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Information on EC 1.11.1.19 - dye decolorizing peroxidase
for references in articles please use BRENDA:EC1.11.1.19
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EC Tree 1 Oxidoreductases
1.11 Acting on a peroxide as acceptor
1.11.1 Peroxidases
1.11.1.19 dye decolorizing peroxidase
IUBMB Comments
Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria. They are similar to EC 1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II). The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid. Bacterial TfuDyP catalyses sulfoxidation.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.11.1.19
- peroxidases
- heme
- lignin
- auricula-judae
-
thanatephorus
- cucumeris
-
veratryl
-
auricularia
- irpex
-
ligninolytic
- lacteus
-
lignin-degrading
-
kraft
- adusta
- bjerkandera
- chlorite
-
nonphenolic
- 2,6-dimethoxyphenol
- sapidus
-
lignin-derived
- paper production
- degradation
Reaction Schemes
showSynonyms
dye-decolorizing peroxidase, dyp-type peroxidase, dyp1b, tt1485, dye decolorizing peroxidase, lip ba45, mnp ba30, lip-sn, ancdypd-b1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dye decolorizing peroxidases type B
dye-decolorizing peroxidase
DyP
DyP-I
DyP-type peroxidase
DyP-V
DyP1
DyP1B
DyP2
DyP4
EfeB
LiP BA45
LiP-SN
MnP BA30
reactiveblue-5: hydrogen-peroxide oxidoreductase
tyrA
YfeX
YRW2 Mb
-
myoglobin mutant F43Y/T67R/P88W/F138W exhibiting considerably enhanced dye decolorizing peroxidase activity
dye-decolorizing peroxidase
-
-
DyP
-
-
-
-
DyP
-
-
DyP-type peroxidase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Reactive Blue 5 + 2 H2O2 = phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
Reactive-Blue-5:hydrogen-peroxide oxidoreductase
Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria. They are similar to EC 1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II). The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid. Bacterial TfuDyP catalyses sulfoxidation.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(E)-methyl isoeugenol + H2O2 + H+
veratraldehyde + acetaldehyde
Substrates: -
Products: -
Products: -
?
1,4-diamino-2-sodium anthraquinone sulfonate + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
?
1-amino-4-(3-amino-4-sodium-sulfonoanilino)-2-sodium anthraquinone sulfonate + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
?
1-amino-4-methylamino-2-sodium anthraquinone sulfonate + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
?
2 1,2-phenylenediamine + H2O2 + H+
4a,10a-dihydrophenazine-2,3-diamine + H2O
-
Substrates: -
Products: -
Products: -
?
2 2,5-diaminobenzenesulfonic acid + H2O2 + H+
2,7-diaminophenazine-1,6-disulfonic acid + H2O
-
Substrates: -
Products: -
Products: -
?
2 2,6-dimethoxyphenol + H2O2
coerulignone + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
2,2'-azino-bis(3-ethylbenzthiazoline)-6-sulfonic acid + H2O2 + H+
?
Q8YWM0
Substrates: 89% activity compared to guaiacol
Products: -
Products: -
?
2,4,6-trichlorophenol + H2O2 + H+
?
-
Substrates: about 63% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
2,5-diaminobenzenesulfonic acid + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
?
3 1,4-phenylenediamine + H2O2 + H+
(3E,6E)-3,6-bis[(4-aminophenyl)imino]cyclohexa-1,4-diene-1,4-diamine + H2O
-
Substrates: -
Products: -
Products: -
?
3 N1-phenylbenzene-1,4-diamine + H2O2 + H+
(3E,6E)-3,6-bis[(4-anilinophenyl)imino]-N1-phenylcyclohexa-1,4-diene-1,4-diamine + H2O
-
Substrates: -
Products: -
Products: -
?
3,3'-diaminobenzidine + H2O2 + H+
?
Substrates: weak activity
Products: -
Products: -
?
4-aminoantipyrine + H2O2 + H+
?
Q8YWM0
Substrates: 643% activity compared to guaiacol
Products: -
Products: -
?
Acid Blue 45 + H2O2 + H+
oxidized Acid Blue 45 + H2O
Q8YWM0
Substrates: 98% decolorization rate compared to Reactive Blue 5
Products: -
Products: -
?
Acid Blue 62 + H2O2 + H+
oxidized Acid Blue 62 + H2O
Substrates: -
Products: -
Products: -
?
Acid Orange 7 + H2O2 + H+
oxidized Acid Orange 7 + H2O
-
Substrates: 100% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
Products: -
?
Acid Red 151 + H2O2 + H+
oxidized Acid Red 151 + H2O
Q8YWM0
Substrates: 12% decolorization rate compared to Reactive Blue 5
Products: -
Products: -
?
Acid Red 27 + H2O2 + H+
oxidized Acid Red 27 + H2O
-
Substrates: 97.9% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
Products: -
?
Acid Red 73 + H2O2 + H+
oxidized Acid Red 73 + H2O
-
Substrates: 100% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
Products: -
?
adlerol + H2O2 + H+
?
-
Substrates: i.e 1-(3,4-dimethoxyphenyl)-1-oxo-2-(2-methoxyphenoxy)-1,3-dihydroxy-propane, maximum oxidation activity at pH 2.5
Products: -
Products: -
?
alpha-methylstyrene + H2O2 + H+
acetophenone + formaldehyde
Substrates: -
Products: -
Products: -
?
Amaranth + H2O2 + H+
oxidized Amaranth + H2O
-
Substrates: 82% decolorization after 30 min
Products: -
Products: -
?
beta-carotene + H2O2 + H+
beta-ionone + beta-cyclocitral + dihydroactinidiolide + 2-hydroy-2,6,6-trimethylcyclohexanone + ?
Substrates: -
Products: -
Products: -
?
Brilliant Blue R + H2O2 + H+
?
-
Substrates: 54% decolorization after 1 h
Products: -
Products: -
?
commercial humic acid + H2O2 + H+
?
-
Substrates: 81% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
Congo Red + H2O2 + H+
oxidized Congo Red + H2O
Q8YWM0
Substrates: 12% decolorization rate compared to Reactive Blue 5
Products: -
Products: -
?
copper phthalocyanine-3,4',4',4'''-tetrasulfonic acid + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
?
D-isoascorbate + H2O2 + H+
?
Q8YWM0
Substrates: 134% activity compared to guaiacol
Products: -
Products: -
?
Direct Sky Blue 6B + H2O2 + H+
oxidized Direct Sky Blue 6B + H2O
Q8YWM0
Substrates: 50% decolorization rate compared to Reactive Blue 5
Products: -
Products: -
?
guaiacylglycerol-beta-guaiacol ether + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
Indigo Carmine + H2O2 + H+
oxidized Indigo Carmine + H2O
-
Substrates: -
Products: -
Products: -
?
Kraft lignin + H2O2 + H+
oxidized Kraft lignin + H2O
-
Substrates: -
Products: -
Products: -
?
L-ascorbate + H2O2 + H+
?
Q8YWM0
Substrates: 126% activity compared to guaiacol
Products: -
Products: -
?
o-phenylenediamine + H2O2 + H+
?
Substrates: 0.7%activity compared to Reactive Blue 19
Products: -
Products: -
?
pentachlorophenol + H2O2 + H+
?
-
Substrates: 10% activity compared to 2,6-dimethoxyphenol
Products: -
Products: -
?
Poly R-478 + H2O2 + H+
oxidized Poly R-478 + H2O
-
Substrates: -
Products: -
Products: -
?
Procion Blue H-ERD + H2O2 + H+
oxidized Procion Blue H-ERD + H2O
Q8YWM0
Substrates: 90% decolorization rate compared to Reactive Blue 5
Products: -
Products: -
?
Procion Blue H-EXL + H2O2 + H+
oxidized Procion Blue H-EXL + H2O
Q8YWM0
Substrates: 72% decolorization rate compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + ? + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate
Reactive Blue 5 + H2O2 + H+
4-amino-2-((4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl)amino)benzenesulfonic acid + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid + 4-amino-2-[(4-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid
Reactive Blue 5 + H2O2 + H+
4-amino-2-([4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl]amino)benzenesulfonic acid + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid + 4-amino-2-[(4-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid
Substrates: -
Products: -
Products: -
?
Reactive Dye Remazol Brilliant Violet 5R + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
?
Reactive Green 19 + H2O2 + H+
oxidized Reactive Green 19 + H2O
Q8YWM0
Substrates: 35% decolorization rate compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Orange 14 + H2O2 + H+
oxidized Reactive Orange 14 + H2O
Q8YWM0
Substrates: 10% decolorization rate compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Orange 16 + H2O2 + H+
?
-
Substrates: 70% decolorization after 30 min
Products: -
Products: -
?
Reactive Red 120 + H2O2 + H+
oxidized Reactive Violet 23 + H2O
-
Substrates: slight decolorization
Products: -
Products: -
?
Reactive Red 187 + H2O2 + H+
oxidized Reactive Red 187 + H2O
-
Substrates: 100% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
Products: -
?
Reactive Red 202 + H2O2 + H+
oxidized Reactive Red 202 + H2O
-
Substrates: 98.8% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
Products: -
?
Reactive Violet 23 + H2O2 + H+
oxidized Reactive Violet 23 + H2O
-
Substrates: weak decolorization
Products: -
Products: -
?
Reactive Yellow 86 + H2O2 + H+
oxidized Reactive Yellow 86 + H2O
Q8YWM0
Substrates: 3% decolorization rate compared to Reactive Blue 5
Products: -
Products: -
?
Remazol Brilliant Blue R + H2O2
oxidized Remazol Brilliant Blue R + H2O
-
Substrates: -
Products: -
Products: -
?
Remazol Brilliant Blue R + H2O2 + H+
oxidized Remazol Brilliant Blue R + H2O
-
Substrates: -
Products: -
Products: -
?
syringaldehyde + H2O2 + H+
oxidized syringaldehyde + H2O
Q8YWM0
Substrates: 23% activity compared to guaiacol
Products: -
Products: -
?
trans-anethole + H2O2 + H+
4-anisaldehyde + H2O
Substrates: -
Products: -
Products: -
?
veratryl glycerol-beta-guaiacyl ether + H2O2 + H+
veratryl aldehyde + guaiacol + H2O
-
Substrates: -
Products: -
Products: -
?
1-amino-2-sulfonyl-4-aminomethyl-9,10-anthraquinone + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
1-amino-2-sulfonyl-4-aminomethyl-9,10-anthraquinone + H2O2 + H+
?
-
Substrates: isozyme Dyp1 exhibits 77% relative activity, isozyme DyP2 exhibits 85% relative activity, and isozyme Dyp3 exhibits 150% relative activity compared to Reactive Blue 5
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: about 92% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: 82% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: 65% activity compared to 2,6-dimethoxyphenol
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Irpex lacteus F17
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Pleurotus ostreatus HAUCC 162
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Xylaria grammica IHIA82
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
?
-
Substrates: 65% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
?
-
Substrates: 65% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
? + H2O
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
? + H2O
Substrates: -
Products: -
Products: -
?
2,4,5-trichlorophenol + H2O2 + H+
?
-
Substrates: 31% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
2,4,5-trichlorophenol + H2O2 + H+
?
-
Substrates: 64% activity compared to 2,6-dimethoxyphenol
Products: -
Products: -
?
2,4,5-trichlorophenol + H2O2 + H+
?
-
Substrates: 60% activity compared to 2,6-dimethoxyphenol
Products: -
Products: -
?
2,4-dichlorophenol + H2O2 + H+
?
-
Substrates: 100% activity
Products: -
Products: -
?
2,4-dichlorophenol + H2O2 + H+
?
-
Substrates: 100% activity with 2,4-dichlorophenol, 88% activity with H2O2
Products: -
Products: -
?
2,4-dichlorophenol + H2O2 + H+
?
-
Substrates: 70% activity compared to 2,6-dimethoxyphenol
Products: -
Products: -
?
2,4-dichlorophenol + H2O2 + H+
?
-
Substrates: 100% activity
Products: -
Products: -
?
2,4-dichlorophenol + H2O2 + H+
?
-
Substrates: 100% activity
Products: -
Products: -
?
2,6-dichlorophenol + H2O2 + H+
?
-
Substrates: 69% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
2,6-dichlorophenol + H2O2 + H+
?
-
Substrates: 66% activity compared to 2,6-dimethoxyphenol
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
?
Q8YWM0
Substrates: 31% activity compared to guaiacol
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
?
-
Substrates: 75% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
?
Substrates: 18.3% of the activity with Reactive Blue 5
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
?
Substrates: 18.3% of the activity with Reactive Blue 5
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
?
Substrates: 0.5% activity compared to Brilliant Green
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
?
-
Substrates: native DyP shows 9.3% activity, recombinant enzyme expressed in Escherichia coli shows 9.0% activity, and recombinant enzyme expressed in Aspergillus oryzae shows 8.1% activity compared to Reactive Blue 5
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
?
-
Substrates: isozyme Dyp1 exhibits 10% relative activity, isozyme DyP2 exhibits 11% relative activity, and isozyme Dyp3 exhibits 6.5% relative activity compared to Reactive Blue 5
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
?
Substrates: 4.0% activity compared to Reactive Blue 19
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
-
Substrates: 75% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
-
Substrates: 100% activity with 2,6-dimethoxyphenol, 95% activity with H2O2
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
Irpex lacteus F17
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
Streptomyces albidoflavus BSII#1
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
Xylaria grammica IHIA82
-
Substrates: -
Products: -
Products: -
?
2-dianisidine + H2O2 + H+
?
-
Substrates: 85% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
2-dianisidine + H2O2 + H+
?
-
Substrates: 91% activity compared to 2,6-dimethoxyphenol
Products: -
Products: -
?
4-chlorophenol + H2O2 + H+
?
-
Substrates: 25% activity compared to 2,6-dimethoxyphenol
Products: -
Products: -
?
4-chlorophenol + H2O2 + H+
?
-
Substrates: about 45% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
4-hydroxyacetophenone + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
4-hydroxybenzoic acid + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
4-hydroxybenzonitrile + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
Acid Blue 158 + H2O2 + H+
?
-
Substrates: highest decolorization activity (about 90% after 12 h)
Products: -
Products: -
?
Acid Blue 324 + H2O2 + H+
?
-
Substrates: efficient substrate
Products: -
Products: -
?
Acid Blue 324 + H2O2 + H+
?
-
Substrates: efficient substrate
Products: -
Products: -
?
Azure B + H2O2 + H+
?
Substrates: 13.2% activity compared to Brilliant Green
Products: -
Products: -
?
Azure B + H2O2 + H+
?
-
Substrates: approximately 30% decolourisation is observed after 24 h (0.001 mM dye)
Products: -
Products: -
?
Azure B + H2O2 + H+
?
Streptomyces albidoflavus BSII#1
-
Substrates: approximately 30% decolourisation is observed after 24 h (0.001 mM dye)
Products: -
Products: -
?
beta,beta-carotene + H2O2 + H+
beta-ionone + beta-apo-10'-carotenal + H2O
-
Substrates: -
Products: -
Products: -
?
beta,beta-carotene + H2O2 + H+
beta-ionone + beta-apo-10'-carotenal + H2O
-
Substrates: -
Products: -
Products: -
?
beta,beta-carotene + H2O2 + H+
beta-ionone + beta-apo-10'-carotenal + H2O
-
Substrates: -
Products: -
Products: -
?
beta,beta-carotene + H2O2 + H+
beta-ionone + beta-apo-10'-carotenal + H2O
-
Substrates: -
Products: -
Products: -
?
beta,beta-carotene + H2O2 + H+
beta-ionone + beta-apo-10'-carotenal + H2O
-
Substrates: -
Products: -
Products: -
?
beta,beta-carotene + H2O2 + H+
beta-ionone + beta-apo-10'-carotenal + H2O
-
Substrates: -
Products: -
Products: -
?
beta,beta-carotene + H2O2 + H+
beta-ionone + beta-apo-10'-carotenal + H2O
-
Substrates: -
Products: -
Products: -
?
beta,beta-carotene + H2O2 + H+
beta-ionone + beta-apo-10'-carotenal + H2O
-
Substrates: -
Products: -
Products: -
?
beta,beta-carotene + H2O2 + H+
beta-ionone + beta-apo-10'-carotenal + H2O
-
Substrates: -
Products: -
Products: -
?
beta,beta-carotene + H2O2 + H+
beta-ionone + beta-apo-10'-carotenal + H2O
-
Substrates: -
Products: -
Products: -
?
beta-carotene + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
Brilliant Green + H2O2 + H+
?
