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Enzyme Nomenclature
Information on EC 1.11.1.16 - versatile peroxidase
for references in articles please use BRENDA:EC1.11.1.16
Word Map on EC 1.11.1.16
- 1.11.1.16
- pleurotus
-
lignin
- peroxidases
-
ligninolytic
- eryngii
-
white-rot
- bjerkandera
- ostreatus
- laccase
-
veratryl
- adusta
- chrysosporium
-
phanerochaete
- trametes
-
non-phenolic
- 2,6-dimethoxyphenol
-
aryl-alcohols
-
mn-oxidizing
-
delignification
- phlebia
-
lignin-degrading
- degradation
-
mn-dependent
- synthesis
- industry
- analysis
- paper production
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.11.1.16
-
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RECOMMENDED NAME
GeneOntology No.
versatile peroxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O
(2)
-
-
-
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
(1)
-
-
-
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
study of reaction of H2O2 with the enzyme in the absence of substrate suggests an amino acid radical in moderate distance from ferryl heme. A tryptophan radical is formed during the catalytic mechanism
-
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
the radical intermediate in the reaction of enzyme with H2O2 is a tryptophan neutral radical at W164
-
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
NMR study of enzyme both in resting state and cyanide-inhibited form. Analysis of interaction with Mn2+
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
reactive-black-5:hydrogen-peroxide oxidoreductase
A hemoprotein. This ligninolytic peroxidase combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, EC 1.11.1.13, manganese peroxidase and EC 1.11.1.14, lignin peroxidase. Unlike these two enzymes, it is also able to oxidize phenols, hydroquinones and both low- and high-redox-potential dyes, due to a hybrid molecular architecture that involves multiple binding sites for substrates [2,4].
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CAS REGISTRY NUMBER
COMMENTARY
114995-15-2
-
42613-30-9
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
growth without Mn2+ added, stimulation of enzyme synthesis by addition of glycolate, glyoxylate, or oxalate to medium
-
-
growth without Mn2+ added, stimulation of enzyme synthesis by addition of glycolate, glyoxylate, or oxalate to medium
-
-
induction of enzyme transcripts and activity by growth on glucose-peptone medium, addition of more than 0.025 mM Mn2+ results in no detectable enzyme transkripts or activity. Enzyme expression is strongly induced by exogenous H2O2 or continuous H2O2 generation
-
-
isoenzymes MP-1 and MP-2, addition of Mn2+ to growth medium represses enzyme activity
-
-
induction of enzyme by rich peptone medium, addition of 0.5 mM Mn2+ decrease enzyme activity by 50%
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
despite the presence of Mn2+ in the medium, a transformant overexpressing the enzyme produces mnp4 transcripts as well as versatile peroxidase activity as early as 4 days after inoculation. The level of expression is constant throughout 10 days of incubation and the activity is comparable to the typical activity in Mn2+-deficient media
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,4-dimethoxybenzene + H2O2
1,4-benzoquinone + H2O
-
Mn2+-independent activity
-
-
?
1-methylanthracene + H2O2
1-methylanthraquinone + H2O
-
at 43% of the rate with 9-methylanthracene
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
? + H2O
-
-
-
?
2,7-diaminofluorene + H2O2
? + H2O
-
during oxidation of 2,7-diaminofluorene, both with and without Mn2+, biphasic kinetics with apparent saturation in both micromolar and millimolar ranges are obtained
-
-
?
2-chloro-1,4-dimethoxybenzene + H2O2
2-chloro-1,4-benzoquinone + H2O
-
Mn2+-independent activity
-
-
?
2-methylanthracene + H2O2
2-methylanthraquinone + H2O
-
at 24% of the rate with 9-methylanthracene
-
-
?
3-methyl-2-benzothiazolinone hydrazone + H2O2
? + H2O
-
enzyme has several substrate binding sites for 3-methyl-2-benzothiazolinone hydrazone, in addition to low and high affinity binding sites for Mn2+
-
-
?
anthracene + H2O2
anthraquinone + H2O
-
at 4.8% of the rate with 9-methylanthracene
-
-
?
bovine pancreatic RNase
oxidized bovine pancreatic RNase
-
no redox mediators involved
-
-
?
carbazole + H2O2
? + H2O
-
at 4.8% of the rate with 9-methylanthracene
-
-
?
manganese(II)-substituted polyoxometalate + H2O2
manganese(III)-substituted polyoxometalate + H2O2
-
-
-
-
?
