C and the enzyme activity after incubation is up to 120% of the original activity measured at 25°C
50
150 min, 85% of the original enzyme activity is retained
50
Tm of Lcc3 is determined at 73.9°C and it shows a t1/2 of 120 min at 50°C
50
-
60 min, purified isozyme Lacc I shows loss of 20% activity, purified isozyme Lacc II is stable
50
recombinant laccase is stable at temperatures below 50°C
50
30 min, no loss of activity, both wild-type and region Pro357-His406 deletion mutant
50
-
20 h, 80% loss of activity
50
fully active after 5 h at 50°C. Half-life: 1 day
50
-
purified enzyme, unstable above
50
-
purified enzyme, half-life: 281 min
50
half-life of recombinant, expressed in Saccharomyces cerevisiae, wild-type enzyme is 23 h, and of the L559A mutant is 6 h
50
-
1 h, about 65% loss of activity
50
-
pH 3, 1 h, about 80% loss of activity
50
-
inactivated rapidly above
50
the enzyme retains 100% activity after 3 h
50
-
60 min, 70% residual activity
50
-
210 min, 50% residual activity
50
-
3 h, at temperatures over 50°C the remaining laccase activity drops to below 70% of the initial activity
50
-
10 min, about 80% loss of activity
50
-
30 min, 75% loss of activity
50
-
8 h, 70% loss of activity
50
Thermochaetoides thermophila
-
half-life: 12 h
50
-
purified free enzyme half-life: 140 min, purified enzyme conjugated with 1.1 kDa PEG half-life: 70 min, purified enzyme conjugated with 2 kDa PEG half-life: 150 min, purified enzyme conjugated with 5.0 kDa PEG half-life: 210 min
50
-
20 min, 25% loss of activity
50
-
purified native enzyme, 60 min, 10% loss of activity
50
-
purified enzyme, 93% remaining activity after 24 h, 76% remaining activity after 48 h
50
-
purified enzyme, rapid decrease in activity
50
after 20 min the enzyme loses 60% of its initial activity
50
-
4 h, soluble and immobilized laccases retain more than 90% activity at 50°C. Copper alginate shows better stability than calcium alginate immobilized laccase
55
-
purified native enzyme, half-life is 47 min
55
-
loss of 80% activity, half-life: 12 min
55
the enzyme is fully active after 1 h at 55°C
55
-
incubation of enzyme above 55 °C initiates denaturing of enzyme and conformational changes, leveraging the decreased enzyme activity
55
Thermochaetoides thermophila
-
stable below
55
-
loss of 50% activity after 90 min
55
-
4 h, calcium alginate-chitosan immobilized laccase retains 91% activity
55
4 h, the relative enzyme activity is still over 50%, mutant enzyme V281A/P309L/S318G/D232V
60
-
half-life 40 min
60
-
10 h, almost complete inactivation
60
-
60 min, 25% residual activity
60
-
30 min, enzyme retains 54.0% of its activity. 90 min, enzyme retains 48% of its activity
60
-
pH 4.5, 60 min, 50% residual activity
60
stable up to when using the substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
60
360 min, 40% loss of activity
60
-
after 15 min incubation relative activity reaches to 140%
60
-
1 h, 9% loss of activity
60
10 h, no loss of activity
60
t1/2: 4.85 h (wild-type PM1 laccase), t1/2: 2.8 h (mutant 7D5 laccase)
60
-
1 h, 18% loss of activity
60
-
Lac-3.5 and Lac-4.8 show thermal stability at up to 60°C
60
150 min, 56% of the original enzyme activity is retained
60
recombinant enzyme, stable up to
60
the stability of laccase is not affected by temperatures below 60°C
60
pH 4.5, half-life of wild-type enzyme Lcc9 is 24 min, half-life of the recombinant enzyme expressed in Pichia pastoris is 15 min
60
the enzyme retains 100% of its initial activity after 3 h of incubation
60
-
complete inactivation, half-life: 4 min
60
30 min, 50% loss of activity, both wild-type and region Pro357-His406 deletion mutant
60
1 h, 10% loss of activity
60
-
purified enzyme, 90 min, 65% remaining activity
60
-
30 min, 33% loss of activity
60
-
purified enzyme, half-life: 25 min
60
Loweporus lividus
-
the enzyme is stable at 60°C for 2 h
60
Loweporus lividus MTCC-1178
-
2 h, stable
60
half-life of recombinant, expressed in Saccharomyces cerevisiae, wild-type enzyme is 4.5 h, and of the L559A mutant is below 10 min
60
-
10 min, about 85% loss of activity
60
-
5 h, 50% residual activity
60
-
pH 3, 1 h, complete loss of activity
60
-
60 min, 15% residual activity
60
-
POXA3a and POXA3b, 50% residual activity after a few min
60
-
purified enzyme, 10 min, loss of 90% activity
60
-
23 min, 50% residual activity
60
-
1 h, complete loss of activity
60
-
10 min, about 85% loss of activity. 40 min, complete inactivation
60
Sporothrix carnis
-
the enzyme retains 91% of its initial activity after 180 min of incubation with 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as substrate
60
-
purified isozymes, half-lives are 5-6 h, after 8 h 20% remaining activity for isozyme laccase I, 40% for laccase II and III
60
1 h, 50% loss of activity
60
-
8 h, 90% loss of activity
60
-
6 h, the enzyme retains 50% of its initial activity
60
-
20 min, about 80% loss of activity
60
-
purified enzyme, 2 h, 80% remaining activity
60
-
stable below, temperature stability profile
60
-
14 min, 50% residual activity
60
-
1 h, loss of 40% activity, purified enzyme
60
-
pH 5.0, half-life is 74 min
60
1 h, residual activity is more that 50%
65
-
purified native enzyme, half-life is 33 min
65
-
24 h, completely stable
65
the enzyme undergoes slow partial unfolding and thermal inactivation above 65°C, making it unsuitable for long incubations above this temperature
65
-
loss of 50% activity after 30 min
65
-
purified enzyme, half-life is 60 min
65
-
4 h, sol-gel immobilized laccase retains 90% activity
65.8
-
T50-value, mutant enzyme V159E
65.8
-
T50-value, mutant enzyme V159E/N398D