Substrates: 100% activity
Products: -
Products: -
?
Brilliant Green + H2O2 + H+
?
Substrates: 100% activity
Products: -
Products: -
?
catechol + H2O2 + H+
?
Substrates: low activity
Products: -
Products: -
?
Cibacet Brilliant Blue BG + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + H2O2 + H+
?
-
Substrates: 97% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
coniferyl alcohol + H2O2 + H+
?
-
Substrates: 97% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
coniferyl alcohol + H2O2 + H+
coniferaldehyde + H2O
-
Substrates: 97% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
coniferyl alcohol + H2O2 + H+
coniferaldehyde + H2O
-
Substrates: 65% activity compared to 2,6-dimethoxyphenol
Products: -
Products: -
?
Crystal Violet + H2O2 + H+
?
Substrates: 33.6% activity compared to Brilliant Green
Products: -
Products: -
?
guaiacol + H2O2 + H+
?
-
Substrates: 91% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
guaiacol + H2O2 + H+
?
-
Substrates: about 27% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
guaiacol + H2O2 + H+
?
-
Substrates: native DyP shows 9.2% activity, recombinant enzyme expressed in Escherichia coli shows 10% activity, and recombinant enzyme expressed in Aspergillus oryzae shows 6.0% activity compared to Reactive Blue 5
Products: -
Products: -
?
guaiacol + H2O2 + H+
?
-
Substrates: isozyme Dyp1 exhibits 5.6% relative activity, isozyme DyP2 exhibits 6.6% relative activity, and isozyme Dyp3 exhibits 37% relative activity compared to Reactive Blue 5
Products: -
Products: -
?
guaiacol + H2O2 + H+
?
Substrates: 0.7% activity compared to Reactive Blue 19
Products: -
Products: -
?
guaiacol + H2O2 + H+
?
Substrates: low activity
Products: -
Products: -
?
guaiacol + H2O2 + H+
oxidized guaiacol + H2O
-
Substrates: -
Products: -
Products: -
?
guaiacol + H2O2 + H+
oxidized guaiacol + H2O
-
Substrates: 55% activity compared to 2,6-dimethoxyphenol
Products: -
Products: -
?
guaiacol + H2O2 + H+
oxidized guaiacol + H2O
Substrates: -
Products: -
Products: -
?
guaiacol + H2O2 + H+
oxidized guaiacol + H2O
-
Substrates: -
Products: -
Products: -
?
guaiacol + H2O2 + H+
oxidized guaiacol + H2O
-
Substrates: -
Products: -
Products: -
?
guaiacol + H2O2 + H+
oxidized guaiacol + H2O
Substrates: -
Products: -
Products: -
?
guaiacol + H2O2 + H+
oxidized guaiacol + H2O
-
Substrates: -
Products: -
Products: -
?
guaiacol + H2O2 + H+
oxidized guaiacol + H2O
-
Substrates: -
Products: -
Products: -
?
guaiacol + H2O2 + H+
oxidized guaiacol + H2O
Substrates: -
Products: -
Products: -
?
guaiacol + H2O2 + H+
oxidized guaiacol + H2O
-
Substrates: -
Products: -
Products: -
?
guaiacylglycerol-beta-guaiacyl ether + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
guaiacylglycerol-beta-guaiacyl ether + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
guaiacylglycerol-beta-guaiacyl ether + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
guaiacylglycerol-beta-guaiacyl ether + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
?
guaiacylglycerol-beta-guaiacyl ether + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
guaiacylglycerol-beta-guaiacyl ether + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
humic acid + H2O2 + H+
?
-
Substrates: 81% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
humic acid + H2O2 + H+
?
-
Substrates: 75% activity compared to 2,6-dimethoxyphenol
Products: -
Products: -
?
isopropylglycerol-beta-guaifenesin + H2O2 + H+
veratrylaldehyde + ?
-
Substrates: -
Products: -
Products: -
?
isopropylglycerol-beta-guaifenesin + H2O2 + H+
veratrylaldehyde + ?
-
Substrates: -
Products: -
Products: -
?
L-DOPA + H2O2 + H+
?
-
Substrates: 26% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
L-DOPA + H2O2 + H+
?
-
Substrates: 70% activity compared to 2,6-dimethoxyphenol
Products: -
Products: -
?
Malachite Green + H2O2 + H+
?
Substrates: 73.63% decolorization after 30 min
Products: -
Products: -
?
Malachite Green + H2O2 + H+
?
Substrates: 73.63% decolorization after 30 min
Products: -
Products: -
?
Malachite Green + H2O2 + H+
?
-
Substrates: 94% decolorization after 1 h
Products: -
Products: -
?
Malachite Green + H2O2 + H+
?
Substrates: 68.6% activity compared to Brilliant Green
Products: -
Products: -
?
Methyl Violet + H2O2 + H+
?
Substrates: 63.89% decolorization after 30 min
Products: -
Products: -
?
Methyl Violet + H2O2 + H+
?
Substrates: 63.89% decolorization after 30 min
Products: -
Products: -
?
Mn2+ + H2O2 + H+
Mn3+ + 2 H2O
Substrates: -
Products: -
Products: -
?
o-dianisidine + H2O2 + H+
?
-
Substrates: 85% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
o-dianisidine + H2O2 + H+
?
-
Substrates: about 76% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
pyrogallol + H2O2 + H+
?
Q8YWM0
Substrates: 93% activity compared to guaiacol
Products: -
Products: -
?
pyrogallol + H2O2 + H+
?
-
Substrates: 80% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
pyrogallol + H2O2 + H+
?
-
Substrates: about 75% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
pyrogallol + H2O2 + H+
oxidized pyrogallol + H2O
-
Substrates: 80% activity compared to 2,4-dichlorophenol
Products: -
Products: -
?
pyrogallol + H2O2 + H+
oxidized pyrogallol + H2O
-
Substrates: 52% activity compared to 2,6-dimethoxyphenol
Products: -
Products: -
?
pyrogallol + H2O2 + H+
oxidized pyrogallol + H2O
Substrates: -
Products: -
Products: -
?
pyrogallol + H2O2 + H+
oxidized pyrogallol + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
Substrates: 16.4% of the activity with Reactive Blue 5
Products: -
Products: -
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
Substrates: 16.4% of the activity with Reactive Blue 5
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
?
Substrates: 7.8% activity compared to Brilliant Green
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
?
Substrates: 7.8% activity compared to Brilliant Green
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
Q8YWM0
Substrates: 8% decolorization rate compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
Substrates: 32.96% decolorization after 30 min
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
Substrates: 32.96% decolorization after 30 min
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
-
Substrates: weak decolorization, 0.5% activity of the native wild type enzyme compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
Substrates: -
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
-
Substrates: 54% decolorization after 30 min
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
-
Substrates: approximately 30% decolourisation is observed after 24 h (0.001 mM dye)
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
Streptomyces albidoflavus BSII#1
-
Substrates: approximately 30% decolourisation is observed after 24 h (0.001 mM dye)
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
-
Substrates: native DyP shows 1.0% activity, recombinant enzyme expressed in Escherichia coli shows 0.9% activity, and recombinant enzyme expressed in Aspergillus oryzae shows 1.0% activity compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
-
Substrates: 99.9% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
-
Substrates: recombinant DyP shows relatively low activity against azo dyes like Reactive Black 5
Products: -
Products: -
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
Substrates: poor decolorization, 1.4% activity compared to Reactive Blue 19
Products: -
Products: -
?
Reactive Blue 114 + H2O2 + H+
oxidized Reactive Blue 114 + H2O
Q8YWM0
Substrates: 187% decolorization rate compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Blue 114 + H2O2 + H+
oxidized Reactive Blue 114 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 114 + H2O2 + H+
oxidized Reactive Blue 114 + H2O
-
Substrates: native DyP shows 4.4% activity, recombinant enzyme expressed in Escherichia coli shows 2.4% activity, and recombinant enzyme expressed in Aspergillus oryzae shows 2.2% activity compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Blue 114 + H2O2 + H+
oxidized Reactive Blue 114 + H2O
-
Substrates: 100% decolorization rate after 10 days
Products: -
Products: -
?
Reactive Blue 114 + H2O2 + H+
oxidized Reactive Blue 114 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 182 + H2O2 + H+
oxidized Reactive Blue 182 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 182 + H2O2 + H+
oxidized Reactive Blue 182 + H2O
-
Substrates: 100% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
Products: -
?
Reactive Blue 19 + H2O2
?
Substrates: 10.5% activity compared to Brilliant Green
Products: -
Products: -
?
Reactive Blue 19 + H2O2
?
Substrates: 10.5% activity compared to Brilliant Green
Products: -
Products: -
?
Reactive Blue 19 + H2O2
oxidized Reactive Blue 5 + H2O
Substrates: 19% of the activity with Reactive Blue 5
Products: -
Products: -
?
Reactive Blue 19 + H2O2
oxidized Reactive Blue 5 + H2O
Substrates: 19% of the activity with Reactive Blue 5
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
?
-
Substrates: low activity
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
?
-
Substrates: low activity
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
-
Substrates: Remazol Brilliant Blue R
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
Q8YWM0
Substrates: 153% decolorization rate compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
-
Substrates: highest activity
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
-
Substrates: 92% activity of the native wild type enzyme compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
-
Substrates: 85% decolorization after less than 10 s
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
-
Substrates: native DyP shows 119% activity, recombinant enzyme expressed in Escherichia coli shows 102% activity, and recombinant enzyme expressed in Aspergillus oryzae shows 101% activity compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
-
Substrates: 100% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
-
Substrates: isozyme Dyp1 exhibits 94% relative activity, isozyme DyP2 exhibits 84% relative activity, and isozyme Dyp3 exhibits 160% relative activity compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
Substrates: 100% activity
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
-
Substrates: i.e. disodium;1-amino-9,10-dioxo-4-[3-(2-sulfonatooxyethylsulfonyl)anilino]anthracene-2-sulfonate
Products: -
Products: -
?
Reactive Blue 21 + H2O2 + H+
oxidized Reactive Blue 21 + H2O
-
Substrates: native DyP shows 26% activity, recombinant enzyme expressed in Escherichia coli shows 32% activity, and recombinant enzyme expressed in Aspergillus oryzae shows 25% activity compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Blue 21 + H2O2 + H+
oxidized Reactive Blue 21 + H2O
-
Substrates: 87.2% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
Products: -
?
Reactive Blue 21 + H2O2 + H+
oxidized Reactive Blue 21 + H2O
-
Substrates: isozyme Dyp1 exhibits 7.5% relative activity, isozyme DyP2 exhibits 9.6% relative activity, and isozyme Dyp3 exhibits 38% relative activity compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Blue 4 + H2O2 + H+
oxidized Reactive Blue 4 + H2O
Q8YWM0
Substrates: 64% decolorization rate compared to Reactive Blue 5
Products: -
Products: -
?
Reactive Blue 4 + H2O2 + H+
oxidized Reactive Blue 4 + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 4 + H2O2 + H+
oxidized Reactive Blue 4 + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 4 + H2O2 + H+
oxidized Reactive Blue 4 + H2O
Irpex lacteus F17
Substrates: -
Products: -
Products: -
?
Reactive Blue 4 + H2O2 + H+
oxidized Reactive Blue 4 + H2O
-
Substrates: approximately 30% decolourisation is observed after 24 h (0.001 mM dye)
Products: -
Products: -
?
Reactive Blue 4 + H2O2 + H+
oxidized Reactive Blue 4 + H2O
Streptomyces albidoflavus BSII#1
-
Substrates: approximately 30% decolourisation is observed after 24 h (0.001 mM dye)
Products: -
Products: -
?
Reactive Blue 4 + H2O2 + H+
oxidized Reactive Blue 4 + H2O
Substrates: 29.5% activity compared to Reactive Blue 19
Products: -
Products: -
?
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
4-amino-2-((4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl)amino)benzenesulfonic acid + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid + 4-amino-2-[(4-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
4-amino-2-((4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl)amino)benzenesulfonic acid + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid + 4-amino-2-[(4-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
4-amino-2-((4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl)amino)benzenesulfonic acid + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid + 4-amino-2-[(4-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
4-amino-2-((4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl)amino)benzenesulfonic acid + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid + 4-amino-2-[(4-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
4-amino-2-((4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl)amino)benzenesulfonic acid + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid + 4-amino-2-[(4-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
4-amino-2-((4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl)amino)benzenesulfonic acid + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid + 4-amino-2-[(4-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
4-amino-2-((4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl)amino)benzenesulfonic acid + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid + 4-amino-2-[(4-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
? + phthalic acid + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
? + phthalic acid + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
? + phthalic acid + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
? + phthalic acid + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
? + phthalic acid + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
? + phthalic acid + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
? + phthalic acid + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
? + phthalic acid + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
? + phthalic acid + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
? + phthalic acid + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
Q8YWM0
Substrates: 123% activity compared to guaiacol, the apparent optimum concentration of H2O2 required for the decolorization of Reactive Blue 5 by AnaPX is 0.4 mM
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: 100% activity
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
Irpex lacteus F17
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: the immobilized enzyme is able to decolorize Reactive Blue 5 at concentrations of 0.1, 0.05, and 0.01% (w/v) with efficiency rates of about 20, 29, and 45%, respectively
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: the immobilized enzyme is able to decolorize Reactive Blue 5 at concentrations of 0.1, 0.05, and 0.01% (w/v) with efficiency rates of about 20, 29, and 45%, respectively
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: native DyP and recombinant enzymes expressed in Escherichia coli and Aspergillus oryzae show 100% activity
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: 98.7% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: isozyme DyP1, Dyp2 and Dyp3 show 100% activity towards Reactive Blue 5
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: DyP decolorizes Reactive Blue 5 to 91% to light red-brown compounds
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
Xylaria grammica IHIA82
-
Substrates: -
Products: -
Products: -
?
Reactive Green 19 + H2O2 + H+
?
Substrates: 10.8% activity compared to Brilliant Green
Products: -
Products: -
?
Reactive Green 19 + H2O2 + H+
?
Substrates: 10.8% activity compared to Brilliant Green
Products: -
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?
Reactive Orange 13 + H2O2 + H+
oxidized Reactive Orange 13 + H2O
-
Substrates: native DyP shows 0.22% activity compared to Reactive Blue 5, recombinant enzymes expressed in Escherichia coli or in Aspergillus oryzae show no activity with Reactive Orange 13
Products: -
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?
Reactive Orange 13 + H2O2 + H+
oxidized Reactive Orange 13 + H2O
-
Substrates: 75.2% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
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?
Reactive Red 120 + H2O2 + H+
?
Substrates: 5.6% activity compared to Brilliant Green
Products: -
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?
Reactive Red 120 + H2O2 + H+
oxidized Reactive Red 120 + H2O
Q8YWM0
Substrates: 5% decolorization rate compared to Reactive Blue 5
Products: -
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?