Mn2+ + H2O2 + remazol black-5
?
-
incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
-
-
-
Mn2+ + H2O2 + remazol blue-19
?
-
incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
-
-
-
Mn2+ + H2O2 + remazol brilliant violet
?
-
incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
-
-
-
Mn2+ + H2O2 + remazol orange-16
?
-
incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
-
-
-
Mn2+ + H2O2 + rose bengal
?
-
incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
-
-
-
p-dimethoxybenzene + H2O2
benzoquinone + H2O
-
catalyzed by isoforms PS3, PS1
-
-
?
phenol red + H2O2
oxidized phenol red + H2O
-
Mn2+-dependent activity
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
Mn2+-independent activity
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
coerulignone + ?
-
Mn2+-independent activity
-
-
?
2,6-dimethoxyphenol + H2O2
coerulignone + ?
-
Mn2+-independent activity
-
-
?
2,6-dimethoxyphenol + H2O2
coerulignone + ?
-
Mn2+-dependent and independent activity
-
-
?
lignin + H2O2
? + H2O
-
lignin fraction from straw pulpin, versatile peroxidase reacts with soluble lignin fragments in the absence of added mediators, most probably causing extensive polymerisation of high and intermediate fractions of lignin, and an increase of the small-molecular-mass lignin fraction
-
-
?
lignin + H2O2
? + H2O
-
substrate Kraft lignin. The highest production of radicals with minimal loss of activity, is obtained by using an enzyme dose of 15 U/g, with a continuous addition of H2O2 during 1 h. Enzymatically generated Mn(III)-malonate is able to activate lignin
-
-
?
lignin + H2O2
? + H2O
-
substrate Kraft lignin. The highest production of radicals with minimal loss of activity, is obtained by using an enzyme dose of 15 U/g, with a continuous addition of H2O2 during 1 h. Enzymatically generated Mn(III)-malonate is able to activate lignin
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
-
the Mn2+-binding site in versatile peroxidase is formed by the side-chains of Glu36, Glu40, and Asp175 located in front of the internal (i.e. more distant from the main haem access-channel) propionate of haem, and connected to the solvent by a narrow access-channel that presents a variable geometry during catalysis
-
-
?
Reactive Black 5 + H2O2
?
-
versatile peroxidase activity on Reactive Black 5 is eliminated by the R257D mutation
-
-
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
-
-
-
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
-
catalyzed by isoform PS1
-
-
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
-
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Mn2+-independent activity
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
catalyzed by isoforms PS2, PS1
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Mn2+-independent activity
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
a solvent-exposed tryptophan is the catalytically-active residue in veratryl alcohol oxidation, initiating an electron transfer pathway to haem
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
-
?
additional information
?
-
-
enzyme is able to decolorize 27 out of 41 industrial dyes tested
-
-
-
additional information
?
-
-
manganese peroxidase activity is more efficient than lignin peroxidase activity, with activity increasing with increasing concentrations of Mn2+ due to a second metal binding site involved in homotropic substrate Mn2+ activation. The activation of maganese peroxidase is also accompanied by a decrease in both activation energy and substrate Mn2+ affinity
-
-
-
additional information
?
-
-
oxidation of substrates may occur in two ways, either directly by the enzyme or by diffusible chelated Mn3+ as an oxidizing agent
-
-
-
additional information
?
-
-
enzyme is able to oxidize efficiently Mn2+ and phenolic and nonphenolic compounds in absence of this ion
-
-
-
additional information
?
-
-
in presence of H2O2 and Mn2+, a cell-free supernatant is capable to decolorize commercial azo dyes acid black 1 and reactive black 5, reaching efficiencies between 15 and 95%. For all assays performed with 33 microM Mn2+, the initial rate of the decolorization process is dependent on the dosage of H2O2
-
-
-
additional information
?
-
-
in presence of H2O2 and Mn2+, a cell-free supernatant is capable to decolorize commercial azo dyes acid black 1 and reactive black 5, reaching efficiencies between 15 and 95%. For all assays performed with 33 microM Mn2+, the initial rate of the decolorization process is dependent on the dosage of H2O2
-
-
-
additional information
?
-
-
in the absence of Mn2+, efficient hydroquinone oxidation is dependent on exogenous H2O2. In the presence of Mn2+, exogenous H2O2 is not required for complete oxidation of hydroquinones
-
-
-
additional information
?