70
-
half-life 10 min
70
the mutant enzyme is resistant to heat treatment of 10 min. The mutant protein loses 45% of its original activity after incubation for 1 h. Mutant laccase in which sixteen original residues are replaced with those found in the phylogenetically inferred ancestral sequence
70
half-life time (t1/s): 30 min
70
-
30 min, enzyme retains 15.0% of its activity. 90 min, enzyme retains 10% of its activity. 180 min, complete inactivation
70
-
1 h, 57% loss of activity
70
wild-type and mutant enzymes retain more than 50% activity on both 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) and guaiacol upon incubation at 70 or 80°C for 2h
70
-
after 15 min incubation relative activity reaches to 148%
70
half-life: 60 min, recombinant enzyme
70
-
1 h, 21% loss of activity
70
-
after incubation for 10 h the residual activity is greater than 50%. Activity increases by more than 120% after 1 h incubation
70
10 h, more than 50% of activity
70
t1/2: 1.6 h (wild-type PM1 laccase), t1/2: 0.22 h (mutant 7D5 laccase)
70
-
1 h, 47% loss of activity
70
-
half-life: 30 min, laccase Lac-4.8
70
-
half-life: 60 min, laccase Lac-3.5
70
inactivated after 20 min
70
-
20 min, purified isozyme Lacc I shows complete loss of activity, isozyme Lacc II 10% after 60 min
70
recombinant enzyme, pH 5.0 for 9 h, loss of 80% activity
70
1 h, 40% loss of activity
70
-
purified enzyme, half-life: 4 min
70
-
100 mim, 20% loss of activity
70
FJ560721
the purified native enzyme retains 50% of its activity after 120 min of incubation
70
-
15 min, 50% residual activity
70
-
2 h, complete inactivation
70
-
purified enzyme, 10 min, 70% activity remaining
70
-
the purified enzyme retains its original activity after 24 h of incubation at pH between 4.0 and 8.0 and after 3 h of incubation at 70°C, pH 7.2 and supplemented with 1.3 M (NH4)2SO4
70
Sporothrix carnis
-
the enzyme retains 84% of its initial activity after 180 min of incubation with 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as substrate
70
-
purified isozymes, 8-15% remainng activity after 4 h, 50% remaining activity after 1.7 h
70
-
30 min, complete inactivation
70
-
purified recombinant enzyme, 90% remaining activity after 25 min, 50% remaining actiivty after 110 min
70
-
8 h, complete loss of activity
70
-
60 min, 40% residual activity
70
Thermochaetoides thermophila
-
1 h, stable
70
-
5 min, 90% loss of activity
70
-
purified native enzyme, 60 min, inactivation
70
-
purified enzyme, 2 h, 40% remaining activity
75
-
purified native enzyme, half-life is 23 min
75
mutant 7D5 laccase is notably activated at high temperature (laccase activity increases around 60% during the first 5 min of incubation at 75°C) whereas PM1 laccase is not
75
-
2 h, 97% loss of activity
75
-
40 min, enzyme hardly retains any activity
75
-
purified recombinant enzyme, 5 min, loss of 90% activity
75
-
purified enzyme, inactivation
75
27 min, 50% residual activity
79
-
melting temperature at pH 7.0. Presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol reduces melting temperature to 45-52°C
79
T50: 10 min, wild-type PM1 laccase
80
10 min, mutant enzyme retains 70% of its original activity, mutant laccase in which sixteen original residues are replaced with those found in the phylogenetically inferred ancestral sequence
80
10 min, complete inactivation
80
-
90 min, complete inactivation
80
-
pH 4.5, less than 2 min, 50% residual activity
80
-
1 h, 92% loss of activity
80
90 min, 25% loss of activity
80
wild-type and mutant enzymes retain more than 50% activity on both 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) and guaiacol upon incubation at 70 or 80°C for 2h
80
half-life: 20 min, recombinant enzyme
80
-
1 h, 44% loss of activity
80
half-life: 2.5 h, 21 % of the initial activity is detected after 10 h
80
-
ativity increases by nearly 90% after 1 h incubation
80
t1/2: 0.12 h (wild-type PM1 laccase), t1/2: 0.03 h (mutant 7D5 laccase)
80
-
1 h, complete loss of activity
80
-
20 min, 80% loss of activity
80
inactivated after 2 min
80
-
rapid inactivation of purified isozyme Lacc II with 95% loss of activity within 10 min
80
the remaining activity is 37% and 7% following treatment for 10 min and 60 min
80
Sporothrix carnis
-
the enzyme retains 65% of its initial activity after 180 min of incubation with 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as substrate
80
30 min, wild-type enzyme shows 60% of initial activity after incubation, mutant enzymes M199G and Y230A exhibit less than 30% of the initial activity
80
Thermochaetoides thermophila
-
half-life: 10 min
80
half-life: more than 14 h
80
-
0-4 h, residual enzymatic activity decreases with the increase of the incubation time. The wild-type, K428M, K428E and K428R enzymes remain 70% of corresponding initial activity after incubated for 4 h. The K428L mutant is most affected, only 30% of the initial activity is retained after 4 h
80
4 h, wild-type enzymed retains 80% of its activity. The thermal stability of D394R mutant decreases significantly, with the residual activity of 15% after 4 h
80
-
purified enzyme, 2 h, 5% remaining activity, half-life at 80°C is 20 min
85
10 min, mutant enzyme retains 30% of its original activity, mutant laccase in which sixteen original residues are replaced with those found in the phylogenetically inferred ancestral sequence
85
-
10 min, complete inactivation
85
-
purified enzyme, 10 min, inactivation
90
35 min, 30% loss of activity
90
-
1 h, 68% loss of activity
90
-
2 h, recombinant enzyme retains 85% of its activity
90