Reactive Red 120 + H2O2 + H+
oxidized Reactive Red 120 + H2O
-
Substrates: native DyP shows 0.96% activity, recombinant enzyme expressed in Escherichia coli shows 0.61% activity compared to Reactive Blue 5, and recombinant enzyme expressed in Aspergillus oryzae shows no activity with Reactive Red 120
Products: -
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?
Reactive Red 120 + H2O2 + H+
oxidized Reactive Red 120 + H2O
-
Substrates: 92.9% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
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?
Reactive Red 123 + H2O2 + H+
oxidized Reactive Red 123 + H2O
-
Substrates: 100% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
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?
Reactive Red 123 + H2O2 + H+
oxidized Reactive Red 123 + H2O
-
Substrates: isozyme Dyp1 exhibits 0.72% relative activity, isozyme DyP2 exhibits 1.4% relative activity, and isozyme Dyp3 exhibits 0.8% relative activity compared to Reactive Blue 5
Products: -
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?
Reactive Red 225 + H2O2 + H+
oxidized Reactive Red 225 + H2O
-
Substrates: 100% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
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?
Reactive Red 225 + H2O2 + H+
oxidized Reactive Red 225 + H2O
-
Substrates: isozyme Dyp1 exhibits 8.2% relative activity, isozyme DyP2 exhibits 14% relative activity, and isozyme Dyp3 exhibits 9.9% relative activity compared to Reactive Blue 5
Products: -
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?
Reactive Red 33 + H2O2 + H+
oxidized Reactive Red 33 + H2O
-
Substrates: -
Products: -
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?
Reactive Red 33 + H2O2 + H+
oxidized Reactive Red 33 + H2O
-
Substrates: weak decolorization, 2% activity of the native wild type enzyme compared to Reactive Blue 5
Products: -
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?
Reactive Red 33 + H2O2 + H+
oxidized Reactive Red 33 + H2O
-
Substrates: native DyP shows 2.3 activity, recombinant enzyme expressed in Escherichia coli shows 1.8% activity, and recombinant enzyme expressed in Aspergillus oryzae shows 2.2% activity compared to Reactive Blue 5
Products: -
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?
Reactive Red 33 + H2O2 + H+
oxidized Reactive Red 33 + H2O
-
Substrates: recombinant DyP shows relatively low activity against azo dyes like Reactive Red 33
Products: -
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?
Reactive Yellow 2 + H2O2 + H+
?
Substrates: 39.7% activity compared to Brilliant Green
Products: -
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?
Reactive Yellow 2 + H2O2 + H+
?
Substrates: 39.7% activity compared to Brilliant Green
Products: -
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?
Reactive Yellow 2 + H2O2 + H+
oxidized Reactive Yellow 2 + H2O
-
Substrates: -
Products: -
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?
Reactive Yellow 2 + H2O2 + H+
oxidized Reactive Yellow 2 + H2O
-
Substrates: 2.6% activity of the native wild type enzyme compared to Reactive Blue 5
Products: -
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?
Reactive Yellow 2 + H2O2 + H+
oxidized Reactive Yellow 2 + H2O
-
Substrates: 44.4% decolorization rate after 10 days compared to Reactive Blue 114
Products: -
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?
Remazol Brilliant Blue Reactif + H2O2 + H+
?
-
Substrates: highest decolorization activity (about 90% after 12 h)
Products: -
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?
Remazol Brilliant Blue Reactif + H2O2 + H+
?
-
Substrates: -
Products: -
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?
Remazol Brilliant Blue Reactif + H2O2 + H+
?
-
Substrates: -
Products: -
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?
signayl alcohol + H2O2 + H+
signaldehyde + H2O
-
Substrates: 94% activity compared to 2,4-dichlorophenol
Products: -
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?
signayl alcohol + H2O2 + H+
signaldehyde + H2O
-
Substrates: 68% activity compared to 2,6-dimethoxyphenol
Products: -
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?
Vat Blue 6 + H2O2
oxidized Vat Blue 6 + H2O
Substrates: 5.1% of the activity with Reactive Blue 5
Products: -
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?
Vat Blue 6 + H2O2
oxidized Vat Blue 6 + H2O
Substrates: 5.1% of the activity with Reactive Blue 5
Products: -
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?
veratryl alcohol + H2O2 + H+
?
Substrates: very weak substrate
Products: -
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?
veratryl alcohol + H2O2 + H+
?
-
Substrates: 99% activity compared to 2,4-dichlorophenol
Products: -
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?
veratryl alcohol + H2O2 + H+
?
-
Substrates: 99% activity compared to 2,4-dichlorophenol
Products: -
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?
veratryl alcohol + H2O2 + H+
?
Substrates: 0.2% activity compared to Brilliant Green
Products: -
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?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Substrates: oxidation occurs only at acidic pHs
Products: -
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?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Substrates: maximum oxidation activity at pH 1.4
Products: -
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?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Substrates: -
Products: -
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?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Substrates: -
Products: -
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?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Substrates: 99% activity compared to 2,4-dichlorophenol
Products: -
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?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Substrates: 72% activity compared to 2,6-dimethoxyphenol
Products: -
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?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
Substrates: -
Products: -
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?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Substrates: -
Products: -
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?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
Substrates: 0.2% activity compared to Reactive Blue 19
Products: -
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?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Substrates: -
Products: -
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?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
Xylaria grammica IHIA82
-
Substrates: -
Products: -
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?
veratrylglycerol-beta-guaiacyl ether + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
veratrylglycerol-beta-guaiacyl ether + H2O2 + H+
?
Substrates: -
Products: -
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?
veratrylglycerol-beta-guaiacyl ether + H2O2 + H+
?
Substrates: -
Products: -
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?
veratrylglycerol-beta-guaiacyl ether + H2O2 + H+
?
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with veratryl alcohol and veratrylglycerol-beta-guaiacyl ether
Products: -
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?
additional information
?
-
Q8YWM0
Substrates: the decolorization activity of AnaPX toward azo dyes is relatively low. No decolorization of Toluidine Blue O, Reactive Red 33, and Reactive Yellow 2 is observed
Products: -
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?
additional information
?
-
-
Substrates: Mn2+ is not oxidized
Products: -
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?
additional information
?
-
Substrates: no activity with Mn2+, veratryl alcohol and guaiacylglycerol-beta-guaiacyl ether
Products: -
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?
additional information
?
-
-
Substrates: no activity with thioanisole
Products: -
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?
additional information
?
-
-
Substrates: no activity with 2,4,6-trichlorophenol, 4-chlorophenol, and pentachlorophenol
Products: -
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?
additional information
?
-
-
Substrates: higher decolorizing activity is observed for anthraquinone dyes than for azo dyes. DyP does not oxidize veratryl alcohol
Products: -
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?
additional information
?
-
-
Substrates: veratryl alcohol, Reactive Red 123, Reactive Orange 13, and Reactive Yellow 2 are not decolorized by the recombinant enzyme
Products: -
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?
additional information
?
-
Substrates: the enzyme has an oxidase function in addition to a peroxidase activity
Products: -
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?
additional information
?
-
-
Substrates: the enzyme has an oxidase function in addition to a peroxidase activity
Products: -
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?
additional information
?
-
Substrates: the enzyme lacks the typical activity towards anthraquinone dyes like Reactive Blue 19 and Reactive Black 5
Products: -
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?
additional information
?
-
-
Substrates: the enzyme lacks the typical activity towards anthraquinone dyes like Reactive Blue 19 and Reactive Black 5
Products: -
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?
additional information
?
-
-
Substrates: the enzyme also successfully catalyses coupling reactions between several phenolic monomer pairs including catechin-caffeic acid, catechin-catechol, catechin-guaiacol and guaiacol-syringaldazine
Products: -
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?
additional information
?
-
-
Substrates: no activity with 3-hydroxyanthranilic acid, 4-methylcatechol, L-tyrosine, 4-cresol, resorcinol, and syringaldazine
Products: -
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?
additional information
?
-
-
Substrates: no activity with AQ-2, M303, Reactive Black 5, and Reactive Red 33
Products: -
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?
additional information
?
-
-
Substrates: no activity with AQ-2, M303, Reactive Black 5, and Reactive Red 33
Products: -
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?
additional information
?
-
-
Substrates: no activity with commercial humic acid
Products: -
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?
additional information
?
-
-
Substrates: DyP shows both dye-decolorizing and lignin-degrading activities when H2O2 is added
Products: -
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?
additional information
?
-
-
Substrates: native and recombinant DyPs do not oxidize veratryl alcohol
Products: -
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?
additional information
?
-
-
Substrates: DyP shows both dye-decolorizing and lignin-degrading activities when H2O2 is added
Products: -
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?
additional information
?
-
-
Substrates: isozymes DyP1, Dyp2 and Dyp3 do not oxidize veratryl alcohol and Reactive Red 202
Products: -
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?
additional information
?
-
-
Substrates: Reactive Red 187 and veratryl alcohol are no substrates of DyP
Products: -
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?
additional information
?
-
Substrates: the enzyme does not function as a catalase-peroxidase
Products: -
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?
additional information
?
-
Substrates: the enzyme is inactive toward 2,6-dimethoxyphenol, 2,4-dichlorophenol, veratryl alcohol, and Reactive Black 5
Products: -
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?
additional information
?
-
-
Substrates: the enzyme is inactive toward 2,6-dimethoxyphenol, 2,4-dichlorophenol, veratryl alcohol, and Reactive Black 5
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with veratryl alcohol and veratrylglycerol-beta-guaiacyl ether
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is inactive toward 2,6-dimethoxyphenol, 2,4-dichlorophenol, veratryl alcohol, and Reactive Black 5
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
-
Substrates: -
Products: -
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?
Reactive Blue 5 + 2 H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
-
Substrates: -
Products: -
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?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
Substrates: -
Products: -
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?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
DyP contains one heme with an iron at the center of the molecule
heme
Q8YWM0
iron protoporphyrin-containing heme peroxidase, the heme content is estimated to be 0.91 mol per mole of protein
heme
enzyme displays typical heme absorbance of Soret band, with an Rz value of 1.18
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
Ca2+
Co2+
Cu2+
Iron
DyP contains one heme with an iron at the center of the molecule
Mg2+
Mn2+
Zn2+
additional information
Mg2+
-
180% activity at 5 mM. The addition of 5 mM of Mg2+ enhances the thermostability of the enzyme
Mn2+
-
225% activity at 5 mM. The addition of 5 mM of Mn2+ enhances the thermostability of the enzyme
Mn2+
highest activity in the presence of 25 mM Mn2+. The enzyme activity rises with increasing Mn2+ concentration, but is not completely dependent on the addition of Mn2+
Mn2+
-
about 139% activity at 1 mM. The addition of 1 mM of Mn2+ also enhances the thermostability of the enzyme
additional information
-
the enzyme shows manganese-independent peroxidase activity
additional information
-
not significantly affected by Zn2+, Fe2+, and Li+
additional information
-
not significantly affected by Mg2+, Ba2+, Li+, and K+
additional information
-
no enhancement of the DyP activity by the addition of Mn2+ is observed
additional information
-
the oxidation of 2,6-dimethoxyphenol and guaiacol by rDyP occurs without the addition of Mn2+, and no enhancement of activity by the addition of Mn21 is observed
additional information
not influenced by Zn2+, Ba2+, Mg2+, Fe2+, and EDTA
additional information
-
not influenced by Zn2+, Ba2+, Mg2+, Fe2+, and EDTA
additional information
-
not affected by Ca2+, Co2+, Fe2+, Mg2+, Mn2+, and Zn2+
additional information
-
Cu2+, Mg2+, Zn2+, and Fe2+ do not exert significant effects on enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
55% residual activity at 1 mM; 70% residual activity at 1 mM
4-arbutin
-
24.2% inhibition at 1.0 mM, 66.4% inhibition at 50 mM
-
ascorbate
-
39.5% inhibition at 0.05 mM, complete inhibition at 0.5 mM
dithiothreitol
-
65% residual activity at 1 mM; 81% residual activity at 1 mM
hydroxylamine
-
10% residual activity at 2 mM; 25% residual activity at 2 mM
KCN
Q8YWM0
AnaPX shows very low sensitivity to KCN which causes only 9% and 14% inhibition of the activity at 1 and 10 mM, respectively
L-cysteine
-
33.9% inhibition at 0.02 mM, complete inhibition at 0.1 mM
Metabisulfite
-
93.5% inhibition at 0.5 mM, complete inhibition at 1.0 mM
phenylhydrazine
Q8YWM0
AnaPX is highly sensitive to the suicide substrate phenylhydrazine (complete inhibition at 1 mM)
H2O2
-
DyP activity for Reactive Blue 5 is inhibited when the H2O2 concentration exceeds 0.2 mM at a fixed DyP concentration of 0.6 nM. At 2.8 nM of DyP, its activity for 1,4-diamino-2-sodium anthraquinone sulfonate decreases sharply when the H2O2 concentration exceeds 0.1 mM
H2O2
-
maximum relative activity at final H2O2 concentrations between 0.4 and 0.8 mM, activity then gradually drops off. A residual activity of 30% still remains at 12.5 mM H2O2, and the enzyme is completely inactivated in the presence of 50 mM H2O2
H2O2
-
the protein becomes progressively inactivated with increasing incubation time and peroxide concentration, detecting the highest inactivation above 100000 molar equivalents. Around 80% inactivation is observed with 3000 molar equivalents in 5 min, and the protein is completely deactivated after 10 min. The activity of the recombinant protein falls below 20% in 60 min of incubation at all the hydrogen peroxide concentrations tested
H2O2
an increase of the hydrogen peroxide concentration of more than 0.1 mM leads to a continuous activity decrease
potassium cyanide
-
3% residual activity at 10 mM; complete inhibition at 10 mM
SDS
-
27% inhibition at 20 mM; 68% residual activity at 20 mM; 73% residual activity at 20 mM
Sodium azide
-
5% residual activity at 10 mM; complete inhibition at 10 mM
additional information
Q8YWM0
the enzyme is not sensitive to the prototypical catalase inhibitor 3-amino-1,2,4,-triazole in the presence of ascorbic acid (1.0 mM), metal chelating and sulfhydryl reagents do not significantly affect activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2O2
-
the maximum activity is obtained with an initial H2O2 concentration of about 0.33 mM
syringaldehyde
Q8YWM0
the presence of syringaldehyde drastically enhances the rate of decolorization of Reactive Black 5, Reactive Orange 14, Reactive Red 120, Reactive Green 19, and Acid Red with 50fold, 9fold, 15fold, 2fold, and 7fold improvements, respectively
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.084
