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2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
guaiacol + H2O2
oxidized guaiacol + 2 H2O
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
-
-
-
?
1,4-benzohydroquinone + H2O2
? + H2O
-
-
-
-
?
2 2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn2+ + 2 H+ + H2O2
2 Mn3+ + 2 H2O
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
-
-
?
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 + H+
?
-
-
-
?
2,6-dimethoxybenzohydroquinone + H2O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + H+ + H2O2
?
2-methoxy-1,4-benzohydroquinone + H2O2
? + H2O
-
-
-
-
?
4-hydroquinone + H2O2
4-benzoquinone + H2O
-
-
-
?
catechol + H2O2
2-benzoquinone + H2O
-
-
-
?
guaiacol + H2O2
3,3'-dimethoxy-4,4'-biphenylquinone + H2O
-
-
-
?
guaiacol + H2O2
? + H2O
-
-
-
-
?
guaiacol + H2O2
oxidized guaiacol + 2 H2O
-
-
-
?
manganese(II)-substituted polyoxometalate + H2O2
manganese(III)-substituted polyoxometalate + H2O2
-
-
-
-
?
methoxyhydroquinone + H2O2
? + H2O
Mn2+ + H+ + H2O2
Mn3+ + H2O
Mn2+ + H2O2 + Reactive Black 5
?
-
-
-
?
NADH + H2O2
NAD+ + H2O
-
-
-
-
?
p-dimethoxybenzene + H2O2
benzoquinone + H2O
-
catalyzed by isoforms PS3, PS1
-
-
?
phenol red + H2O2
oxidized phenol red + H2O
-
Mn2+-dependent activity
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
-
-
-
?
Reactive Black 5 + H+ + H2O2
?
Reactive Black 5 + H2O2
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
sinapic acid + H2O2
? + 2 H2O
-
-
-
?
syringol + H2O2
? + H2O
-
-
-
-
?
vanillylidenacetone + H2O2
? + H2O
-
Mn2+-dependent activity
-
-
?
veratryl alcohol + H2O2
verytryl aldehyde + 2 H2O
-
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
additional information
?
-
2 2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
-
-
-
?
2 2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
-
-
-
-
?
2 2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
-
Mn2+-dependent and independent activity
-
-
?
2 Mn2+ + 2 H+ + H2O2
2 Mn3+ + 2 H2O
-
-
-
?
2 Mn2+ + 2 H+ + H2O2
2 Mn3+ + 2 H2O
-
-
-
-
?
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
-
-
-
-
?
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 + H+ + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H+ + H2O2
?
-
-
-
?
methoxyhydroquinone + H2O2
? + H2O
-
-
-
-
?
methoxyhydroquinone + H2O2
? + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
-
-
-
-
?
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 + H+ + H2O2
?
-
-
-
-
?
Reactive Black 5 + H+ + H2O2
?
-
-
-
?
Reactive Black 5 + H2O2
?
-
-
-
?
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
-
-
-
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
-
-
-
-
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
-
-
-
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
-
-
-
-
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
-
catalyzed by isoform PS1
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
?
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
-
-
?
additional information
?
-
the enzyme shows a broad substrate spectrum
-
-
-
additional information
?
-
-
the enzyme shows a broad substrate spectrum
-
-
-
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
?
-
-
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
-
-
?