above, high thermal stability of purified wild-type rMmPPOA-695-His and mutant rMmPPOA-637-His enzymes
90
Sporothrix carnis
-
the enzyme retains 50% of its initial activity after 180 min of incubation with 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as substrate
additional information
-
T1 copper depletion is a key event in inactivation and a determinant of the thermodynamic stability, thermodynamic stability of wild-type and mutant proteins, overview
additional information
-
laccase 2 has higher thermostability than laccase 1
additional information
the recombinant His-tagged MmPPOA-695 shows a very high thermal stabilit
additional information
-
the recombinant His-tagged MmPPOA-695 shows a very high thermal stabilit
additional information
thermal stability of the enzyme is negatively influenced by an alteration of the amino acid sequence at the C terminus. Glycosylation enhances the thermal stability of the enzyme
additional information
-
thermal stability of the enzyme is negatively influenced by an alteration of the amino acid sequence at the C terminus. Glycosylation enhances the thermal stability of the enzyme
additional information
-
the activation energy for thermal denaturation of the enzyme is 38.20 kJ/mole/K
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analysis
-
sensitive, rapid, and precise determination of phenols and their derivatives is important in environmental control and protection. An amperometric principle-based biosensor, employing immobilized laccase enzyme from Trametes versicolor, is developed for the detection of disubstituted methyl and methoxy phenols (industrial effluents). Evaluation of the influence of different enzyme immobilization techniques, on nylon membrane, on the performances of laccase-based Clark-type electrodes. The analytical properties and operating stabilities of the resulting biosensors are tested with different disubstituted methyl and methoxy derivatives of phenol substrates. Co-cross-linking method is superior to the other methods of immobilization in terms of sensitivity, limit of detection, response time, and operating stability. In co-cross-linking method of immobilization, laccase is mixed with bovine serum albumin as protein-based stabilizing agent and glutaraldehyde as crosslinking agent
biofuel production
construction of a long-life biofuel cell using a hyperthermophilic enzyme. For the cathode, the multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum is used, which catalyzes a four-electron reduction, and, for the anode, the PQQ-dependent glucose dehydrogenase from Pyrobaculum aerophilum is used. When the enzymes are used as electrodes, oriented with carbon nanotubes in a highly organized manner, the maximum output is 0.011 mW at 0.2 V. This output can be maintained 70% after 14 days
biofuel production
potential for bioconversion of lignin rich agricultural byproducts into animal feed and cellulosic ethanol. The enzyme effectively improves in vitro digestibility of maize straw
biofuel production
-
lignin degradation of agricultural biomass for biofuel production
biofuel production
-
construction of a long-life biofuel cell using a hyperthermophilic enzyme. For the cathode, the multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum is used, which catalyzes a four-electron reduction, and, for the anode, the PQQ-dependent glucose dehydrogenase from Pyrobaculum aerophilum is used. When the enzymes are used as electrodes, oriented with carbon nanotubes in a highly organized manner, the maximum output is 0.011 mW at 0.2 V. This output can be maintained 70% after 14 days
-
biotechnology
-
expression of non-fused enzyme and hydrophobin-enzyme fusion protein in Trichoderma reesei, intracellular accumulation and degradation of fusion protein, production of non-fused enzyme at up to 920 mg per l of fed-batch culture, purification from culture supernatant
biotechnology
-
five SvLAC genes (SvLAC9, SvLAC13, SvLAC15, SvLAC50, and SvLAC52) fulfill the criteria established to identify lignin-related candidates. They are strong candidates to be involved in lignin polymerization in Setaria viridis and might be good targets for lignin bioengineering strategies
biotechnology
MK290990.1
robust catalytic efficiency in the presence of organic solvents suggest its industrial and biotechnological application potentials for the sustainable development of green chemistry
biotechnology
-
the purified enzyme displays greater efficiency in Remazol Brilliant Blue R decolourization (90%) in absence of redox mediator, an important property for biotechnological applications
degradation
-
mineralization of organochlorine from toxic chlorophenols
degradation
-
enzyme shows dye-decolourizing activity against several anthraquinone dyes, azo dyes, polymeric dyes and others
degradation
-
enzyme shows dye-decolourizing activity against several anthraquinone dyes, azo dyes, polymeric dyes and others
degradation
-
enzyme shows dye-decolourizing activity against several anthraquinone dyes, azo dyes, polymeric dyes and others
degradation
-
use of enzyme in biodegradation of endocrine-disrupting chemicals such as bisphenol A and nonylphenol
degradation
-
use of enzyme to decolourize textile dye
degradation
-
cyanobacterial laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Due to phototrophic mode of nutrition, short generation time and easy mass cultivation, Spirulina platensis laccase appears as good candidate for laccase production. The high yield of laccase in short production period are profitable for its industrial application. Pure Spirulina platensis laccase alone can efficiently decolorized anthraquinonic dye Reactive Blue 4 without any mediators which makes it cost effective and suitable candidate for decolorization of synthetic dyes and help in waste water treatment