1-amino-4-methylamino-2-sodium anthraquinone sulfonate
-
at pH 3.2 and 30°C
0.448
veratrylglycerol-beta-guaiacyl ether
at pH 3.0 and 25°C
0.00023
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme D222A, at pH 3.0 and 25°C
0.0015
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
recombinant wild type enzyme, at pH 3.0 and 25°C
0.0033
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme D222E, at pH 3.0 and 25°C
0.0085
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 30°C
0.011
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme R390A, at pH 3.0 and 25°C
0.013
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH and temperature not specified in the publication
0.013
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme R390K, at pH 3.0 and 25°C
0.015
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild type enzyme, at pH 3.0 and 22°C
0.015
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme D222E/R390K, at pH 3.0 and 25°C
0.018
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild type enzyme, at pH 3.0 and 25°C
0.01947
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W264R, at pH 3.5 and 35°C
0.02
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
manganese-independent peroxidase I, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
0.02
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
manganese-independent peroxidase II, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
0.028
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3,0, temperature not specified in the publication
0.028
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
native wild type enzyme, at pH 3.0 and 25°C
0.037
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 4.0 and 30°C
0.041
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.5 and 25°C
0.06
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 7.0 and 25°C
0.0623
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W264Y, at pH 3.5 and 35°C
0.06321
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W147F, at pH 3.5 and 35°C
0.06644
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W109F, at pH 3.5 and 35°C
0.06729
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild type enzyme, at pH 3.5 and 35°C
0.0689
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W264H, at pH 3.5 and 35°C
0.07148
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W212F, at pH 3.5 and 35°C
0.07187
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W264F, at pH 3.5 and 35°C
0.099
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.8 and 30°C
0.121
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild type enzyme, at pH 3.0 and 25°C
0.123
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.0 and 25°C
0.1521
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 30°C
0.165
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.0 and 25°C
0.166
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 30°C
0.18
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 8.0 and 25°C
0.1875
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 30°C
0.22
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme E188K, at pH 4.3 and 25°C
0.26
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme A142V, at pH 5.5 and 25°C
0.27507
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W380Y, at pH 3.5 and 35°C
0.28
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme E188K/H125R, at pH 4.3 and 25°C
0.283
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild type enzyme, at pH 3.0 and 30°C
0.309
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.0 and 25°C
0.5
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme H125R, at pH 4.3 and 25°C
0.7
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild type enzyme, at pH 5.0 and 25°C
0.752
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W380F, at pH 3.5 and 35°C
0.79
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.5 and 30°C
1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme E188K/A142V, at pH 5.5 and 25°C
1.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme E188K/A142V/H125Y, at pH 5.5 and 25°C
1.2
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 25°C
1.3
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme Y288F, at pH 5.0 and 25°C
1.5873
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 30°C
1.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme Y437F, at pH 5.0 and 25°C
2.5
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild type enzyme, at pH 4.3 and 25°C
2.5
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 5.0 and 30°C
2.75
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W377S, at pH 3.0 and 25°C
4.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 4.0 and 25°C
6.3
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme Y374F, at pH 5.0 and 25°C
0.023
2,6-dimethoxyphenol
-
manganese-independent peroxidase II, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
0.027
2,6-dimethoxyphenol
-
manganese-independent peroxidase I, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
0.058
2,6-dimethoxyphenol
-
mutant enzyme E188K/A142V/H125Y, at pH 5.5 and 25°C
0.0726
2,6-dimethoxyphenol
-
pH 3.0, temperature not specified in the publication
0.703
2,6-dimethoxyphenol
wild type enzyme, at pH 3.0 and 25°C
1.32
2,6-dimethoxyphenol
wild type enzyme, at pH 3.0 and 30°C
0.179
guaiacylglycerol-beta-guaiacyl ether
at pH 3.0 and 25°C
0.005
H2O2
-
manganese-independent peroxidase II, using 2,2'-azino-bis(3-ethylthiazoline)-6-sulfonate as cosubstrate, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
0.007
H2O2
-
with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 4.0 and 30°C
0.01
H2O2
-
manganese-independent peroxidase I, using 2,2'-azino-bis(3-ethylthiazoline)-6-sulfonate as cosubstrate, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
0.011
H2O2
-
mutant enzyme E201D, with Reactive Blue 19 as cosubstrate, at pH 5.0, temperature not specified in the publication
0.033
H2O2
with hydroquinone as cosubstrate, wild type enzyme, at pH 3.0 and 22°C
0.033
H2O2
-
wild type enzyme, with Reactive Blue 19 as cosubstrate, at pH 5.0, temperature not specified in the publication
0.036
H2O2
-
using 1-amino-4-methylamino-2-sodium anthraquinone sulfonate as cosubstrate, at pH 3.2 and 30°C
0.0395
H2O2
-
recombinant wild type enzyme, with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 3.0 and 25°C
0.077
H2O2
with guaiacol as cosubstrate, wild type enzyme, at pH 3.0 and 22°C
0.079
H2O2
-
with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 5.0 and 30°C
0.0795
H2O2
-
native wild type enzyme, with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 3.0 and 25°C
0.084
H2O2
with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, wild type enzyme, at pH 3.0 and 22°C
2
H2O2
with guaiacol as cosubstrate, mutant enzyme D220A, at pH 3.0 and 22°C
11
H2O2
with guaiacol as cosubstrate, mutant enzyme H312C, at pH 3.0 and 22°C
0.005
Reactive Black 5
-
manganese-independent peroxidase I, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C
0.007
Reactive Black 5
-
manganese-independent peroxidase II, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C
0.017
Reactive Blue 19
-
wild type enzyme, at pH 5.0, temperature not specified in the publication
0.029
Reactive Blue 19
in 25 mM citrate buffer (pH 3.5), at 25°C
0.036
Reactive Blue 19
-
mutant enzyme E201D, at pH 5.0, temperature not specified in the publication
0.08
Reactive Blue 19
pH and temperature not specified in the publication
0.0106
Reactive Blue 5
mutant enzyme W377S, at pH 3.5 and 25°C
0.015
Reactive Blue 5
-
manganese-independent peroxidase II, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C
0.0156
Reactive Blue 5
wild type enzyme, at pH 3.5 and 25°C
0.023
Reactive Blue 5
-
manganese-independent peroxidase I, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C
0.084
Reactive Blue 5
in 25 mM citrate buffer, pH 3.2, at 25°C
1.779
veratryl alcohol
-
manganese-independent peroxidase I, at pH 2.5 in sodium tartrate buffer (50 mM), at 20°C
2.89
veratryl alcohol
-
manganese-independent peroxidase II, at pH 2.5 in sodium tartrate buffer (50 mM), at 20°C
7.36
veratryl alcohol
mutant enzyme W377S, at pH 2.5 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
270
1-amino-4-methylamino-2-sodium anthraquinone sulfonate
-
at pH 3.2 and 30°C
0.3
veratrylglycerol-beta-guaiacyl ether
at pH 3.0 and 25°C
0.02
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 30°C
0.036
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme D222A, at pH 3.0 and 25°C
0.14
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme R390A, at pH 3.0 and 25°C
0.96
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 30°C
1.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild type enzyme, at pH 5.0 and 25°C
1.15
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 30°C
1.21
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.5 and 30°C
1.3
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme Y288F, at pH 5.0 and 25°C
1.5
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme Y437F, at pH 5.0 and 25°C
1.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme Y374F, at pH 5.0 and 25°C
2.5
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme D222E, at pH 3.0 and 25°C
2.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 25°C
4.4
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme A142V, at pH 5.5 and 25°C
5
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme D222E/R390K, at pH 3.0 and 25°C
5.4
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild type enzyme, at pH 3.0 and 25°C
6.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 4.0 and 30°C
7.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme R390K, at pH 3.0 and 25°C
12
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.5 and 25°C
15
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme E188K/A142V, at pH 5.5 and 25°C
15
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme E188K/A142V/H125Y, at pH 5.5 and 25°C
23
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild type enzyme, at pH 4.3 and 25°C
26
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme H125R, at pH 4.3 and 25°C
30
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.0 and 25°C
49.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
recombinant wild type enzyme, at pH 3.0 and 25°C
52.78
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W264R, at pH 3.5 and 35°C
53
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.0 and 25°C
69
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme E188K/H125R, at pH 4.3 and 25°C
76.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 7.0 and 25°C
87
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH and temperature not specified in the publication
88.38
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W380Y, at pH 3.5 and 35°C
89.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 4.0 and 25°C
128
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme E188K, at pH 4.3 and 25°C
171
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W377S, at pH 3.0 and 25°C
224
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3,0, temperature not specified in the publication
224
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild type enzyme, at pH 3.0 and 25°C
224
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
native wild type enzyme, at pH 3.0 and 25°C
225
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.0 and 25°C
243.13
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W264Y, at pH 3.5 and 35°C
260
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild type enzyme, at pH 3.0 and 22°C
316.16
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W380F, at pH 3.5 and 35°C
322
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
manganese-independent peroxidase II, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
368
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
manganese-independent peroxidase I, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
375
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.8 and 30°C
384.85
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W264F, at pH 3.5 and 35°C
500
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 8.0 and 25°C
602.5
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W109F, at pH 3.5 and 35°C
654
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild type enzyme, at pH 3.0 and 30°C
665.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W212F, at pH 3.5 and 35°C
684.34
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W264H, at pH 3.5 and 35°C
786.7
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W147F, at pH 3.5 and 35°C
790
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild type enzyme, at pH 3.5 and 35°C
0.07
2,6-dimethoxyphenol
-
pH and temperature not specified in the publication
6
2,6-dimethoxyphenol
-
mutant enzyme E188K/A142V/H125Y, at pH 5.5 and 25°C
70.9
2,6-dimethoxyphenol
-
pH 3.0, temperature not specified in the publication
89
2,6-dimethoxyphenol
-
manganese-independent peroxidase II, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
90
2,6-dimethoxyphenol
-
manganese-independent peroxidase I, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
120
2,6-dimethoxyphenol
wild type enzyme, at pH 3.0 and 25°C
420
2,6-dimethoxyphenol
wild type enzyme, at pH 3.0 and 30°C
12
guaiacylglycerol-beta-guaiacyl ether
at pH 3.0 and 25°C
0.36
H2O2
with guaiacol as cosubstrate, wild type enzyme, at pH 3.0 and 22°C
0.58
H2O2
with guaiacol as cosubstrate, mutant enzyme H312C, at pH 3.0 and 22°C
0.59
H2O2
with guaiacol as cosubstrate, mutant enzyme D220A, at pH 3.0 and 22°C
27
H2O2
with hydroquinone as cosubstrate, wild type enzyme, at pH 3.0 and 22°C
145.3
H2O2
-
recombinant wild type enzyme, with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 3.0 and 25°C
238
H2O2
-
manganese-independent peroxidase II, using 2,2'-azino-bis(3-ethylthiazoline)-6-sulfonate as cosubstrate, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
268
H2O2
-
manganese-independent peroxidase I, using 2,2'-azino-bis(3-ethylthiazoline)-6-sulfonate as cosubstrate, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
280
H2O2
with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, wild type enzyme, at pH 3.0 and 22°C
419
H2O2
-
native wild type enzyme, with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 3.0 and 25°C
3
Reactive Black 5
-
manganese-independent peroxidase I, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C
3
Reactive Black 5
-
manganese-independent peroxidase II, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C
0.22
Reactive Blue 19
-
wild type enzyme, at pH 5.0, temperature not specified in the publication
2.88
Reactive Blue 19
-
mutant enzyme E201D, at pH 5.0, temperature not specified in the publication
980
Reactive Blue 19
pH and temperature not specified in the publication
0.7
Reactive Blue 5
mutant enzyme W377S, at pH 3.5 and 25°C
5.9
Reactive Blue 5
in 25 mM citrate buffer, pH 3.2, at 25°C
114
Reactive Blue 5
-
manganese-independent peroxidase I, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C
256
Reactive Blue 5
-
manganese-independent peroxidase II, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C
0.065
veratryl alcohol
-
pH and temperature not specified in the publication
0.23
veratryl alcohol
mutant enzyme W377S, at pH 2.5 and 25°C
0.62
veratryl alcohol
-
manganese-independent peroxidase II, at pH 2.5 in sodium tartrate buffer (50 mM), at 20°C
0.86
veratryl alcohol
-
manganese-independent peroxidase I, at pH 2.5 in sodium tartrate buffer (50 mM), at 20°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3200
1-amino-4-methylamino-2-sodium anthraquinone sulfonate
-
at pH 3.2 and 30°C
0.7
veratrylglycerol-beta-guaiacyl ether
at pH 3.0 and 25°C
1.1
1,2-phenylenediamine
-
mutant enzyme E188K/A142V/H125Y, at pH 8.0 and 25°C
18
1,4-phenylenediamine
-
mutant enzyme E188K/A142V/H125Y, at pH 8.0 and 25°C
1.71
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.5 and 30°C
2.4
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 25°C
2.43
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 30°C
6.12
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 30°C
6.31
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 30°C
8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 5.0 and 30°C
9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild type enzyme, at pH 4.3 and 25°C
12
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme R390A, at pH 3.0 and 25°C
14
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme E188K/A142V/H125Y, at pH 5.5 and 25°C
15
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme E188K/A142V, at pH 5.5 and 25°C
17
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme A142V, at pH 5.5 and 25°C
21.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 4.0 and 25°C
52
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme H125R, at pH 4.3 and 25°C
60
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme E188K, at pH 4.3 and 25°C
62
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W377S, at pH 3.0 and 25°C
70
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 30°C
150
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme D222A, at pH 3.0 and 25°C
170
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.0 and 25°C
180
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.0 and 25°C
184