-
-
versatile peroxidase is able to oxidize typical substrates of other peroxidases, these ‘hybrid’ properties are due to the coexistence in a single protein of different catalytic sites reminiscent of those present in the other basidiomycete peroxidase families
-
-
-
additional information
?
-
-
presence of two independent catalytic sites for different phenols and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in native enzyme, characterizedby high and low specificity constants, i.e. Km in the micromolar range and Km in the millimolar range, respcetively
-
-
-
additional information
?
-
no activity with Phenol Red and Remazol Brilliant Blue
-
-
-
additional information
?
-
-
no substrates: Fe2+, veratryl alcohol
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
enzyme shows the typical Soret band, heme content is 0.5 mol per mol of protein
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Manganese
Mn2+
Ca2+
-
required, Ca2+-depleted enzyme is able to form the active intermediate compound I but its long range electron transfer has been disrupted
Manganese
-
oxidation of Mn(II) to Mn(III), presence of manganese in the reaction mixture with industrial dyes does not enhance the decoloration rate
Manganese
-
Km value 0.022 for wild-type, 0.021 for mutant W170A, 0.022 for mutant R263N, 0.026 for mutant Q266F, 0.027 for mutant V166/168L
Mn2+
-
activity of manganese peroxidase progressively increases with concentration of Mn2+ to a maximum at about 1.8 mM, with a corresponding decrease in lignin peroxidase activity to less than 10%
Mn2+
-
isoenzyme Pl, putative Mn-interaction site near E35, E39, D175. Isoenzyme Ps1, putative Mn-interaction site near E36, E40, D181
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
substrate inhibition
bovine pancreatic RNase
-
competitive to oxidation of veratryl alcohol, non-competitive to oxidation of Mn2+
-
N-bromosuccinimide
-
modification of tryptophan residues by N-bromosuccinimide drastically reduces the Mn(II)-independent activity and dye decoloration, while Mn(II)-dependent activity is maintained. Effect is not reversed by addition of mediators
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.4
manganese(II)-substituted polyoxometalate
-
in 0.1 M sodium tartrate, pH 5.0, at 20°C
-
0.005
vanillylidenacetone
-
presence of Mn2+, isoenzyme MP-1, pH 5.0; presence of Mn2+, isoenzyme MP-2, pH 5.0
0.0007
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C
0.0017
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant R257L
0.0023
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant P76G, high efficiency site, pH 3.5, 25°C
0.0026
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant M247L
0.0028
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant S158E
0.003
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, wild-type
0.003
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild-type, high efficiency site, pH 3.5, 25°C
0.0032
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant R257A/A260F
0.0035
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant M247F
0.0036
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant R257K
0.004
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant S158D
0.004
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K176D, high efficiency site, pH 3.5, 25°C
0.0041
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant F142G, high efficiency site, pH 3.5, 25°C
0.0054
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K176G, high efficiency site, pH 3.5, 25°C; mutant K215G, high efficiency site, pH 3.5, 25°C; mutant P141G, high efficiency site, pH 3.5, 25°C
0.0065
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant K264A
0.008
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K215Q, high efficiency site, pH 3.5, 25°C
0.009
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant A260F
0.0143
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G, high efficiency site, pH 3.5, 25°C
0.0194
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C; mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
0.056
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
0.0836
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K215G, low efficiency site, pH 3.5, 25°C
0.18
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at 30°C and pH 4.5
0.305
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G, low efficiency site, pH 3.5, 25°C
0.383
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K176G, low efficiency site, pH 3.5, 25°C
0.461
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant P141G, low efficiency site, pH 3.5, 25°C
0.48
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
absence of Mn2+, pH 3.0, temperature not specified in the publication
0.54
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild-type, pH 3.5, temperature not specified in the publication
0.54
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 3.0 and 25°C
0.828
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant F142G, low efficiency site, pH 3.5, 25°C
0.86
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
presence of Mn2+, pH 3.0, temperature not specified in the publication