degradation
-
degradation of synthetic dyes from wastewater using biological treatment
degradation
-
eliminating toxic compounds (biogenic amines) present in fermented food and beverages
degradation
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatmen
degradation
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment
degradation
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment
degradation
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment, thermostable and acidophilic laccase that can efficiently decolorize several synthetic dyes without addition of an expensive redox mediator
degradation
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme alone can decolourize indigo carmine partially after 60-min incubation at 45 °C. Decolorization is much more efficient in the presence of syringaldehyde. Nearly 90 % decolorization is observed within 20 min
degradation
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme is effective in the decolorization of bromothymol blue, evans blue, methyl orange, and malachite green with decolorizationefficiencies of 50%-85%
degradation
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Two anthraquinonic dyes (reactive blue 4 and reactive yellow brown) and two azo dyes (reactive red 11 and reactive brilliant orange) can be partially decolorized by purified laccase in the absence of a mediator. The decolorization process is efficiently promoted when methylsyringate is present, with more than 90 % of color removal occurring in 3 h at pH 7.0 or 9.0
degradation
the enzyme is potentially useful for industrial and environmental applications such as textile finishing and wastewater treatment. It decolorizes structurally different dyes and a real textile effluent
degradation
-
bisphenol A degradation
degradation
-
decolorization of industrial dyes. Evans blue decolorization and detoxification
degradation
degradation of endocrine disrupting compounds
degradation
-
degradation of lignin
degradation
-
deinking of old newspaper, indigo carmine decolorization
degradation
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment
-
degradation
-
enzyme shows dye-decolourizing activity against several anthraquinone dyes, azo dyes, polymeric dyes and others
-
degradation
-
degradation of synthetic dyes from wastewater using biological treatment
-
degradation
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme is effective in the decolorization of bromothymol blue, evans blue, methyl orange, and malachite green with decolorizationefficiencies of 50%-85%
-
degradation
-
cyanobacterial laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Due to phototrophic mode of nutrition, short generation time and easy mass cultivation, Spirulina platensis laccase appears as good candidate for laccase production. The high yield of laccase in short production period are profitable for its industrial application. Pure Spirulina platensis laccase alone can efficiently decolorized anthraquinonic dye Reactive Blue 4 without any mediators which makes it cost effective and suitable candidate for decolorization of synthetic dyes and help in waste water treatment
-
degradation
-
the enzyme is potentially useful for industrial and environmental applications such as textile finishing and wastewater treatment. It decolorizes structurally different dyes and a real textile effluent
-
degradation
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme alone can decolourize indigo carmine partially after 60-min incubation at 45 °C. Decolorization is much more efficient in the presence of syringaldehyde. Nearly 90 % decolorization is observed within 20 min
-
degradation
-
eliminating toxic compounds (biogenic amines) present in fermented food and beverages
-
degradation
-
enzyme shows dye-decolourizing activity against several anthraquinone dyes, azo dyes, polymeric dyes and others
-
energy production
-
combination oflaccase and catalase in construction of H2O2-O2 based biocathode for applications in glucose biofuel cells. The deposited enzymes laccase and catalase by means of alternating current electrophoretic deposition (AC-EPD) do not inhibit each other and carry out about 90% of the catalytic reduction process of O2-H2O2
energy production
-
molecular design of laccase cathode for direct electron transfer in a biofuel cell. Functionalized graphite electrodes with a substrate-like molecule, that can interact as ligand with the redox site of the protein, are able to orientate the coupling of laccase molecule with the electrode surface through the T1 site. This molecular orientation enhances the direct electron transfer between the T1 site and the graphite electrode surface. The molecular design of enzymatic electrodes seems to be a powerful tool for the optimization of enzyme-based fuel cells
energy production
-
a CotA mutant from Bacillus licheniformis, operating in basic media and seawater, is effective in catalyzing the bioelectrocatalytic O2 reduction, suggesting a prospective enzyme application for sustainable production of energy from seawater and oxygen
energy production
-
molecular design of laccase cathode for direct electron transfer in a biofuel cell. Functionalized graphite electrodes with a substrate-like molecule, that can interact as ligand with the redox site of the protein, are able to orientate the coupling of laccase molecule with the electrode surface through the T1 site. This molecular orientation enhances the direct electron transfer between the T1 site and the graphite electrode surface. The molecular design of enzymatic electrodes seems to be a powerful tool for the optimization of enzyme-based fuel cells