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 4.0 and 30°C
250
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme E188K/H125R, at pH 4.3 and 25°C
287
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.5 and 25°C
290
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild type enzyme, at pH 3.0 and 25°C
321
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W380Y, at pH 3.5 and 35°C
330
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme D222E/R390K, at pH 3.0 and 25°C
420
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W380F, at pH 3.5 and 35°C
530
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme R390K, at pH 3.0 and 25°C
770
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme D222E, at pH 3.0 and 25°C
1276.57
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 7.0 and 25°C
1800
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.0 and 25°C
1850
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild type enzyme, at pH 3.0 and 25°C
2300
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild type enzyme, at pH 3.0 and 30°C
2710
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W264R, at pH 3.5 and 35°C
3800
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.8 and 30°C
3900
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W264Y, at pH 3.5 and 35°C
5350
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W264F, at pH 3.5 and 35°C
6600
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH and temperature not specified in the publication
8000
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
native wild type enzyme, at pH 3.0 and 25°C
9030
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W109F, at pH 3.5 and 35°C
9300
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W212F, at pH 3.5 and 35°C
9930
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W264H, at pH 3.5 and 35°C
11700
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild type enzyme, at pH 3.5 and 35°C
12500
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant enzyme W147F, at pH 3.5 and 35°C
17000
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild type enzyme, at pH 3.0 and 22°C
33000
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
recombinant wild type enzyme, at pH 3.0 and 25°C
2.9
2,5-diaminobenzenesulfonic acid
-
wild type enzyme, at pH 4.3 and 25°C
3.8
2,5-diaminobenzenesulfonic acid
-
mutant enzyme E188K/A142V/H125Y, at pH 8.0 and 25°C
110
2,6-dimethoxyphenol
-
mutant enzyme E188K/A142V/H125Y, at pH 5.5 and 25°C
200
2,6-dimethoxyphenol
wild type enzyme, at pH 3.0 and 25°C
320
2,6-dimethoxyphenol
wild type enzyme, at pH 3.0 and 30°C
3300
2,6-dimethoxyphenol
-
manganese-independent peroxidase I, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
3900
2,6-dimethoxyphenol
-
manganese-independent peroxidase II, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
420
4-aminodiphenylamine
-
mutant enzyme E188K/A142V/H125Y, at pH 5.0 and 25°C
67
guaiacylglycerol-beta-guaiacyl ether
at pH 3.0 and 25°C
0.053
H2O2
with guaiacol as cosubstrate, mutant enzyme H312C, at pH 3.0 and 22°C
0.21
H2O2
with guaiacol as cosubstrate, mutant enzyme D220A, at pH 3.0 and 22°C
4.7
H2O2
with guaiacol as cosubstrate, wild type enzyme, at pH 3.0 and 22°C
180
H2O2
-
with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 5.0 and 30°C
820
H2O2
with hydroquinone as cosubstrate, wild type enzyme, at pH 3.0 and 22°C
2000
H2O2
-
with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 4.0 and 30°C
3400
H2O2
with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, wild type enzyme, at pH 3.0 and 22°C
3680
H2O2
-
recombinant wild type enzyme, with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 3.0 and 25°C
5300
H2O2
-
native wild type enzyme, with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 3.0 and 25°C
27000
H2O2
-
manganese-independent peroxidase I, using 2,2'-azino-bis(3-ethylthiazoline)-6-sulfonate as cosubstrate, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
48000
H2O2
-
manganese-independent peroxidase II, using 2,2'-azino-bis(3-ethylthiazoline)-6-sulfonate as cosubstrate, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C
410
Reactive Black 5
-
manganese-independent peroxidase II, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C
570
Reactive Black 5
-
manganese-independent peroxidase I, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C
13
Reactive Blue 19
-
wild type enzyme, at pH 5.0, temperature not specified in the publication
80
Reactive Blue 19
-
mutant enzyme E201D, at pH 5.0, temperature not specified in the publication
5000
Reactive Blue 5
-
manganese-independent peroxidase I, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C
17000
Reactive Blue 5
-
manganese-independent peroxidase II, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C
0.032
veratryl alcohol
mutant enzyme W377S, at pH 2.5 and 25°C
0.096
veratryl alcohol
wild type enzyme, at pH 2.5 and 25°C
0.22
veratryl alcohol
-
manganese-independent peroxidase II, at pH 2.5 in sodium tartrate buffer (50 mM), at 20°C
0.48
veratryl alcohol
-
manganese-independent peroxidase I, at pH 2.5 in sodium tartrate buffer (50 mM), at 20°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.032
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme D222E/R390K, at pH 3.0 and 25°C
0.047
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme R390K, at pH 3.0 and 25°C
0.072
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild type enzyme, at pH 3.0 and 25°C
0.079
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme D222A, at pH 3.0 and 25°C
0.09
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme D222E, at pH 3.0 and 25°C
0.19
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant enzyme R390A, at pH 3.0 and 25°C
13
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 25°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.2
mutant enzyme D171N, at 30°C, pH not specified in the publication
1.8
-
DyP, using Reactive Black 5 as substrate, in 0.1 M sodium tartrate buffer (pH 3.0), at 30°C
1478
Q8YWM0
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using 4-aminoantipyrine as substrate
18.6
-
after 60fold purification, with 2,6-dimethoxyphenol as substrate, at pH 4.0 and 50°C
204
Q8YWM0
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using 2,2'-azino-bis(3-ethylbenzthiazoline)-6-sulfonic acid as substrate
216
Q8YWM0
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using pyrogallol as substrate
230
Q8YWM0
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using guaiacol as substrate
270
-
DyP, using Reactive Blue 19 as substrate, in 0.1 M sodium tartrate buffer (pH 3.0), at 30°C
283
Q8YWM0
recombinant enzyme after 50.5fold purification, using Reactive Blue 5 as substrate, pH 4.0-4.4, at 37°C
290
Q8YWM0
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using L-ascorbate as substrate
308
331
-
after 14.8fold purification, at 30°C, pH not specified in the publication
34
-
DyP, using guaiacol as substrate, in 0.1 M sodium tartrate buffer (pH 3.0), at 30°C
340
-
DyP, using Reactive Blue 5 as substrate, in 0.1 M sodium tartrate buffer (pH 3.0), at 30°C
347.8
-
manganese-independent peroxidase II after 12.2fold purification, at pH 3.0 and 20°C
37.8
-
substrate 2,2'-azino-bis(3-ethylthiazoline)-6-sulfonate, pH 5.0, temperature not specified in the publication
374
Q8YWM0
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using NADH as substrate
4.2
-
DyP, using Reactive Red 33 as substrate, in 0.1 M sodium tartrate buffer (pH 3.0), at 30°C
469
-
manganese-independent peroxidase I after 16.5fold purification, at pH 3.0 and 20°C
5.6
Q8YWM0
recombinant enzyme from crude extract, using Reactive Blue 5 as substrate, pH 4.0-4.4, at 37°C
54
Q8YWM0
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using syringaldehyde as substrate
57
-
after 210fold purification, in 25 mM citrate buffer (pH 3.2), at 30°C
600
wild type enzyme, at 30°C, pH not specified in the publication
66.8
-
with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), at pH 3.0 and 50°C
7.5
-
DyP, using Reactive Blue 114 as substrate, in 0.1 M sodium tartrate buffer (pH 3.0), at 30°C
71
Q8YWM0
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using 2,6-dimethoxyphenol as substrate
834
-
recombinant enzyme after 14385fold purification, at 30°C, pH 3.2
9.12
-
after 48fold purification, with 2,6-dimethoxyphenol as substrate, at pH 3.0 and 70°C
308
Q8YWM0
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using D-isoascorbate as substrate
308
Q8YWM0
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using NADPH as substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.4
3.2
3.5
4.5
8
-
the enzyme has two pH optima at 3.0 and 8.0, depending on substrate
1.4
-
maximum activity at pH 1.4 using veratryl alcohol as substrate
3
-
using 1-amino-4-methylamino-2-sodium anthraquinone sulfonate as substrate
3
-
Reactive Blue 19 and Reactive Black 5 decolorization and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) oxidation are maximal at pH 3.0
3
-
the enzyme has two pH optima at 3.0 and 8.0, depending on substrate
3.2
-
using Reactive Blue 5, Reactive Blue 19, 1-amino-4-(3-amino-4-sodium-sulfonoanilino)-2-sodium anthraquinone sulfonate, 1,4-diamino-2-sodium anthraquinone sulfonate, Reactive Black 5, Reactive Red 33, or Reactive Yellow 2 as substrate
3.5
for Reactive Blue 19-decolorizing activity in 25 mM citrate buffer
4
optimum pH for oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), pyrogallol and veratryl alcohol
4
-
the enzyme shows the highest activity for 2,6-dimethoxyphenol at pH 4.0
4
-
overall efficiency is maximum for immobilized recombinant DyP on AlSBA-15 at pH 4.0
4.5
-
the enzyme shows the highest activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) or Acid Blue 324 at pH 4.5
5
-
overall efficiency is maximum for immobilized recombinant DyP on FSM-16 at pH 5.0
5
-
the overall efficiency of recombinant DyP immobilized in synthesized silica-based mesocellular foam reaches its maximum of 83% at pH 5.0
7
-
pH optimum for enzyme immobilized in Ca-alginate ferromagnetic beads
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 5
the enzyme retains over 60-70% of the peak activity at pH 3.0 and 5.0 for both Malchite Green and Methyl Violet. The enzyme retains more than 60% of its activity at pH 2.0 and 4.0 for Reactive Black 5
3 - 4
3 - 4.5
-
the oxidation of 2,6-dimethoxyphenol occurs with with approximately 95% and 90% of the maximum activity at pH 3.0 and 4.0, respectively. Above pH 4.0, 2,6-dimethoxyphenol oxidation drops rapidly to 20% at pH 5.0 and to almost zero at pH 6.0. On the other hand, over 40% activity remains at pH 2.0. The oxidation of Reactive Blue 5 occurs with with approximately 50% of the maximum activity at pH 3.0 and 4.5, respectively
3 - 5
more than 50% of activity is conserved between pH 3.0 and 5.0. At lower or higher pH values, less than 25% of activity remains
4 - 5.5
-
the curve for the oxidation of Mn2+ shows appreciable activities down to pH 4.0 and up to pH 5.5 (80-90% in relation to the maximal activity). Mn2+ oxidizing activities are still detectable at less optimal pH above 5.5
5.5 - 8
-
free enzyme shows 25% of initial activity within a pH range between 6.0 and 8.0. The immobilized enzyme displays better activity in a broader pH range than the free peroxidase, which reaches around 58, 72, 82, 88, and 71% at pH 5.5, 6.0, 6.5, 7.5, and 8.0, respectively
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
40
50
70
25
for Reactive Blue 19-decolorizing activity in 25 mM citrate buffer pH 3.5
40
-
temperature optimum for enzyme immobilized in Ca-alginate ferromagnetic beads
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 40
the enzyme is highly active (more than 90% activity) between 4 and 30°C and shows about 60% and 30% activity at 40°C and 50°C, respectively
5 - 80
-
the enzyme is active over a wide temperature range (from 5 to 80°C)
50 - 80
the enzyme retains about 63% of its maximum activity at 50-80°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8
4.1
6.7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly called Thanatephorus cucumeris Dec 1 and Geotrichum candidum Dec 1
UniProt
brenda
formerly called Thanatephorus cucumeris Dec 1 and Geotrichum candidum Dec 1
UniProt
brenda
strain Dec 1, formerly Geotrichum candidum Dec 1
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Thermobifida fusca DyP requires the Tat system for periplasmic export
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DYP2_AMYS7
Amycolatopsis sp. (strain ATCC 39116 / 75iv2)
464
0
50225
Swiss-Prot
-
DYP_EXIGL
501
0
52641
Swiss-Prot
Secretory Pathway (Reliability: 1)
D1A807_THECD
Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9)
403
0
43627
TrEMBL
-
D5LRR6_PSEAI
299
0
32397
TrEMBL
Mitochondrion (Reliability: 2)
M5C6U3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
516
0
58217
TrEMBL
-
EFEB_BACSU
Bacillus subtilis (strain 168)
416
0
45693
Swiss-Prot
Secretory Pathway (Reliability: 4)
Q5NM63_ZYMMO
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
309
0
34923
TrEMBL
Mitochondrion (Reliability: 2)
Q8EIU4_SHEON
Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
311
0
35760
TrEMBL
-
Q9KQ59_VIBCH
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
302
0
33496
TrEMBL
other Location (Reliability: 5)
T1SP91_9PSEU
404
0
44462
TrEMBL
Secretory Pathway (Reliability: 1)
Q9RKQ2_STRCO
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
420
0
44523
TrEMBL
-
Q9ZBW9_STRCO
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
445
0
47025
TrEMBL
-
Q9FBY9_STRCO
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
316
0
34147
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46000
1 * 46000, molecular mass of the unprocessed precursor calculated from amino acid sequence
47000
47460
-
recombinant enzyme expressed in Escherichia coli, deduced from amino acid sequence
48000
50000
-
recombinant enzyme expressed in Escherichia coli, gel filtration
55000
58000
60000
58000
-
recombinant enzyme expressed in Aspergillus oryzae, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotetramer
monomer
trimer
?
x * 54900, SDS-PAGE, recombinant enzyme, calculated from amino acid sequence
?
-
x * 49400, His6-tagged enzyme, calculated from amino acid sequence
?
-
x * 49400, His6-tagged enzyme, calculated from amino acid sequence
-
monomer
-
1 * 40000, manganese-independent peroxidase II, SDS-PAGE
monomer
-
1 * 48000, the protein exists as a monomer in solution, gel filtration and dynamic light scattering
monomer
1 * 46000, molecular mass of the unprocessed precursor calculated from amino acid sequence
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
DyP is glycosylated with N-acetylglucosamine and mannose (17% (w/w))
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 32.5% (w/v) PEG 4000 as precipitant
to 2.1 A resolution. At the distal side of the heme molecule, flexible aspartate residue Asp168 plays a key role in catalysis. It guides incoming hydrogen peroxide toward the heme iron and mediates proton rearrangement in the process of Compound I formation. Afterward, its side chain changes its conformation, now pointing toward the protein backbone. A transient radical on the surface-exposed residue Tyr337 is the oxidation site for bulky substrates
HEPES-bound enzyme, sitting drop vapor diffusion method, using 25% (v/v) 2-methyl-2,4-pentanediol, 50 mM HEPES, pH 7.0
resonance Raman and electrochemical study. In solution, enzyme shows a heterogeneous spin population, with the six-coordinated low-spin state being the most populated. The poor catalytic activity of BsDyP is ascribed to the presence of a catalytically incompetent six-coordinated low-spin population. The spin population is sensitively dependent on the pH, temperature, and physical, i.e., solution versus crystal versus immobilized, state of the enzymes. The redox potential for the Fe2+/Fe3+ couple is -40 mV at pH 7.6, which is substantially more positive than those reported for the majority of other peroxidases
-
sitting drop vapor diffusion method, using 1.6-1.95 M ammonium sulfate and 0.1 M MES or 0.1 M citrate buffer pH 6.5
-
structures of native enzyme, the D171N mutant, the native enzyme complexed with cyanide, and the D171N mutant associated with cyanide, to 1.4 A, 1.42 A, 1.45 and 1.4 A resolution, respectively. Structures contain four amino acids forming the binding pocket for hydrogen peroxide, and they are remarkably conserved in this family. The structures show that OD2 of Asp171 accepts a proton from hydrogen peroxide in compound I formation, and that OD2 can swing to the appropriate position in response to the ligand for heme iron
sitting drop vapor diffusion method, using 20% (w/v) PEG300, 0.1 M Tris buffer pH 8.5, 5% PEG8000 and 10% (v/v) glycerol
-
enzyme in the absence of substrate as well as in the presence of potassium cyanide and veratryl alcohol, hanging drop vapor diffusion method, using 2.4 M sodium malonate pH 7.0
in complex with heme, hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 20% (w/v) PEG3350 and 0.1 M Bis-Tris pH 5.5
-
sitting drop vapor diffusion method, using 0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate and 34% (w/v) PEG 4000
TyrA in complex with iron protoporphyrin (IX), hanging drop vapor diffusion method, using 0.1 M Tris pH 8.0, 5% (v/v) 2-propanol, 20% (w/v) polyethylene glycol 4000, and 1 mM hemin