1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant W164S, low efficiency site, pH 3.5, 25°C
1.09
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild-type, low efficiency site, pH 3.5, 25°C
1.66
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K215Q, low efficiency site, pH 3.5, 25°C
2.23
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K176D, low efficiency site, pH 3.5, 25°C
2.86
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant P76G, low efficiency site, pH 3.5, 25°C
0.01
2,6-dimethoxyphenol
-
presence of Mn2+, isoenzyme MP-1, pH 5.0; presence of Mn2+, isoenzyme MP-2, pH 5.0
0.036
2,6-dimethoxyphenol
-
mutant P76G, high efficiency site, pH 3.5, 25°C
0.038
2,6-dimethoxyphenol
-
mutant K176D, high efficiency site, pH 3.5, 25°C
0.058
2,6-dimethoxyphenol
-
mutant K215G, high efficiency site, pH 3.5, 25°C
0.063
2,6-dimethoxyphenol
-
presence of Mn2+, pH 7.0, temperature not specified in the publication
0.065
2,6-dimethoxyphenol
-
mutant F142G, high efficiency site, pH 3.5, 25°C
0.066
2,6-dimethoxyphenol
-
mutant E140G, high efficiency site, pH 3.5, 25°C
0.078
2,6-dimethoxyphenol
-
mutant K215Q, high efficiency site, pH 3.5, 25°C; wild-type, high efficiency site, pH 3.5, 25°C
0.104
2,6-dimethoxyphenol
-
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
0.119
2,6-dimethoxyphenol
-
mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C
0.155
2,6-dimethoxyphenol
-
mutant P141G, high efficiency site, pH 3.5, 25°C
0.189
2,6-dimethoxyphenol
-
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
0.345
2,6-dimethoxyphenol
-
absence of Mn2+, pH not specified in the publication, temperature not specified in the publication
2.38
2,6-dimethoxyphenol
-
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
2.97
2,6-dimethoxyphenol
-
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
3.33
2,6-dimethoxyphenol
-
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
6.5
2,6-dimethoxyphenol
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
16
2,6-dimethoxyphenol
-
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
32
2,6-dimethoxyphenol
-
wild-type, pH 3.5, temperature not specified in the publication
0.009
2,7-diaminofluorene
-
absence of Mn2+, pH 4.5, temperature not specified in the publication
0.038
2,7-diaminofluorene
-
presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
0.0251
4-hydroquinone
-
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
0.0362
4-hydroquinone
-
mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C
0.0397
4-hydroquinone
-
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
0.41
4-hydroquinone
-
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
0.618
4-hydroquinone
-
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
0.884
4-hydroquinone
-
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
1.18
4-hydroquinone
-
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
0.051
H2O2
-
wild-type, pH 3.5, temperature not specified in the publication
0.2
H2O2
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
0.015
Mn2+
-
cosubstrate dimethoxyphenol, isoenzyme MP-1, pH 5.0; cosubstrate dimethoxyphenol, isoenzyme MP-2, pH 5.0
0.02
Mn2+
-
cosubstrate H2O2, isoenzyme MP-1, pH 5.0; cosubstrate H2O2, isoenzyme MP-2, pH 5.0
0.045
Mn2+
-
wild-type, pH 3.5, temperature not specified in the publication
0.12
Mn2+
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
0.68
Mn2+
-
pH not specified in the publication, temperature not specified in the publication
0.0066
Reactive Black 5
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
0.007
Reactive Black 5
-
wild-type, pH 3.5, temperature not specified in the publication
0.035
syringaldazine
-
presence of Mn2+, pH 7.0, temperature not specified in the publication
0.066
syringaldazine
-
absence of Mn2+, pH 7.0, temperature not specified in the publication
0.304
veratryl alcohol
-
absence of Mn2+, pH 3.0, temperature not specified in the publication
0.53
veratryl alcohol
-
presence of Mn2+, pH 4.5, temperature not specified in the publication
13.5
veratryl alcohol
-
pH 3.0, 25°C, mutant R257A/A260F; pH 3.0, 25°C, mutant R257L
additional information
fulvic acid
-
Hill coefficient 3.0, presence of Mn2+, Km value 0.009 g/l, pH 3.5, 25°C; Hill coefficient 3.6, absence of Mn2+, Km value 0.044 g/l, pH 3.5, 25°C
additional information
humic acid
-
Hill coefficient 1.2, absence of Mn2+, Km value 0.08 g/l, pH 3.5, 25°C; Hill coefficient 2.8, presence of Mn2+, Km value 0.005 g/l, pH 3.5, 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
47
manganese(II)-substituted polyoxometalate
-
in 0.1 M sodium tartrate, pH 5.0, at 20°C
-
0.7
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant M247F
2.77
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
absence of Mn2+, pH 3.0, temperature not specified in the publication
4.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant M247L
5.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant A260F
6.2
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
presence of Mn2+, pH 3.0, temperature not specified in the publication
6.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant P76G, high efficiency site, pH 3.5, 25°C
7.7
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant S158D
7.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K215Q, high efficiency site, pH 3.5, 25°C