-
environmental protection
-
fast biodegradation of 2,4-dichlorophenol, a potent xenobiotic compound
environmental protection
-
laccase is capable of efficiently removing 2,4-dimethylphenol from water at very low enzyme concentrations and hence shows great potential for cost-effective industrial applications
environmental protection
-
LI1 shows activity over a broad range of pH and temperature, which may make it useful in the biodegradation of phenolic compounds present in wastewater from several industrial processes
environmental protection
-
the stability of this laccase against metal ions makes the enzyme an efficient agent in the treatment of wastewater containing heavy metals
environmental protection
-
cyanobacterial laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Due to phototrophic mode of nutrition, short generation time and easy mass cultivation, Spirulina platensis laccase appears as good candidate for laccase production. The high yield of laccase in short production period are profitable for its industrial application. Pure Spirulina platensis laccase alone can efficiently decolorized anthraquinonic dye Reactive Blue 4 without any mediators which makes it cost effective and suitable candidate for decolorization of synthetic dyes and help in waste water treatment
environmental protection
-
degradation of synthetic dyes from wastewater using biological treatment
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment, thermostable and acidophilic laccase that can efficiently decolorize several synthetic dyes without addition of an expensive redox mediator
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme alone can decolorize indigo carmine partially after 60-min incubation at 45°C. Decolorization is much more efficient in the presence of syringaldehyde. Nearly 90 % decolorization is observed within 20 min
environmental protection
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme can also be considered as a candidate for treating industrial effluent containing malachite green
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme is effective in the decolorization of bromothymol blue, evans blue, methyl orange, and malachite green with decolorizationefficiencies of 50%-85%
environmental protection
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Two anthraquinonic dyes (reactive blue 4 and reactive yellow brown) and two azo dyes (reactive red 11 and reactive brilliant orange) can be partially decolorized by purified laccase in the absence of a mediator. The decolorization process is efficiently promoted when methylsyringate is present, with more than 90 % of color removal occurring in 3 h at pH 7.0 or 9.0
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and is a suitable candidate for the treatment of wastewater from industrial effluents
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and is a suitable candidate for the treatment of wastewater from industrial effluents
environmental protection
laccase can be efficiently used to decolorize synthetic dye and is a suitable candidate for the treatment of wastewater from industrial effluents
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and is a suitable candidate for the treatment of wastewater from industrial effluents. The wide pH- and thermostability attributes of immobilized laccase make them suitable for environmental applications
environmental protection
-
sensitive, rapid, and precise determination of phenols and their derivatives is important in environmental control and protection. An amperometric principle-based biosensor, employing immobilized laccase enzyme from Trametes versicolor, is developed for the detection of disubstituted methyl and methoxy phenols (industrial effluents). Evaluation of the influence of different enzyme immobilization techniques, on nylon membrane, on the performances of laccase-based Clark-type electrodes. The analytical properties and operating stabilities of the resulting biosensors are tested with different disubstituted methyl and methoxy derivatives of phenol substrates. Co-cross-linking method is superior to the other methods of immobilization in terms of sensitivity, limit of detection, response time, and operating stability. In co-cross-linking method of immobilization, laccase is mixed with bovine serum albumin as protein-based stabilizing agent and glutaraldehyde as crosslinking agent
environmental protection
the enzyme has potential for application in the treatment of contaminated water with low pH values and high phenolic content
environmental protection
the enzyme is potentially useful for industrial and environmental applications such as textile finishing and wastewater treatment. It decolorizes structurally different dyes and a real textile effluent
environmental protection
decolorization of industrial dyes with different chemical structures and decolorization of industrial wastewaters
environmental protection
-
decolorization of industrial dyes. Evans blue decolorization and detoxification
environmental protection
-
deinking of old newspaper, indigo carmine decolorization
environmental protection
good application prospect in wastewater treatment and dye degradation. error-prone PCR is a feasible method to improve the degradation activity of laccase for environmental pollutants, which provide a basis for the application of laccase on dye degradation and other environmental pollutants