batch method, using 0.89 M ammonium sulfate, 0.92 M sodium chloride, at 10°C
deglycosylated DyP is crystallized by the batch method, using 0.92 M NaCl and 0.89 M ammonium sulfate as precipitant
-
deglycosylated DyP is crystallized by the sitting drop vapor diffusion method, using 25.3% (w/v) PEG 8000 at 5.5 K (pH 6.2)
-
sitting drop vapor diffusion method, using 0.2 M potassium thiocyanate and 20% (w/v) PEG 3000
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
M401F
-
heme cavity mutant with significantly increased H2O2 stability of 8.2fold, the mutant retains 16% activity at 100 mM H2O2
M401I
-
heme cavity mutant with significantly increased H2O2 stability of 3.7fold
M401L
-
heme cavity mutant with significantly increased H2O2 stability of 2.4fold
M451I
-
heme cavity mutant with significantly increased H2O2 stability of 5.2fold, the mutant retains 5% activity at 100 mM H2O2
G169L
the mutant shows strongly increased activity compared to the wild type enzyme
Y147F/Y337F
the mutant shows reduced activity compared to the wild type enzyme
Y147S
the mutant shows reduced activity compared to the wild type enzyme
D222A
-
the mutant shows reduced catalytic efficiency with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), Reactive Black 5 and H2O, as compared to the wild type enzyme
D222E
-
the mutant shows increased catalytic efficiency with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and reduced activity with Reactive Black 5 and H2O, as compared to the wild type enzyme
D222E/R390K
-
the mutant shows increased catalytic efficiency with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and reduced activity with Reactive Black 5 and H2O, as compared to the wild type enzyme
R390A
-
the mutant shows reduced catalytic efficiency with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), Reactive Black 5 and H2O, as compared to the wild type enzyme
R390K
-
the mutant shows increased catalytic efficiency with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and H2O and reduced activity with Reactive Black 5, as compared to the wild type enzyme
E201D
-
the mutant shows a significantly higher activity on several dyes when compared with the wild type enzyme and the activity of the mutant enzyme is almost 10fold greater than the wild type at pH 4.0
D143A
-
the mutant shows no activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and guaiacol, but about 20% of wild type activity with Reactive Blue 19 and 10% activity with catechol
D143N
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
H215A
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
L246W
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
R232E
-
the mutant shows no activity towards Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), but about 40% of wild type activity with guaiacol and 35% activity with catechol
R232L
-
the mutant shows no activity towards Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), but about 90% of wild type activity with guaiacol and 50% activity with catechol
S234Y
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
D143A
-
the mutant shows no activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and guaiacol, but about 20% of wild type activity with Reactive Blue 19 and 10% activity with catechol
-
D143N
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
H215A
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
R232E
-
the mutant shows no activity towards Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), but about 40% of wild type activity with guaiacol and 35% activity with catechol
-
R232L
-
the mutant shows no activity towards Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), but about 90% of wild type activity with guaiacol and 50% activity with catechol
-
W109F
the mutant shows decreased oxidative activity and decolorizing ability compared to the wild type enzyme
W147F
the mutant shows decreased oxidative activity and increased decolorizing ability compared to the wild type enzyme
W212F
the mutant shows decreased oxidative activity and increased decolorizing ability compared to the wild type enzyme
W264F
the mutant shows decreased oxidative activity and increased decolorizing ability compared to the wild type enzyme
W264H
the mutant shows decreased oxidative activity and decolorizing ability compared to the wild type enzyme
W264Y
the mutant shows decreased oxidative activity and decolorizing ability compared to the wild type enzyme
W380F
the mutant shows severely decreased oxidative activity and decolorizing ability compared to the wild type enzyme
W380G
the mutant shows decreased oxidative activity and decolorizing ability compared to the wild type enzyme
W380Y
the mutation does not weaken the first step of the catalytic cycles (oxidation of the resting state Fe3+ by H2O2) significantly, but it weakens the oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and other reducing substrates which has a larger size than H2O2
E188K
-
the mutant shows 3-4fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
E188K/A142V
-
the mutant shows 2fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
E188K/A142V/H125Y
-
the mutant shows a 100fold enhanced catalytic efficiency (kcat/Km) for 2,6-dimethoxyphenol and 2fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
E188K/H125R
-
the mutant shows 6fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
H125R
-
the mutant shows 3-4fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
E188K
-
the mutant shows 3-4fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
E188K/A142V
-
the mutant shows 2fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
E188K/A142V/H125Y
-
the mutant shows a 100fold enhanced catalytic efficiency (kcat/Km) for 2,6-dimethoxyphenol and 2fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
E188K/H125R
-
the mutant shows 6fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
H125R
-
the mutant shows 3-4fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
Y288F
-
kcat is least affected by the mutation whereas Km shows significant increase compared to the wild type enzyme
Y374F
-
the mutation results in an overall 5.5fold decrease in catalytic efficiency as compared to the wild type enzyme
Y437F
-
kcat is least affected by the mutation whereas Km shows significant increase compared to the wild type enzyme
D171N
the mutant displays 3000fold less enzymatic activity compared to the wild type DyP
H164A
-
the specific activity of the purified mutant is 99.8% lower than that of recombinant DyP expressed in Escherichia coli
H166A
-
the specific activity of the purified mutant is 95% lower than that of recombinant DyP expressed in Escherichia coli
D242A
the mutant shows 0.7% of the Reactive Blue 19-decolorizing activity of the wild type protein
H338A
the mutant lacks the heme cofactor and shows 3% of the Reactive Blue 19-decolorizing activity of the wild type protein
D220A
the catalytic efficiency of the mutant toward H2O2 drops by 22fold compared to the wild type enzyme
D220F
the mutant shows reduced activity compared to the wild type enzyme
D220G
the mutant shows reduced activity compared to the wild type enzyme
D220H
the mutant shows reduced activity compared to the wild type enzyme
D220K
the mutant shows reduced activity compared to the wild type enzyme
D220N
the mutant shows reduced activity compared to the wild type enzyme
H312C
the catalytic efficiency of the mutant toward H2O2 drops by 88fold compared to the wild type enzyme
D220A
-
the catalytic efficiency of the mutant toward H2O2 drops by 22fold compared to the wild type enzyme
-
D220F
-
the mutant shows reduced activity compared to the wild type enzyme
-
D220G
-
the mutant shows reduced activity compared to the wild type enzyme
-
H312C
-
the catalytic efficiency of the mutant toward H2O2 drops by 88fold compared to the wild type enzyme
-
D138V
-
the mutant displays significantly increased activity at pH 6.5 as compared to the wild type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 4
-
the enzyme maintains 50% of its original activity at pH 2.0 and 4.0 after incubation for 9 and 5 h at 50°C, respectively
2 - 5.5
the enzyme activity is more than 90% between pH 2.0 and 5.5 after 1 h of incubation
2.5
2.5 - 5
-
isozymes DyP1, DyP2 and DyP3 are completely inactivated at pH 2.5. Isozymes DyP1, DyP2 and DyP3 exhibit approximately 20% activity at pH 3.0. Isozymes DyP1 and Dyp2 show almost 100% activity at pH 3.5, isozyme DyP3 shows about 95% activity at pH 3.5. Isozyme DyP1 shows less than 50% activity at pH 4.0, isozymes DyP2 and Dyp3 show about 50% activity at pH 4.0. Isozymes Dyp1, DyP2 and Dyp3 show about 30% activity at pH 4.5 and about 20% activity at pH 5.0
3 - 5
-
the enzyme maintains 50% of its original activity at pH 3.0 and 5.0 after incubation for 10 and 6 h at 40°C, respectively
3 - 6
3.5 - 9.5
Q8YWM0
when maintained at 40°C for 20 min, the enzyme is stable at pH values between 3.5 and 9.5. The enzyme shows 20% relative activity at pH 3.0 and 10.0, 40% relative activity at pH 4.0, about 65% relative activity at pH 4.5 and 9.0, about 80% relative activity at pH 5.0, more than 90% relative activity at pH 6.0-8.0
4 - 6
-
the immobilized enzyme has an optimum stability at pH ranging from 5.5 to 6.0 compared with pH ranging from 4.0 to 5.0 for the free peroxidase. In these pH ranges, both enzymes show 50% activity after 72 h incubation
4 - 9
the enzyme shows more than 80% activity after 24 h at pH 4.0-9.0
5 - 10
the enzyme shows more than 80% activity after incubation at pH 5.0-10.0 for 1 h at 37°C
5 - 9
-
more than 50% activity after 24 h between pH 5.0-9.0, total loss of activity after the enzyme is incubated at pH 3.0-4.0, and more than 90% loss of activity at pH 4.5
7 - 10
-
the enzyme maintains 100% of its original activity at pH values between 7 and 10 after incubation for 48 h at 40°C
2.5
-
the enzyme does not lose any activity during 4 h of incubation at pH 2.5
2.5
-
at pH 2.5, manganese-independent peroxidase I is quite stable and does not lose any activity within 4 h, while manganese-independent peroxidase II loses about 40% of its activity within the same time
3 - 6
-
the enzyme is very stable between pH 3.0-6.0 at 4°C, keeping 90% activity after 168 incubation. At 25°C, the enzyme retains 90% activity between pH 5.0 and 6.0 and 60% and 20% at pH 3.0 and 4.0, respectively, after 70 h incubation
3 - 6
-
more than 90% of initial free recombinant DyP activity remains active after incubation in citrate buffered solution at pH 3.0-5.0 for 48 h. Adsorption yields of recombinant DyP immobilized on FSM-16 and AlSBA-15 increases as pH decreased from 6.0 to 3.0, however, the activity yield of immobilized recombinant DyP decreases with decreasing pH
3 - 6
-
the adsorption yields of recombinant DyP immobilized in synthesized silica-based mesocellular foam increases as the pH decreased from 6.0 to 3.0, however, the activity yields of the immobilized recombinant DyP decreases with decreasing pH
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 70
after 5 min incubation, respectively, the enzyme shows 100% activity between 15 and 25°C, about 85% activity at 30-35°C, about 75% activity at 40-45°C, about 62% activity at 50°C, and less than 30% activity at 55°C and above
20 - 60
30 - 40
30 - 60
30 - 65
30 - 70
30 - 80
-
the enzyme remains stable at temperatures of up to 80°C for 60 min
40
40 - 60
-
the half-life times of the enzyme in the absence of 5 mM of Mg2+ are 6, 4, and 2 h at 40, 50, and 60°C, respectively
50
60
60 - 80
-
the half-life times of the enzyme in the absence of 5 mM of Mn2+ are 8, 5, and 2 h at 60, 70, and 80°C, respectively. The half-life time of the purified peroxidase at 60, 70, and 80°C increases to 10, 7, and 4 h in the presence 5 mM of MnSO4, respectively
70
20 - 60
the enzyme is relatively stable at temperatures from 20 to 60°C with a residual activity of more than 80%. At higher temperatures, a high loss of activity is observed due to protein denaturation, resulting in residual activities of less than 5%
20 - 60
-
the activity of isozyme DyP3 is less than that of isozymes DyP2 and DyP1 at 35°C and 40°C. Isozymes DyP1, DyP2 and DyP3 exhibit approximately 75% activity at 20°C and about 90% activity at 30°C. Isozyme DyP1 shows about 75% activity at 40°C, isozyme DyP2 shows about 85% activity at 40°C, and isozyme DyP3 shows about 50% activity at 40°C. Isozymes DyP1, DyP2 and DyP3 show about 10% activity at 50°C and are completely inactivated at 60°C
30 - 40
-
the enzyme is stable at a temperature of 30°C for 1 h, but a sharp decrease is detected after the incubation at 40°C. The enzyme shows almost no activity at 60°C
30 - 40
-
the enzyme is stable at a temperature of 30°C for 1 h, but a sharp decrease is detected after the incubation at 40°C. The enzyme shows almost no activity at 60°C
30 - 60
Q8YWM0
the enzyme is considerably stable at 30°C and 40°C where it retains more than 90% of its activity, while the enzyme loses more than 90% of its activity after incubation at 50°C and 60°C for 3 h
30 - 60
-
DyP activity is restored at 30°C after treatment at 40 and 50°C for 11 h, DyP activity is stable after incubation at 50°C for 11 h. When DyP is incubated at 30 and 40°C for 14 days, the inactivation rates are 37 and 59%, respectively. When DyP is heated at 60°C for 3 h, 35% of the initial activity is lost
30 - 60
-
the enzyme retains almost of its initial activity against ABTS and DMP after incubation at 30°C and 40°C for 120 min. The peroxidase activity significantly decreases after incubating at 50°C for 60 min, and is almost completely lost following incubation at 60°C for 30 min
30 - 60
-
the enzyme retains almost all of its initial activity against 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 2,6-dimethoxyphenol after incubation at 30°C or 40°C for 2 h. The peroxidase activity of the enzyme against ABTS significantly decreases after incubating at 50°C for 1 h and is almost completely lost following incubation at 60°C for 30 min. On the other hand, the activity of the enzyme against 2,6-dimethoxyphenol is maintained at 50°C
30 - 60
after incubation for 2 h at 60°C the enzyme loses 50% of its original activity, while at 30°C and 40°C DyP retains its activity after this period. Upon incubation at 60°C, an almost 2fold increase in activity is observed within 10 min
30 - 65
the wild type enzyme remains stable after 24 h at 30-55°C and shows 50% activity after 24 h at 65.5°C
30 - 65
-
the T50 index is adjusted to 48.3°C, after 10 min incubation between 30 and 65°C
30 - 70
-
after 2 h heat treatment, the native enzyme shows 97% residual activity at 40°C, 93% residual activity at 50°C, and 79% residual activity at 60°C when measured at 30°C for 1 min. After heating at 30, 40, and 50°C for 120 min, recombinant DyP retains more than 90% of its activity when measured at 30°C for 1 min, but the enzyme gradually becomes inactive after treatment at 60°C (12% residual activity) and is rapidly inactivated at 70°C
30 - 70
-
recombinant DyP expressed in Escherichia coli does not lose its activity at 30°C and 40°C. The activity is loweres slightly to 83% of full activity after heating 1 h at 50°C. In contrast, the activity drastically declines at 60°C and 70°C. The residual activity is 4% and 10% of full activity after heating 2 h at 60°C and 15 min at 70°C, respectively. The activity of native DyP after 1 h heating at 60°C is 92% of full activity whereas that of recombinant DyPs expressed in Escherichia coli and Aspergillus oryzae are only 42%, and 44%, respectively
50
-
the enzyme shows a residual activity of ca. 80% after incubation at 50°C for 1 h. The enzyme shows almost no activity at 60°C
50
-
the enzyme shows a residual activity of ca. 80% after incubation at 50°C for 1 h. The enzyme shows almost no activity at 60°C
60
-
the half-life times of the enzyme in the absence of 5 mM of Mg2+ are 6, 4, and 2 h at 40, 50, and 60 °C, respectively. The half-life time of the enzyme at 40, 50, and 60°C increases to 7, 5, and 3 h in the presence 5 mM of Mg2+, respectively
60
the enzyme retains about 70% maximal activity after incubation at 60°C for 1 h
70
the enzyme shows more than 60% activity after incubation at 70°C for 2 h at pH 7.0
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after five cycles, the Ca-alginate-immobilized enzyme system retains more than 58% of its initial activity
-
recombinant DyP is partially inactivated during successive batches even by continuous fed-batch supply of H2O2, initial recombinant DyP activity is inactivated by 15% over the first 10 min during dye decolorization and remains stable thereafter at 85% of the initial activity from 10 to 40 min
-
the activity of recombinant DyP immobilized in synthesized silica-based mesocellular foam drops by 6% and 12% at pH 3.0 andpH 4.0, respectively, while the activity decreases by 35% and 70% at pH 5.0 and pH 6.0 after daily leaching treatment
-
the enzyme shows high compatibility with EcoVax and Dipex as laundry detergents for 48 h at 40°C. The enzyme is highly stable against perfume and anti-redeposition agents, particularly 50 mM Na2CO3, and of cationic and other detergent compound, retaining 95, 104, 107, and 125% of its initial activity after treatment with 1% perfume, 50 mM hexadecyltrimethylammonium bromide, 1% (w/v) sodium tripolyphosphate, and 50 mM Na2CO3, respectively.