8.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, wild-type
8.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild-type, high efficiency site, pH 3.5, 25°C
8.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant K264A
9.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant S158E
10.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant F142G, high efficiency site, pH 3.5, 25°C
11.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant R257K
12.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G, high efficiency site, pH 3.5, 25°C
13.2
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K176G, high efficiency site, pH 3.5, 25°C
13.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K176D, high efficiency site, pH 3.5, 25°C; mutant K215G, high efficiency site, pH 3.5, 25°C
16.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant P141G, high efficiency site, pH 3.5, 25°C
18.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant R257A/A260F
19.2
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
22.2
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.5, 25°C, mutant R257L
93
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant P141G, low efficiency site, pH 3.5, 25°C
146
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant P76G, low efficiency site, pH 3.5, 25°C
154
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant F142G, low efficiency site, pH 3.5, 25°C
162
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
165
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K215Q, low efficiency site, pH 3.5, 25°C
186
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild-type, low efficiency site, pH 3.5, 25°C
204
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K215G, low efficiency site, pH 3.5, 25°C
205
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant W164S, low efficiency site, pH 3.5, 25°C
216
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G, low efficiency site, pH 3.5, 25°C
220
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild-type, pH 3.5, temperature not specified in the publication
220
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 3.0 and 25°C
223
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K176D, low efficiency site, pH 3.5, 25°C
227
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
235
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
259
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K176G, low efficiency site, pH 3.5, 25°C
326
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
365
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
12300
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at 30°C and pH 4.5
4.6
2,6-dimethoxyphenol
-
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
10.6
2,6-dimethoxyphenol
-
absence of Mn2+, pH not specified in the publication, temperature not specified in the publication
10.6
2,6-dimethoxyphenol
-
mutant K176D, high efficiency site, pH 3.5, 25°C
17.3
2,6-dimethoxyphenol
-
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
20.4
2,6-dimethoxyphenol
-
mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C
30
2,6-dimethoxyphenol
-
presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
50.2
2,6-dimethoxyphenol
-
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
56.6
2,6-dimethoxyphenol
-
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
58
2,6-dimethoxyphenol
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
61
2,6-dimethoxyphenol
-
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
67
2,6-dimethoxyphenol
-
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
98
2,6-dimethoxyphenol
-
wild-type, pH 3.5, temperature not specified in the publication
231.6
2,6-dimethoxyphenol
-
mutant K176G, low efficiency site, pH 3.5, 25°C
0.19
2,7-diaminofluorene
-
absence of Mn2+, pH 4.5, temperature not specified in the publication
0.83
2,7-diaminofluorene
-
presence of Mn2+, pH 7.0, temperature not specified in the publication
8
4-hydroquinone
-
mutant K176D, high efficiency site, pH 3.5, 25°C; mutant P76G, high efficiency site, pH 3.5, 25°C
14.6
4-hydroquinone
-
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
20
4-hydroquinone
-
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C; mutant W164S, low efficiency site, pH 3.5, 25°C
20.4
4-hydroquinone
-
mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C
65.5
4-hydroquinone
-
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
82.1
4-hydroquinone
-
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
82.2
4-hydroquinone
-
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
85.6
4-hydroquinone
-
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
490
H2O2
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
2
Mn2+
25°C, pH 5, mutant E36A/E40A/D175A; 25°C, pH 5, mutant E36A/E40A/D175A/P327ter
3.9
Mn2+
-
pH not specified in the publication, temperature not specified in the publication
75
Mn2+
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
298
Mn2+
-
0.000083 1/sec/mg, incubates 30 min at 37°C, pH 9.0, spectrophotometrically measured at 415 nm; wild-type, pH 5.0
5
Reactive Black 5
-
0.0 M NaCl, 55.6 IgG relative content, 5.5% relative DNase activity; wild-type, pH 3.5