environmental protection
-
laccases are very important in removing environmental pollutants, detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants, detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants, detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants, detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants, detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants, detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants, detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants, detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants, detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
environmental protection
laccases are very important in removing environmental pollutants. Detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
environmental protection
-
potential for industrial wastewater treatments
environmental protection
-
the enzyme is able to decolorize efficiently a variety of chemical dyes, thus, being potentially applicable in textile and environmental industries
environmental protection
the enzyme is an ideal candidate for lots of biotechnological and industrial applications due to its stability in the extreme conditions
environmental protection
-
the immobilized laccase transforms diclofenac to 4-OH diclofenac. The immobilized laccase can be used to transform or degrade several recalcitrant compounds from industrial effluents
environmental protection
-
the surface display laccase (SDL) biocatalyst, where the enzyme laccase is displayed on the surface of biological cells through synthetic biology, provides a biocatalytic material for removal of emerging contaminants from wastewater
environmental protection
treating waste water containing synthetic dyes
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and is a suitable candidate for the treatment of wastewater from industrial effluents. The wide pH- and thermostability attributes of immobilized laccase make them suitable for environmental applications
-
environmental protection
-
treating waste water containing synthetic dyes
-
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
-
environmental protection
-
laccases are very important in removing environmental pollutants, detoxification from wastewater
-
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
-
environmental protection
-
the enzyme is an ideal candidate for lots of biotechnological and industrial applications due to its stability in the extreme conditions
-
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and is a suitable candidate for the treatment of wastewater from industrial effluents
-
environmental protection
-
degradation of synthetic dyes from wastewater using biological treatment
-
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
-
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme is effective in the decolorization of bromothymol blue, evans blue, methyl orange, and malachite green with decolorizationefficiencies of 50%-85%
-
environmental protection
-
cyanobacterial laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Due to phototrophic mode of nutrition, short generation time and easy mass cultivation, Spirulina platensis laccase appears as good candidate for laccase production. The high yield of laccase in short production period are profitable for its industrial application. Pure Spirulina platensis laccase alone can efficiently decolorized anthraquinonic dye Reactive Blue 4 without any mediators which makes it cost effective and suitable candidate for decolorization of synthetic dyes and help in waste water treatment
-
environmental protection
-
laccases are very important in removing environmental pollutants, detoxification from wastewater
-
environmental protection
-
the enzyme has potential for application in the treatment of contaminated water with low pH values and high phenolic content
-
environmental protection
-
the enzyme is potentially useful for industrial and environmental applications such as textile finishing and wastewater treatment. It decolorizes structurally different dyes and a real textile effluent
-
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
-
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment
-
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme alone can decolorize indigo carmine partially after 60-min incubation at 45°C. Decolorization is much more efficient in the presence of syringaldehyde. Nearly 90 % decolorization is observed within 20 min
-
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme can also be considered as a candidate for treating industrial effluent containing malachite green
-
environmental protection
-
laccase can be efficiently used to decolorize synthetic dye and is a suitable candidate for the treatment of wastewater from industrial effluents
-
environmental protection
-
the enzyme is able to decolorize efficiently a variety of chemical dyes, thus, being potentially applicable in textile and environmental industries
-
environmental protection
-
laccases are very important in removing environmental pollutants, detoxification from wastewater
-
environmental protection
-
laccases are very important in removing environmental pollutants. Detoxification from wastewater
-
food industry
-
both laccase and tyrosinase increase the dough strength and improved the bread-making quality of white wheat flour breads, especially when used in combination with xylanase
food industry