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexane
isopropanol
hexane
-
the enzyme retains at least 75% of the activity of incubation in the presence of 30% (v/v) hexane
hexane
-
the enzyme retains at least 22% of the activity of incubation in the presence of 30% (v/v) hexane
hexane
-
the enzyme retains at least 75% of the activity of incubation in the presence of 30% (v/v) hexane
-
hexane
-
the enzyme retains at least 22% of the activity of incubation in the presence of 30% (v/v) hexane
-
isopropanol
-
the enzyme retains at least 95% of the activity of incubation in the presence of 30% (v/v) isopropanol
isopropanol
-
the enzyme retains at least 115% of the activity of incubation in the presence of 30% (v/v) isopropanol
isopropanol
-
the enzyme retains at least 95% of the activity of incubation in the presence of 30% (v/v) isopropanol
-
isopropanol
-
the enzyme retains at least 115% of the activity of incubation in the presence of 30% (v/v) isopropanol
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilized recombinant DyP has higher stability to H2O2 compared to free recombinant DyP. The stability of recombinant DyP immobilized on FSM-16 at pH 4.0 and on AlSBA-15 at pH 3.0 and 4 are similar to that of free recombinant DyP
-
712777
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20°C, manganese-independent peroxidase I in 50 mM sodium tartrate buffer pH 2.5, 24 h, 20% loss of activity
-
20°C, manganese-independent peroxidase II in 50 mM sodium tartrate buffer pH 2.5, 24 h, 75% loss of activity
-
4°C, 50 mM potassium phosphate buffer (pH 7.0), 40 days, 10% loss of activity
Q8YWM0
deglycosylated DyP exhibits enzymatic activity and is stable for more than 26 d either in MES buffer at pH 6.0 or in 45% (v/v) methanol
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and butyl-Toyopearl column chromatography
-
ammonium sulfate precipitation, QAE-Toyopearl column chromatography, Mono Q column chromatography, Poros PE column chromatography, and Superdex 75 gel filtration
-
ammonium sulfate precipitation-dialysis, Mono-S Sepharose anion-exchange column chromatography, and Sephacryl S-200 gel filtration
-
ammonium sulfate precipitation-dialysis, Sepharose column chromatography, and Sephacryl S-200 gel filtration
-
butyl-Toyopearl column chromatography, Mono Q column chromatography, and Superdex 200 gel filtration
-
Ni-NTA agarose column chromatography and Superdex 75pg gel filtration
-
Ni-NTA agarose column chromatography and Superdex G-75 gel filtration
Ni-NTA bead chromatography
Ni-NTA column chromatography and Superdex 75 gel filtration
Ni-Sepharose column chromatography, and Superdex 200 gel filtration
-
phenyl-Sepharose column chromatography and SP Sepharose 200 column chromatography
Q Sepharose column chromatography, Mono Q column chromatography, and Mono P column chromatography
Q Sepharose column chromatography, Mono Q column chromatography, Mono S column chromatography, and Mono P column chromatography
-
Q-Sepharose column chromatography, Superdex 75 gel filtration, and MonoQ column chromatography
-
quaternary aminoethyl-Toyopearl column chromatography and Mono-Q column chromatography
-
SP-Sepharose column chromatography Mono S column chromatography, and Superdex 75 gel filtration
-
Super Q 650M column chromatography and butyl Toyopearl column chromatography
-
Toyopearl DEAE-650M column chromatography, Toyopearl butyl-650M column chromatography, and hydroxylapatite column chromatography
Q8YWM0
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Aspergillus oryzae strain M-2-3, no exogenous heme is necessary for the expression of DyP
-
expressed in Aspergillus oryzae strain RD005
-
expressed in Escherichia coli
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells and in Aspergillus oryzae strain RD005
-
expressed in Escherichia coli BL21(DE3) Star cells
expressed in Escherichia coli BL21(DE3)Star cells
expressed in Pichia pastoris strain X33 and in Escherichia coli Rosetta (DE3) cells
-
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
complete inhibition of DyP activity by molasses molasses (containing approximately 33% sucrose (w/w), 6.5% glucose (w/w), 7.5% fructose (w/w) and 0.57 g/kg nitrogen) is observed at the concentration of 20 g /l
-
dye decolorizing peroxidase activity is 233fold higher in air-membrane surface bioreactor culture than in submerged culture
-
high-level recombinant DyP activity in limitation of carbon and nitrogen sources is maintained stably for 26 cycles of repeated 1-day batches of Aspergillus oryzae pellets without any additional pH control
-
molasses (containing approximately 33% sucrose (w/w), 6.5% glucose (w/w), 7.5% fructose (w/w) and 0.57 g/kg nitrogen) at concentrations greater than 10 g/l increase the decolorization activity of the culture broth toward Reactive Blue 5 mainly because the amount of enzyme produced is enhanced. When the culture broth is diluted 25times, the dye-decolorizing activity is 7times as much as that of non-diluted culture broth
-
similar average recombinant DyP productivities are observed in repeated-batch cultures using wheat bran powder and rice bran powder. Average recombinant DyP productivities in fed-batch cultures are slightly lower than those in repeated-batch cultures. The recombinant DyP production is affected by the addition of K2HPO4 in the repeated-batch and fed-batch cultures using wheat bran powder. Increase in phosphate does not enhance recombinant DyP production, rather rDyP activity decreases by the repeated-batch culture
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
using 1.6 mM GSSG, 0.16 M urea, 0.01 mM hemin, Britton-Robinson buffer pH 6.5, at 4°C
-
with oxidized glutathione (1.5 mM), hemin (0.03 mM) and urea (0.8 M)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
paper production
additional information
degradation
DyP is a promising enzyme for the decolorizing treatment of dye-contaminated water
paper production
the enzyme has an accelerated action during the biobleaching of eucalyptus kraft pulp
paper production
-
the enzyme has an accelerated action during the biobleaching of eucalyptus kraft pulp
-
additional information
-
the increased stability of Anabaena sp. DyP variants coupled with the broad substrate specificity can be potentially useful for the further practical application of these enzymes especially in bioremediation of wastewater contaminated with recalcitrant anthraquinone dyes
additional information
-
DyP-type peroxidases are interesting for applications in the waste treatment sector
additional information
-
DyP-type peroxidases are interesting for applications in the waste treatment sector
additional information
-
DyP-type peroxidases are interesting for applications in the waste treatment sector
additional information
-
DyP-type peroxidases are interesting for applications in the waste treatment sector
additional information
-
DyP-type peroxidases are interesting for applications in the waste treatment sector
additional information
-
DyP-type peroxidases are interesting for applications in the waste treatment sector
additional information
-
DyP-type peroxidases are interesting for applications in the waste treatment sector
additional information
-
DyP-type peroxidases are interesting for applications in the waste treatment sector
additional information
-
DyP-type peroxidases are interesting for applications in the waste treatment sector
additional information
-
DyP-type peroxidases are interesting for applications in the waste treatment sector
additional information
Q8YWM0
AnaPX is a useful alternative of horseradish peroxidase or fungal DyPs
additional information
-
nonpurified crude recombinant DyP can be a useful candidate for development as a practical biocatalyst in colored wastewater treatment
additional information
the enzyme can be used as biocatalyst for flavor production
additional information
-
the enzyme can be used as biocatalyst for flavor production
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ogola, H.J.; Kamiike, T.; Hashimoto, N.; Ashida, H.; Ishikawa, T.; Shibata, H.; Sawa, Y.
Molecular characterization of a novel DyP-type peroxidase from the cyanobacterium Anabaena sp. PCC 7120
Appl. Environ. Microbiol.
75
7509-7518
2009
Anabaena sp. (Q8YWM0)
brenda
Sato, T.; Hara, S.; Matsui, T.; Sazaki, G.; Saijo, S.; Ganbe, T.; Tanaka, N.; Sugano, Y.; Shoda, M.
A unique dye-decolorizing peroxidase, DyP, from Thanatephorus cucumeris Dec 1: heterologous expression, crystallization and preliminary x-ray analysis
Acta Crystallogr. Sect. D
D60
149-152
2004
Thanatephorus cucumeris
brenda
Saijo, S.; Sato, T.; Tanaka, N.; Ichiyanagi, A.; Sugano, Y.; Shoda, M.
Precipitation diagram and optimization of crystallization conditions at low ionic strength for deglycosylated dye-decolorizing peroxidase from a basidiomycete
Acta Crystallogr. Sect. F
61
729-732
2005
Thanatephorus cucumeris
brenda
Kim, S.J.; Shoda, M.
Purification and characterization of a novel peroxidase from Geotrichum candidum dec 1 involved in decolorization of dyes
Appl. Environ. Microbiol.
65
1029-1035
1999
Geotrichum candidum
brenda
Sugano, Y.; Nakano, R.; Sasaki, K.; Shoda, M.
Efficient heterologous expression in Aspergillus oryzae of a unique dye-decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1
Appl. Environ. Microbiol.
66
1754-1758
2000
Geotrichum candidum
brenda
Sugano, Y.; Matsushima, Y.; Shoda, M.
Complete decolorization of the anthraquinone dye Reactive blue 5 by the concerted action of two peroxidases from Thanatephorus cucumeris Dec 1
Appl. Microbiol. Biotechnol.
73
862-871
2006
Thanatephorus cucumeris
brenda
Shakeri, M.; Shoda, M.
Change in turnover capacity of crude recombinant dye-decolorizing peroxidase (rDyP) in batch and fed-batch decolorization of Remazol Brilliant Blue R
Appl. Microbiol. Biotechnol.
76
919-926
2007
Thanatephorus cucumeris
brenda
Liers, C.; Bobeth, C.; Pecyna, M.; Ullrich, R.; Hofrichter, M.
DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes
Appl. Microbiol. Biotechnol.
85
1869-1879
2010
Auricularia auricula-judae
brenda
van Bloois, E.; Torres Pazmino, D.E.; Winter, R.T.; Fraaije, M.W.
A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily
Appl. Microbiol. Biotechnol.
86
1419-1430
2010
Thermobifida fusca YX (Q47KB1)
brenda
Ogola, H.J.; Hashimoto, N.; Miyabe, S.; Ashida, H.; Ishikawa, T.; Shibata, H.; Sawa, Y.
Enhancement of hydrogen peroxide stability of a novel Anabaena sp. DyP-type peroxidase by site-directed mutagenesis of methionine residues
Appl. Microbiol. Biotechnol.
87
1727-1736
2010
Anabaena sp.
brenda
Hofrichter, M.; Ullrich, R.; Pecyna, M.J.; Liers, C.; Lundell, T.
New and classic families of secreted fungal heme peroxidases
Appl. Microbiol. Biotechnol.
87
871-897
2010
Anabaena sp., Auricularia auricula-judae, Bacillus subtilis, Bacteroides thetaiotaomicron, Escherichia coli, Macrolepiota albuminosa, Mycetinis scorodonius, Shewanella oneidensis, Thanatephorus cucumeris, Thermobifida fusca
brenda
Sugano, Y.; Ishii, Y.; Shoda, M.
Role of H164 in a unique dye-decolorizing heme peroxidase DyP
Biochem. Biophys. Res. Commun.
322
126-132
2004
Thanatephorus cucumeris
brenda
Sugano, Y.; Matsushima, Y.; Tsuchiya, K.; Aoki, H.; Hirai, M.; Shoda, M.
Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec 1
Biodegradation
20
433-440
2009
Thanatephorus cucumeris
brenda
Sugano, Y.
DyP-type peroxidases comprise a novel heme peroxidase family
Cell. Mol. Life Sci.
66
1387-1403
2009
Bacteroides thetaiotaomicron, Escherichia coli, Mycetinis scorodonius, Pleurotus ostreatus (Q0VTU1), Shewanella oneidensis, Thanatephorus cucumeris (M5C6U3), Thanatephorus cucumeris, Thermus thermophilus HB8
brenda
Sugano, Y.; Muramatsu, R.; Ichiyanagi, A.; Sato, T.; Shoda, M.
DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: Asp171 replaces the distal histidine of classical peroxidases
J. Biol. Chem.
282
36652-36658
2007
Thanatephorus cucumeris (M5C6U3), Thanatephorus cucumeris
brenda
Shakeri, M.; Sugano, Y.; Shoda, M.
Production of dye-decolorizing peroxidase (rDyP) from complex substrates by repeated-batch and fed-batch cultures of recombinant Aspergillus oryzae
J. Biosci. Bioeng.
103
129-134
2007
Thanatephorus cucumeris
brenda
Shakeri, M.; Sugano, Y.; Shoda, M.
Stable repeated-batch production of recombinant dye-decolorizing peroxidase (rDyP) from Aspergillus oryzae
J. Biosci. Bioeng.
105
683-686
2008
Thanatephorus cucumeris
brenda
Shimokawa, T.; Hirai, M.; Shoda, M.; Sugano, Y.
Efficient dye decolorization and production of dye decolorizing enzymes by the basidiomycete Thanatephorus cucumeris Dec 1 in a liquid and solid hybrid culture
J. Biosci. Bioeng.
106
481-487
2008
Thanatephorus cucumeris
brenda
Shimokawa, T.; Shoda, M.; Sugano, Y.
Purification and characterization of two DyP isozymes from Thanatephorus cucumeris Dec 1 specifically expressed in an air-membrane surface bioreactor
J. Biosci. Bioeng.
107
113-115
2009
Thanatephorus cucumeris
brenda
Lee, T.H.; Aoki, H.; Sugano, Y.; Shoda, M.
Effect of molasses on the production and activity of dye-decolorizing peroxidase from Geotrichum candidum Dec1
J. Biosci. Bioeng.
89
545-549
2000
Thanatephorus cucumeris
brenda
Shakeri, M.; Shoda, M.
Decolorization of an anthraquinone dye by the recombinant dye-decolorizing peroxidase (rDyP) immobilized on mesoporous materials
J. Mol. Catal. B
54
42-49
2008
Thanatephorus cucumeris
-
brenda
Shakeri, M.; Shoda, M.
Efficient decolorization of an anthraquinone dye by recombinant dye-decolorizing peroxidase (rDyP) immobilized in silica-based mesocellular foam
J. Mol. Catal. B
62
277-281
2010
Thanatephorus cucumeris
-
brenda
Zubieta, C.; Joseph, R.; Krishna, S.S.; McMullan, D.; Kapoor, M.; Axelrod, H.L.; Miller, M.D.; Abdubek, P.; Acosta, C.; Astakhova, T.; et al
Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA
Proteins Struct. Funct. Bioinform.
69
234-243
2007
Shewanella oneidensis MR-1 (Q8EIU4)
brenda
Faraco, V.; Piscitelli, A.; Sannia, G.; Giardina, P.
Identification of a new member of the dye-decolorizing peroxidase family from Pleurotus ostreatus
World J. Microbiol. Biotechnol.
23
889-893
2007
Pleurotus ostreatus (Q0VTU1)
-
brenda
Li, J.; Liu, C.; Li, B.; Yuan, H.; Yang, J.; Zheng, B.
Identification and molecular characterization of a novel DyP-type peroxidase from Pseudomonas aeruginosa PKE117
Appl. Biochem. Biotechnol.
166
774-785
2012
Pseudomonas aeruginosa (D5LRR6), Pseudomonas aeruginosa PKE117 (D5LRR6), Pseudomonas aeruginosa PKE117
brenda
Salvachua, D.; Prieto, A.; Martinez, A.T.; Martinez, M.J.
Characterization of a novel dye-decolorizing peroxidase (DyP)-type enzyme from Irpex lacteus and its application in enzymatic hydrolysis of wheat straw
Appl. Environ. Microbiol.
79
4316-4324
2013
Irpex lacteus
brenda
Santos, A.; Mendes, S.; Brissos, V.; Martins, L.
New dye-decolorizing peroxidases from Bacillus subtilis and Pseudomonas putida MET94: towards biotechnological applications
Appl. Microbiol. Biotechnol.
98
2053-2065
2014
Bacillus subtilis, Bacillus subtilis 168, Pseudomonas putida, Pseudomonas putida MET94
brenda
Sezer, M.; Santos, A.; Kielb, P.; Pinto, T.; Martins, L.O.; Todorovic, S.
Distinct structural and redox properties of the heme active site in bacterial dye decolorizing peroxidase-type peroxidases from two subfamilies: resonance Raman and electrochemical study
Biochemistry
52
3074-3084
2013
Bacillus subtilis
brenda
Wang, L.; Chang, A.; Yuan, W.; Bai, F.
Recombinant expression, purification and characterization of a novel DyP-type peroxidase in Escherichia coli
Chin. J. Biotechnol.
29
772-784
2013
Zymomonas mobilis (Q5NM63), Zymomonas mobilis, Zymomonas mobilis ATCC 31821 (Q5NM63)
brenda
Yoshida, T.; Tsuge, H.; Konno, H.; Hisabori, T.; Sugano, Y.
The catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue
FEBS J.
278
2387-2394
2011
Bjerkandera adusta (Q8WZK8)
brenda
Strittmatter, E.; Liers, C.; Ullrich, R.; Wachter, S.; Hofrichter, M.; Plattner, D.A.; Piontek, K.
First crystal structure of a fungal high-redox potential dye-decolorizing peroxidase: substrate interaction sites and long-range electron transfer
J. Biol. Chem.
288
4095-4102
2013
Auricularia auricula-judae (I2DBY1), Auricularia auricula-judae
brenda
Brissos, V.; Tavares, D.; Sousa, A.; Robalo, M.; Martins, L.
Engineering a bacterial DyP-type peroxidase for enhanced oxidation of lignin-related phenolics at alkaline pH
ACS Catal.