10.6
Reactive Black 5
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
11.8
Reactive Black 5
-
wild-type, pH 3.5, temperature not specified in the publication
0.22
syringaldazine
-
absence of Mn2+, pH 7.0, temperature not specified in the publication
6.1
syringaldazine
-
presence of Mn2+, pH 7.0, temperature not specified in the publication
7.08
veratryl alcohol
-
absence of Mn2+, pH 3.0, temperature not specified in the publication
9.6
veratryl alcohol
-
pH 3.0, 25°C, mutant S158D; pH 3.0, 25°C, mutant S158E
26.8
veratryl alcohol
-
presence of Mn2+, pH 4.5, temperature not specified in the publication
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
7.36
manganese(II)-substituted polyoxometalate
-
in 0.1 M sodium tartrate, pH 5.0, at 20°C
-
1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K215Q, high efficiency site, pH 3.5, 25°C
2.45
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K176G, high efficiency site, pH 3.5, 25°C
2.53
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
2.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K215G, high efficiency site, pH 3.5, 25°C
3.48
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K176D, high efficiency site, pH 3.5, 25°C
5.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
absence of Mn2+, pH 3.0, temperature not specified in the publication
7.2
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
presence of Mn2+, pH 3.0, temperature not specified in the publication
51
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant P76G, low efficiency site, pH 3.5, 25°C
99
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K215Q, low efficiency site, pH 3.5, 25°C
100
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K176D, low efficiency site, pH 3.5, 25°C
171
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild-type, low efficiency site, pH 3.5, 25°C
185
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant F142G, low efficiency site, pH 3.5, 25°C
200
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant W164S, low efficiency site, pH 3.5, 25°C
201
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant P141G, low efficiency site, pH 3.5, 25°C
244
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K215G, low efficiency site, pH 3.5, 25°C
410
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild-type, pH 3.5, temperature not specified in the publication
410
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 3.0 and 25°C
676
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant K176G, low efficiency site, pH 3.5, 25°C
710
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G, low efficiency site, pH 3.5, 25°C
882
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G, high efficiency site, pH 3.5, 25°C
1120
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
2640
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant F142G, high efficiency site, pH 3.5, 25°C
2700
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
wild-type, high efficiency site, pH 3.5, 25°C
2830
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant P76G, high efficiency site, pH 3.5, 25°C
3010
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant P141G, high efficiency site, pH 3.5, 25°C
4090
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
5670
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
5680
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
6480
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
3.1
2,6-dimethoxyphenol
-
wild-type, pH 3.5, temperature not specified in the publication
3.8
2,6-dimethoxyphenol
-
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
9.1
2,6-dimethoxyphenol
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
15.1
2,6-dimethoxyphenol
-
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
22.6
2,6-dimethoxyphenol
-
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
23.8
2,6-dimethoxyphenol
-
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
30.7
2,6-dimethoxyphenol
-
absence of Mn2+, pH not specified in the publication, temperature not specified in the publication
44.6
2,6-dimethoxyphenol
-
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
91.3
2,6-dimethoxyphenol
-
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
171
2,6-dimethoxyphenol
-
mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C; mutant P76G, high efficiency site, pH 3.5, 25°C
476.2
2,6-dimethoxyphenol
-
presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
21.1
2,7-diaminofluorene
-
absence of Mn2+, pH 4.5, temperature not specified in the publication
21.8
2,7-diaminofluorene
-
presence of Mn2+, pH 7.0, temperature not specified in the publication
55.6
4-hydroquinone
-
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
96.8
4-hydroquinone
-
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
132.8
4-hydroquinone
-
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
203.2
4-hydroquinone
-
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
368
4-hydroquinone
-
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
565
4-hydroquinone
-
mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C
600
4-hydroquinone
-
mutant K176D, high efficiency site, pH 3.5, 25°C; mutant K215G, high efficiency site, pH 3.5, 25°C