potential for bioconversion of lignin rich agricultural byproducts into animal feed and cellulosic ethanol. The enzyme effectively improves in vitro digestibility of maize straw
industry
-
Pycnoporus sp. SYBC-L1 is a potential candidate for industrial application. It can be exploited for a number of industrial and environmental applications, such as paper pulping and bleaching, textile dye bleaching, bioremediation, and detoxification, overview
industry
-
the laccase has a wide application in industrial processes, particularly in renewable bio-energy industry
industry
-
delignification of sugar beet pulp. Delignification pretreatment is the most challenging and critical step in the recycling process of lignocellulosic materials as the most abundant natural resources on the earth and has a large impact on cellulose extraction, cellulose digestibility, and downstream costs. Amongst the various delignification strategies, the enzymatic method has been demonstrated as a promising eco-friendly process with no inhibitor generation, although it is not highly efficient
industry
-
potential use of the laccase in lignin modification
industry
-
the enzyme can be usedc in industrial bleaching processes, thermostable and acidophilic laccase that can efficiently decolorize several synthetic dyes without an expensive redox mediator
industry
the enzyme decoloures up to six different industrial dyes, with or without the use of redox mediators such as ABTS
industry
advantageous for laccases in industrial application as it acts as broad pH range acting enzyme
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
industry
-
laccases can be considered as one of the most important biocatalyst which can be exploited for divergent industrial applications viz. paper pulp bleaching, fiber modification, dye decolorization, bioremediation as well as organic synthesis
industry
-
laccases can be considered as one of the most important biocatalyst which can be exploited for divergent industrial applications viz. paper pulp bleaching, fiber modification, dye decolorization, bioremediation as well as organic synthesis
industry
-
laccases can be considered as one of the most important biocatalyst which can be exploited for divergent industrial applications viz. paper pulp bleaching, fiber modification, dye decolorization, bioremediation as well as organic synthesis
industry
-
laccases can be considered as one of the most important biocatalyst which can be exploited for divergent industrial applications viz. paper pulp bleaching, fiber modification, dye decolorization, bioremediation as well as organic synthesis
industry
-
laccases can be considered as one of the most important biocatalyst which can be exploited for divergent industrial applications viz. paper pulp bleaching, fiber modification, dye decolorization, bioremediation as well as organic synthesis
industry
-
laccases can be considered as one of the most important biocatalyst which can be exploited for divergent industrial applications viz. paper pulp bleaching, fiber modification, dye decolorization, bioremediation as well as organic synthesis
industry
-
potential for industrial wastewater treatments
industry
-
the enzyme is able to decolorize efficiently a variety of chemical dyes, thus, being potentially applicable in textile and environmental industries
industry
-
the high thermostability makes LacG potentially useful for industrial applications
industry
-
Pycnoporus sp. SYBC-L1 is a potential candidate for industrial application. It can be exploited for a number of industrial and environmental applications, such as paper pulping and bleaching, textile dye bleaching, bioremediation, and detoxification, overview
-
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
-
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
-
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
-
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
-
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
-
industry
-
the laccase has a wide application in industrial processes, particularly in renewable bio-energy industry
-
industry
-
the enzyme is able to decolorize efficiently a variety of chemical dyes, thus, being potentially applicable in textile and environmental industries
-
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
-
industry
-
application of laccases in chemical processes and industrial usages, such as bioremediation, nanobiotechnology, woodworking industries, bleaching of paper pulp, dyeing in the textile industry
-
medicine
-
inhibitory activity of enzyme against HIV-1 reverse transcriptase, 50% inhibition at 0.0095 mM
medicine
-
no inhibitory activity of enzyme against HIV-1 reverse transcriptase
medicine
-
no inhibitory activity of enzyme against HIV-1 reverse transcriptase
paper production
biobleaching of eucalyptus kraft pulps results in a significant decrease in the kappa number and a significant increase in the brightness of the pulps
paper production
-
biobleaching of eucalyptus kraft pulps results in a significant decrease in the kappa number and a significant increase in the brightness of the pulps
-
synthesis
-
addition of phenolic and aromatic monomers to growth medium to enhance enzyme production, ferulic acid plus vanillin are most efficient inducers increasing enzyme production up to 10 times
synthesis
-
Pycnoporus sp. SYBC-L1 is a potential candidate for laccase production
synthesis
-
owing to their broad substrate range laccases are considered to be versatile biocatalysts which are capable of oxidizing natural and non-natural industrial compounds, with water as sole by-product
synthesis
-
potential use of the laccase in lignin modification