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0.0007 - 2.86
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
0.01 - 76
2,6-dimethoxyphenol
0.0059 - 2.24
4-hydroquinone
6.4
manganese(II)-substituted polyoxometalate
-
in 0.1 M sodium tartrate, pH 5.0, at 20°C
-
0.017 - 3
methoxyhydroquinone
2.4
p-dimethoxybenzene
-
pH 3.0, isoenzyme PS1
0.0013 - 0.007
Reactive Black 5
0.005
vanillylidenacetone
1.65 - 54.7
veratryl alcohol
additional information
additional information
-
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
0.0054
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K215G, high efficiency site, pH 3.5, 25°C
0.0054
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
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
0.0194
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
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
0.305
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
0.54
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
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
0.01
2,6-dimethoxyphenol
-
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
0.065
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
0.078
2,6-dimethoxyphenol
wild-type, high efficiency site, pH 3.5, 25°C
0.1
2,6-dimethoxyphenol
mutant K176G, 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
0.16
2,6-dimethoxyphenol
-
absence of Mn2+, isoenzyme MP-1, pH 3.0
0.189
2,6-dimethoxyphenol
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
0.25
2,6-dimethoxyphenol
-
absence of Mn2+, isoenzyme MP-2, pH 3.0
2.38
2,6-dimethoxyphenol
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
2.56
2,6-dimethoxyphenol
mutant K215Q, 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
10.5
2,6-dimethoxyphenol
wild-type, low efficiency site, pH 3.5, 25°C
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
32
2,6-dimethoxyphenol
at pH 3.0 and 25°C
36.2
2,6-dimethoxyphenol
mutant K176G, low efficiency site, pH 3.5, 25°C
37.4
2,6-dimethoxyphenol
mutant E140G, low efficiency site, pH 3.5, 25°C
37.6
2,6-dimethoxyphenol
mutant W164S, low efficiency site, pH 3.5, 25°C
76
2,6-dimethoxyphenol
mutant P141G, low efficiency site, pH 3.5, 25°C
0.0059
4-hydroquinone
mutant F142G, high efficiency site, pH 3.5, 25°C
0.0103
4-hydroquinone
mutant P76G, high efficiency site, pH 3.5, 25°C
0.0122
4-hydroquinone
mutant K215Q, high efficiency site, pH 3.5, 25°C
0.013
4-hydroquinone
mutant K176D, high efficiency site, pH 3.5, 25°C
0.0156
4-hydroquinone
wild-type, high efficiency site, pH 3.5, 25°C
0.0174
4-hydroquinone
mutant K215G, high efficiency site, pH 3.5, 25°C
0.0189
4-hydroquinone
mutant K176G, high efficiency site, pH 3.5, 25°C
0.0205
4-hydroquinone
mutant E140G, high efficiency site, pH 3.5, 25°C
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
0.04
4-hydroquinone
mutant P141G, high efficiency site, pH 3.5, 25°C
0.38
4-hydroquinone
mutant F142G, low efficiency site, pH 3.5, 25°C
0.41
4-hydroquinone
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
0.42
4-hydroquinone
mutant K176D, low efficiency site, pH 3.5, 25°C
0.618
4-hydroquinone
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
0.716
4-hydroquinone
wild-type, low efficiency site, pH 3.5, 25°C
0.836
4-hydroquinone
mutant E140G, low efficiency site, pH 3.5, 25°C
0.884
4-hydroquinone
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
1.02
4-hydroquinone
mutant K215Q, low efficiency site, pH 3.5, 25°C
1.026
4-hydroquinone
mutant P76G, low efficiency site, pH 3.5, 25°C
1.05
4-hydroquinone
mutant K176G, low efficiency site, pH 3.5, 25°C
1.112
4-hydroquinone
mutant K215G, low efficiency site, pH 3.5, 25°C