800
4-hydroquinone
-
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C; mutant P76G, high efficiency site, pH 3.5, 25°C
1.6
guaiacol
-
mutant F142G, pH 3.5, 25°C; mutant K215G, pH 3.5, 25°C; mutant P76G, pH 3.5, 25°C
2
guaiacol
-
mutant K176G, pH 3.5, 25°C; mutant K215Q, pH 3.5, 25°C; wild-type, pH 3.5, 25°C
2400
H2O2
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
2650
H2O2
-
wild-type, pH 3.5, temperature not specified in the publication
5.7
Mn2+
-
pH not specified in the publication, temperature not specified in the publication
630
Mn2+
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
1190
Mn2+
-
wild-type, pH 3.5, temperature not specified in the publication
1600
Reactive Black 5
-
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
1670
Reactive Black 5
-
wild-type, pH 3.5, temperature not specified in the publication
3.3
syringaldazine
-
absence of Mn2+, pH 7.0, temperature not specified in the publication
174.3
syringaldazine
-
presence of Mn2+, pH 7.0, temperature not specified in the publication
2.3
veratryl alcohol
-
absence of Mn2+, pH 3.0, temperature not specified in the publication
50.6
veratryl alcohol
-
presence of Mn2+, pH 4.5, temperature not specified in the publication
additional information
fulvic acid
-
Hill coefficient 3.0, presence of Mn2+, kcat/Km value 300 g/l/min, pH 3.5, 25°C; Hill coefficient 3.6, absence of Mn2+, kcat/Km value 25 g/l/min, pH 3.5, 25°C
additional information
humic acid
-
Hill coefficient 1.2, absence of Mn2+, kcat/Km value 15.5 g/l/min, pH 3.5, 25°C; Hill coefficient 2.8, presence of Mn2+, kcat/Km value 240 g/l/min, pH 3.5, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.4
with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as substrate, at 30°C and pH 4.5
8.8
-
substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), pH 3.5, 25°C
10.8
-
substrate 2,6-dimthoxy-1,4-benzohydroquinone, pH 5.0, absence of Mn2+
61.48
-
after 5.66fold purification, with Mn2+ as substrate, at pH 5.0 and 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
4.2
-
and 3.0, substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), presence of Mn2+
4.5
6.5
-
and 3.0, substrate veratryl alcohol, absence of Mn2+; and 3.0, substrate veratryl alcohol, presence of Mn2+; and 5.0, substrate 2,7-diaminofluorene, presence of Mn2+
7
-
and 4.5, substrate 2,7-diaminofluorene, absence of Mn2+; substrate syringaldazine, absence and presence of Mn2+; substrate syringaldazine, absence of Mn2+
3
-
and 4.2, substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), presence of Mn2+; and 6.5, substrate veratryl alcohol, absence of Mn2+; substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), absence of Mn2+
3
-
Mn2+-independent oxidation of substituted phenols and aromatic molecules
4.5
-
and 7.0, substrate 2,7-diaminofluorene, absence of Mn2+; substrate veratryl alcohol, presence of Mn2+
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.65
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Pleurotus eryngii;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41000
x * 43000, SDS-PAGE, x * 41000, SDS-PAGE of deglycosylated enzyme
43000
43000
x * 43000, SDS-PAGE, x * 41000, SDS-PAGE of deglycosylated enzyme
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
-
W170 exposed on enzyme surface is a substrate-binding site both for veratryl alcohol and for polymeric substrates
?
x * 43000, SDS-PAGE, x * 41000, SDS-PAGE of deglycosylated enzyme
?
x * 34600, calculated from amino acid sequence; x * 38000, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
sequence has one potential N-glycosylation site at Asn109
glycoprotein
-
MP-1, up to 5% carbohydrate content, MP-2, up to 7% carbohydrate
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of enzyme model and identification of active sites for oxidation of Mn2+ and of aromatic substrates
hanging drop vapor diffusion method, crystal structures of untreated versatile peroxidase (immediately after expression in Escherichia coli and in vitro reconstitution), native versatile peroxidase (treated with Mn2+), D175A variant, and wild-type verstile peroxidase (from Pleurotus eryngii culture)
mutant enzyme W164Y, sitting-drop vapor diffusion method, resolution 1.94 A
-
mutants E140G, P141G, K176G, and E140G/K176G, to 1.6, 2.0, 1.5, 1.7 and 2.35 A resolution, respectively
-
sitting drop vapor diffusion method, using 0.1 M sodium MES buffer at pH 6.5, 25% (w/v) PEG 4000 and 0.2 M MgCl2
-
resonance Raman and electrochemical study. In solution, enzyme shows a heterogeneous spin population, with the five-coordinated quantum mechanically mixed-spin state being the most populated in the latter. 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 -260 mV
-
structural changes in the mutants D153H, D153A, R244L, N246H, N246A, D153A/N246A are confined to the distal heme environment
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 55
-
Residual activity of roughly 100% is found after incubation at 25 to 55°C with all three substrates. Stability decreases gradually at temperatures from 60 to 70°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HiTrap Q column chromatography, and Mono Q column chromatography
-
recombinant protein
recombinant protein