synthesis
-
selective biotransformation of aromatic methyl group to aldehyde group in presence of diammonium salt of 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as the mediator
synthesis
the enzyme will serve as a useful tool for enzymatic polymerization of diphenolic compounds such as caffeic acid and ferulic acid
synthesis
-
synthesis of bioactive 1,4-naphthoquinones. A high yield of naphthoquinones (74.93%) with 1,4-naphthoquinone (60.61%), and its derivative 2-hydroxy-1,4-naphthoquinone (14.32%) is obtained at the optimized reaction conditions
synthesis
-
synthesis of the C-N polydye at basic pHs
synthesis
-
the enzyme from Crinipellis sp. synthesizes oxaflavins for redox co-enzymes
synthesis
-
the enzyme from Pycnoporus cinnabarinus synthesizes 1. benzofuropyroles, which are potent pharmaceutical agents, 2. the pharmaceutical agent 6,7-dihydroxy-2,2-dimethyl-1,3,9-trioxa-fluoren-4-one
synthesis
-
the enzyme from Trametes hirsute synthesizes polyanniline
synthesis
-
the enzyme from Trametes versicolor synthesizes 1. polycatechol, a valuable polymer used as a chromatographic resin and in the formation of thin films for biosensors, 2. benzofuranones for medicinal chemistry, 3. poly allylamine with high antioxidant potential, 4. dyes used in hair dyeing, 5. benzoquinones used as intermediates in pharmaceuticals, 6. phenazine and phenoxazinone chromopheres for synthetic dyes
synthesis
-
the enzyme from Trametes villosa synthesizes benzofurans with antimicrobial and anti-inflammatory activities
synthesis
-
the enzyme from Ustilago maydis synthesizes polymers of quercitin and kampferol with improved antioxidant properties of the polymers compared to the monomers
synthesis
-
Pycnoporus sp. SYBC-L1 is a potential candidate for laccase production
-
synthesis
-
owing to their broad substrate range laccases are considered to be versatile biocatalysts which are capable of oxidizing natural and non-natural industrial compounds, with water as sole by-product
-
synthesis
-
selective biotransformation of aromatic methyl group to aldehyde group in presence of diammonium salt of 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) as the mediator
-
synthesis
-
synthesis of bioactive 1,4-naphthoquinones. A high yield of naphthoquinones (74.93%) with 1,4-naphthoquinone (60.61%), and its derivative 2-hydroxy-1,4-naphthoquinone (14.32%) is obtained at the optimized reaction conditions
-
additional information
-
the enzyme is useful in decolorization of azo dyes, method optimization, overview
additional information
-
environmental protection, potential application of waste water cyanobacterial bloom and dyeing effluent as a medium for laccase production by Coriolus versicolor strain MTCC138
additional information
environmental protection: laccases are of interest in the field of bioremediation because of their ability to oxidize both phenolic and nonphenolic lignin-related compounds, as well as environmental pollutants such as endocrine-disrupting chemicals, pesticides, herbicides, and certain explosives
additional information
-
environmental protection: laccases are of interest in the field of bioremediation because of their ability to oxidize both phenolic and nonphenolic lignin-related compounds, as well as environmental pollutants such as endocrine-disrupting chemicals, pesticides, herbicides, and certain explosives
additional information
-
laccases are versatile biocatalysts with various potential biotechnological applications, e.g. the treatment of industrial waste waters, the detoxification of environmental pollutants, or the functionalization of renewable polymeric materials
additional information
-
laccases are versatile biocatalysts with various potential biotechnological applications, e.g. the treatment of industrial waste waters, the detoxification of environmental pollutants, or the functionalization of renewable polymeric materials
additional information
-
the enzyme may be used in a variety of biotechnological applications, including textile dye bleaching, pulp bleaching, bioremediation, polymer synthesis and biosensors
additional information
-
the enzyme may be used in a variety of biotechnological applications, including textile dye bleaching, pulp bleaching, bioremediation, polymer synthesis and biosensors
additional information
-
usage of thermotolerant laccase from Bacillus sp. for biodegradation of synthetic dyes, overview
additional information
-
pulp biobleaching
additional information
-
laccases are versatile biocatalysts with various potential biotechnological applications, e.g. the treatment of industrial waste waters, the detoxification of environmental pollutants, or the functionalization of renewable polymeric materials
-
additional information
-
environmental protection, potential application of waste water cyanobacterial bloom and dyeing effluent as a medium for laccase production by Coriolus versicolor strain MTCC138
-
additional information
-
pulp biobleaching
-
additional information
-
environmental protection: laccases are of interest in the field of bioremediation because of their ability to oxidize both phenolic and nonphenolic lignin-related compounds, as well as environmental pollutants such as endocrine-disrupting chemicals, pesticides, herbicides, and certain explosives
-
additional information
-
laccases are versatile biocatalysts with various potential biotechnological applications, e.g. the treatment of industrial waste waters, the detoxification of environmental pollutants, or the functionalization of renewable polymeric materials
-