7
3454-3465
2017
Pseudomonas putida, Pseudomonas putida MET94
-
brenda
Lauber, C.; Schwarz, T.; Nguyen, Q.K.; Lorenz, P.; Lochnit, G.; Zorn, H.
Identification, heterologous expression and characterization of a dye-decolorizing peroxidase of Pleurotus sapidus
AMB Express
7
164
2017
Pleurotus sapidus (A0A0F7VJ89), Pleurotus sapidus, Pleurotus sapidus DSM 8266 (A0A0F7VJ89)
brenda
Behrens, C.J.; Zelena, K.; Berger, R.G.
Comparative cold shock expression and characterization of fungal dye-decolorizing peroxidases
Appl. Biochem. Biotechnol.
179
1404-1417
2016
Pleurotus ostreatus, Bjerkandera adusta, Mycetinis scorodonius, Auricularia auricula-judae, Pleurotus ostreatus 1020, Auricularia auricula-judae 11326
brenda
Zhang, C.; Xin, Y.; Wang, Y.; Guo, T.; Lu, S.; Kong, J.
Identification of a novel dye-decolorizing peroxidase, EfeB, translocated by a twin-arginine translocation system in Streptococcus thermophilus CGMCC 7.179
Appl. Environ. Microbiol.
81
6108-6119
2015
Streptococcus thermophilus, Streptococcus thermophilus CGMCC 7.179
brenda
Yoshida, T.; Sugano, Y.
A structural and functional perspective of DyP-type peroxidase family
Arch. Biochem. Biophys.
574
49-55
2015
Bjerkandera adusta (Q8WZK8), Bjerkandera adusta Dec 1 (Q8WZK8), Bjerkandera adusta Dec 1
brenda
Singh, R.; Eltis, L.D.
The multihued palette of dye-decolorizing peroxidases
Arch. Biochem. Biophys.
574
56-65
2015
Amycolatopsis sp. (K7N5M8)
brenda
Liu, X.; Yuan, Z.; Wang, J.; Cui, Y.; Liu, S.; Ma, Y.; Gu, L.; Xu, S.
Crystal structure and biochemical features of dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp(143) and Arg(232) play divergent roles toward different substrates
Biochem. Biophys. Res. Commun.
484
40-44
2017
Escherichia coli, Escherichia coli O157
brenda
Linde, D.; Pogni, R.; Canellas, M.; Lucas, F.; Guallar, V.; Baratto, M.C.; Sinicropi, A.; Saez-Jimenez, V.; Coscolin, C.; Romero, A.; Medrano, F.J.; Ruiz-Duenas, F.J.; Martinez, A.T.
Catalytic surface radical in dye-decolorizing peroxidase a computational, spectroscopic and site-directed mutagenesis study
Biochem. J.
466
253-262
2015
Auricularia auricula-judae (I2DBY1), Auricularia auricula-judae
brenda
Uchida, T.; Sasaki, M.; Tanaka, Y.; Ishimori, K.
A dye-decolorizing peroxidase from Vibrio cholerae
Biochemistry
54
6610-6621
2015
Vibrio cholerae (Q9KQ59), Vibrio cholerae
brenda
Bouacem, K.; Rekik, H.; Jaouadi, N.Z.; Zenati, B.; Kourdali, S.; El Hattab, M.; Badis, A.; Annane, R.; Bejar, S.; Hacene, H.; Bouanane-Darenfed, A.; Jaouadi, B.
Purification and characterization of two novel peroxidases from the dye-decolorizing fungus Bjerkandera adusta strain CX-9
Int. J. Biol. Macromol.
106
636-646
2017
Bjerkandera adusta, Bjerkandera adusta CX-9
brenda
Rekik, H.; Nadia, Z.J.; Bejar, W.; Kourdali, S.; Belhoul, M.; Hmidi, M.; Benkiar, A.; Badis, A.; Sallem, N.; Bejar, S.; Jaouadi, B.
Characterization of a purified decolorizing detergent-stable peroxidase from Streptomyces griseosporeus SN9
Int. J. Biol. Macromol.
73
253-263
2015
Streptomyces griseosporeus, Streptomyces griseosporeus SN9
brenda
Chen, C.; Shrestha, R.; Jia, K.; Gao, P.F.; Geisbrecht, B.V.; Bossmann, S.H.; Shi, J.; Li, P.
Characterization of dye-decolorizing peroxidase (DyP) from Thermomonospora curvata reveals unique catalytic properties of a-type DyPs
J. Biol. Chem.
290
23447-23463
2015
Thermomonospora curvata (D1A807), Thermomonospora curvata, Thermomonospora curvata DSM 43183 (D1A807)
brenda
Sugawara, K.; Nishihashi, Y.; Narioka, T.; Yoshida, T.; Morita, M.; Sugano, Y.
Characterization of a novel DyP-type peroxidase from Streptomyces avermitilis
J. Biosci. Bioeng.
123
425-430
2017
Streptomyces avermitilis, Streptomyces avermitilis ATCC31267
brenda
Colpa, D.; Fraaije, M.; Van Bloois, E.
DyP-type peroxidases A promising and versatile class of enzymes
J. Ind. Microbiol. Biotechnol.
41
1-7
2014
Bjerkandera adusta (Q8WZK8), Bjerkandera adusta Dec1 (Q8WZK8)
brenda
Liers, C.; Aranda, E.; Strittmatter, E.; Piontek, K.; Plattner, D.; Zorn, H.; Ullrich, R.; Hofrichter, M.
Phenol oxidation by DyP-type peroxidases in comparison to fungal and plant peroxidases
J. Mol. Catal. B
103
41-46
2014
Exidia glandulosa (I2DBY2), Auricularia auricula-judae (I2DBY1), Mycetinis scorodonius, Mycena epipterygia
-
brenda
Baratto, M.C.; Sinicropi, A.; Linde, D.; Saez-Jimenez, V.; Sorace, L.; Ruiz-Duenas, F.J.; Martinez, A.T.; Basosi, R.; Pogni, R.
Redox-active sites in Auricularia auricula-judae dye-decolorizing peroxidase and several directed variants a multifrequency EPR study
J. Phys. Chem. B
119
13583-13592
2015
Auricularia auricula-judae (I2DBY1), Auricularia auricula-judae
brenda
Yu, W.; Liu, W.; Huang, H.; Zheng, F.; Wang, X.; Wu, Y.; Li, K.; Xie, X.; Jin, Y.
Application of a novel alkali-tolerant thermostable DyP-type peroxidase from Saccharomonospora viridis DSM 43017 in biobleaching of eucalyptus kraft pulp
PLoS ONE
9
e110319
2014
Saccharomonospora viridis (T1SP91), Saccharomonospora viridis, Saccharomonospora viridis DSM 43017 (T1SP91), Saccharomonospora viridis DSM 43017
brenda
Ramzi, A.; Hyeon, J.; Han, S.
Improved catalytic activities of a dye-decolorizing peroxidase (DyP) by overexpression of ALA and heme biosynthesis genes in Escherichia coli
Process Biochem.
50
1272-1276
2015
Bacillus subtilis
-
brenda
Linde, D.; Coscolin, C.; Liers, C.; Hofrichter, M.; Martinez, A.T.; Ruiz-Duenas, F.J.
Heterologous expression and physicochemical characterization of a fungal dye-decolorizing peroxidase from Auricularia auricula-judae
Protein Expr. Purif.
103
28-37
2014
Auricularia auricula-judae (I2DBY1), Auricularia auricula-judae
brenda
Min, K.; Gong, G.; Woo, H.M.; Kim, Y.; Um, Y.
A dye-decolorizing peroxidase from Bacillus subtilis exhibiting substrate-dependent optimum temperature for dyes and beta-ether lignin dimer
Sci. Rep.
5
8245
2015
Bacillus subtilis, Bacillus subtilis KCTC2023
brenda
Loncar, N.; Colpa, D.; Fraaije, M.
Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase
Tetrahedron
72
7276-7281
2016
Thermobifida fusca
-
brenda
Dhankhar, P.; Dalal, V.; Mahto, J.K.; Gurjar, B.R.; Tomar, S.; Sharma, A.K.; Kumar, P.
Characterization of dye-decolorizing peroxidase from Bacillus subtilis
Arch. Biochem. Biophys.
693
108590
2020
Bacillus subtilis (P39597), Bacillus subtilis, Bacillus subtilis 168 (P39597)
brenda
Kimani, V.; Ullrich, R.; Buettner, E.; Herzog, R.; Kellner, H.; Jehmlich, N.; Hofrichter, M.; Liers, C.
First dye-decolorizing peroxidase from an ascomycetous fungus secreted by Xylaria grammica
Biomolecules
11
1391
2021
Xylaria grammica, Xylaria grammica IHIA82
brenda
Wasak, A.; Drozd, R.; Struk, A.; Grygorcewicz, B.
Entrapment of DyP-type peroxidase from Pseudomonas fluorescens Pf-5 into Ca-alginate magnetic beads
Biotechnol. Appl. Biochem.
65
238-245
2018
Pseudomonas fluorescens, Pseudomonas fluorescens Pf-5
brenda
Li, L.; Wang, T.; Chen, T.; Huang, W.; Zhang, Y.; Jia, R.; He, C.
Revealing two important tryptophan residues with completely different roles in a dye-decolorizing peroxidase from Irpex lacteus F17
Biotechnol. Biofuels
14
128
2021
Irpex lacteus (A0A2P1C6N4), Irpex lacteus, Irpex lacteus F17 (A0A2P1C6N4)
brenda
Feng, C.; Pan, M.; Tang, L.
5-Aminolevulinic acid level and dye-decolorizing peroxidase expression regulate heme synthesis in Escherichia coli
Biotechnol. Lett.
44
271-277
2022
Thermobifida fusca (Q47KB1)
brenda
Xu, L.; Sun, J.; Qaria, M.; Gao, L.; Zhu, D.
Dye decoloring peroxidase structure, catalytic properties and applications Current advancement and futurity
Catalysts
11
955
2021
Bacillus subtilis, Bacillus subtilis 168, Pleurotus sapidus, Saccharomonospora viridis, Thermobifida fusca, Thermomonospora curvata
-
brenda
Chaplin, A.; Chicano, T.; Hampshire, B.; Wilson, M.; Hough, M.; Svistunenko, D.; Worrall, J.
An Aromatic dyad motif in dye decolourising peroxidases has implications for free radical formation and catalysis
Chem. Eur. J.
25
6141-6153
2019
Streptomyces lividans
brenda
Musengi, A.; Durrell, K.; Prins, A.; Khan, N.; Agunbiade, M.; Kudanga, T.; Kirby-McCullough, B.; Pletschke, B.; Burton, S.; Le Roes-Hill, M.
Production and characterisation of a novel actinobacterial DyP-type peroxidase and its application in coupling of phenolic monomers
Enzyme Microb. Technol.
141
109654
2020
Streptomyces albidoflavus, Streptomyces albidoflavus BSII#1
brenda
Zitare, U.A.; Habib, M.H.; Rozeboom, H.; Mascotti, M.L.; Todorovic, S.; Fraaije, M.W.
Mutational and structural analysis of an ancestral fungal dye-decolorizing peroxidase
FEBS J.
288
3602-3618
2021
Basidiomycota sp.
brenda
Dhankhar, P.; Dalal, V.; Singh, V.; Sharma, A.K.; Kumar, P.
Structure of dye-decolorizing peroxidase from Bacillus subtilis in complex with veratryl alcohol
Int. J. Biol. Macromol.
193
601-608
2021
Bacillus subtilis, Bacillus subtilis 168
brenda
Linde, D.; Ayuso-Fernandez, I.; Laloux, M.; Aguiar-Cervera, J.E.; de Lacey, A.L.; Ruiz-Duenas, F.J.; Martinez, A.T.
Comparing ligninolytic capabilities of bacterial and fungal dye-decolorizing peroxidases and class-II peroxidase-catalases
Int. J. Mol. Sci.
22
2629
2021
Amycolatopsis sp. ATCC 39116 (K7N5M8), Auricularia auricula-judae (I2DBY1), Thermomonospora curvata (D1A807), Thermomonospora curvata ATCC 19995 (D1A807)
brenda
Rai, A.; Klare, J.P.; Reinke, P.Y.A.; Englmaier, F.; Fohrer, J.; Fedorov, R.; Taft, M.H.; Chizhov, I.; Curth, U.; Plettenburg, O.; Manstein, D.J.
Structural and biochemical characterization of a dye-decolorizing peroxidase from Dictyostelium discoideum
Int. J. Mol. Sci.
22
6265
2021
Dictyostelium discoideum (Q556V8), Dictyostelium discoideum
brenda
Sugawara, K.; Yoshida, T.; Hirashima, R.; Toriumi, R.; Akiyama, H.; Kakuta, Y.; Ishige, Y.; Sugano, Y.
Characterization of class V DyP-type peroxidase SaDyP1 from Streptomyces avermitilis and evaluation of SaDyPs expression in mycelium
Int. J. Mol. Sci.
22
8683
2021
Streptomyces avermitilis, Streptomyces avermitilis ATCC31267
brenda
Nys, K.; Pfanzagl, V.; Roefs, J.; Obinger, C.; Van Doorslaer, S.
In vitro heme coordination of a dye-decolorizing peroxidase - The interplay of key amino acids, pH, buffer and glycerol
Int. J. Mol. Sci.
22
9849
2021
Klebsiella pneumoniae (A0A0W8ATM9)
brenda
Guo, W.; Xu, J.; Wu, S.; Gao, S.; Wen, G.; Tan, X.; Lin, Y.
Design and engineering of an efficient peroxidase using myoglobin for dye decolorization and lignin bioconversion
Int. J. Mol. Sci.
23
413
2022
Physeter macrocephalus
brenda
Li, F.; Shao, R.; Mao, Y.; Yu, W.; Yu, H.
Enzyme cascade reaction involving lytic polysaccharide monooxygenase and dye-decolorizing peroxidase for chitosan functionalization
J. Agric. Food Chem.
69
1049-1056
2021
Pleurotus ostreatus, Pleurotus ostreatus HAUCC 162
brenda
de Eugenio, L.I.; Peces-Perez, R.; Linde, D.; Prieto, A.; Barriuso, J.; Ruiz-Duenas, F.J.; Martinez, M.J.
Characterization of a dye-decolorizing peroxidase from Irpex lacteus expressed in Escherichia coli An enzyme with wide substrate specificity able to transform lignosulfonates
J. Fungi (Basel)
7
325
2021
Irpex lacteus
brenda
Uchida, T.; Omura, I.; Umetsu, S.; Ishimori, K.
Radical transfer but not heme distal residues is essential for pH dependence of dye-decolorizing activity of peroxidase from Vibrio cholerae
J. Inorg. Biochem.
219
111422
2021
Vibrio cholerae
brenda
Cordas, C.M.; Nguyen, G.S.; Valerio, G.N.; Jonsson, M.; Soellner, K.; Aune, I.H.; Wentzel, A.; Moura, J.J.G.
Discovery and characterization of a novel Dyp-type peroxidase from a marine actinobacterium isolated from Trondheim fjord, Norway
J. Inorg. Biochem.
226
111651
2022
Actinomycetota
brenda
Habib, M.; Rozeboom, H.; Fraaije, M.
Characterization of a new DyP-peroxidase from the alkaliphilic cellulomonad, Cellulomonas bogoriensis
Molecules
24
1208
2019
Cellulomonas bogoriensis
brenda
Krahe, N.K.; Berger, R.G.; Ersoy, F.
A DyP-Type peroxidase of Pleurotus sapidus with alkene cleaving activity
Molecules
25
1536
2020
Pleurotus sapidus (A0A6H0MBW1), Pleurotus sapidus
brenda
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