1.114
4-hydroquinone
mutant P141G, low efficiency site, pH 3.5, 25°C
1.18
4-hydroquinone
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
2.24
4-hydroquinone
mutant W164S, low efficiency site, pH 3.5, 25°C
0.034
catechol
mutant E140G/W164S/K176G, pH 3.5, 25°C
1.86
catechol
mutant K176D, pH 3.5, 25°C
2.63
catechol
mutant E140G/K176G, pH 3.5, 25°C
3.68
catechol
mutant K176G, pH 3.5, 25°C
4.04
catechol
mutant K215Q, pH 3.5, 25°C
4.26
catechol
mutant E140G, pH 3.5, 25°C
4.26
catechol
mutant K215G, pH 3.5, 25°C
4.72
catechol
mutant E140G/P141G/K176G, pH 3.5, 25°C
4.79
catechol
mutant P76G, pH 3.5, 25°C
5.04
catechol
wild-type, pH 3.5, 25°C
5.11
catechol
mutant P141G, pH 3.5, 25°C
5.15
catechol
mutant F142G, pH 3.5, 25°C
7.76
catechol
mutant W164S, pH 3.5, 25°C
10.5
catechol
mutant E140G/P141G, pH 3.5, 25°C
1.97
guaiacol
mutant E140G, pH 3.5, 25°C
2.73
guaiacol
mutant E140G/K176G, pH 3.5, 25°C
5.1
guaiacol
mutant E140G/P141G, pH 3.5, 25°C
5.85
guaiacol
mutant E140G/W164S/K176G, pH 3.5, 25°C
6.9
guaiacol
mutant P141G, pH 3.5, 25°C
7.27
guaiacol
mutant K176D, pH 3.5, 25°C
10.3
guaiacol
mutant K215G, pH 3.5, 25°C
10.8
guaiacol
mutant F142G, pH 3.5, 25°C
11.1
guaiacol
wild-type, pH 3.5, 25°C
11.6
guaiacol
mutant K215Q, pH 3.5, 25°C
14.2
guaiacol
mutant E140G/P141G/K176G, pH 3.5, 25°C
16.2
guaiacol
mutant K176G, pH 3.5, 25°C
16.3
guaiacol
mutant P76G, pH 3.5, 25°C
39.8
guaiacol
mutant W164S, pH 3.5, 25°C
0.002
H2O2
-
cosubstrate aromatic compound, pH 3.0, isoenzyme PS1
0.003
H2O2
-
cosubstrate aromatic compound, pH 3.0, isoenzyme PS3
0.006
H2O2
-
cosubstrate Mn2+, isoenzyme MP-1, pH 5.0
0.009
H2O2
-
pH 5.0, cosubstrate Mn2+, isoenzyme PS1
0.01
H2O2
-
cosubstrate Mn2+, isoenzyme MP-2, pH 5.0
0.01
H2O2
-
pH 5.0, cosubstrate Mn2+, isoenzyme PS3
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
0.017
methoxyhydroquinone
-
pH 3.0, isoenzyme PS1
0.019
methoxyhydroquinone
-
2.5 - 3
methoxyhydroquinone
-
pH 3.0, isoenzyme PS3
0.012
Mn2+
-
0.015
Mn2+
-
cosubstrate dimethoxyphenol, isoenzyme MP-1, pH 5.0
0.015
Mn2+
-
cosubstrate dimethoxyphenol, isoenzyme MP-2, pH 5.0
0.02
Mn2+
-
cosubstrate H2O2, isoenzyme MP-1, pH 5.0
0.02
Mn2+
-
cosubstrate H2O2, isoenzyme MP-2, pH 5.0
0.045
Mn2+
wild-type, pH 3.5, temperature not specified in the publication
0.045
Mn2+
at pH 5.0 and 25°C
0.048
Mn2+
-
pH 5.0, isoenzyme PS1
0.076
Mn2+
mutant enzyme W164Y/R257A/A260F
0.078
Mn2+
mutant enzyme W164Y
0.11
Mn2+
-
mutant W164S, pH 5.0
0.11
Mn2+
mutant enzyme W164S
0.12
Mn2+
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
0.126
Mn2+
-
mutant W164H, pH 5.0
0.133
Mn2+
mutant enzyme W164H
0.15
Mn2+
mutant enzyme R257A/A260F
0.189
Mn2+
-
wild-tpye, pH 5.0
0.2
Mn2+
-
pH 5.0, isoenzyme PS3
0.218
Mn2+
-
mutant H232F, pH 5.0
0.262
Mn2+
-
mutant P76H, pH 5.0
0.351
Mn2+
-
mutant W164S/P76H, pH 5.0
0.417
Mn2+
25°C, pH 5, mutant A173R
4.91
Mn2+
25°C, pH 5, mutant E40D
4.98
Mn2+
25°C, pH 5, mutant E36D
11.26
Mn2+
25°C, pH 5, mutant E40A
13.84
Mn2+
25°C, pH 5, mutant E36A
16.1
Mn2+
25°C, pH 5, mutant D175A
46.86
Mn2+
25°C, pH 5, mutant E36A/E40A
69.97
Mn2+
25°C, pH 5, mutant E36A/E40A/D175A/P327ter
76.4
Mn2+
25°C, pH 5, mutant E36A/E40A/D175A
0.0013
Reactive Black 5
pH 3.5, 25°C, mutant M247L
0.0014
Reactive Black 5
pH 3.5, 25°C, mutant S158D
0.0019
Reactive Black 5
pH 3.5, 25°C, mutant A260F
0.002
Reactive Black 5
-
pH 3.0, isoenzyme PS1
0.0022
Reactive Black 5
pH 3.5, 25°C, mutant S158E
0.0025
Reactive Black 5
pH 3.5, 25°C, mutant K264A
0.0026
Reactive Black 5
pH 3.5, 25°C, mutant R257K
0.0027
Reactive Black 5
pH 3.5, 25°C, mutant R257L
0.0028
Reactive Black 5
-
wild-tpye, pH 3.5
0.0031
Reactive Black 5
-
mutant P76H, pH 3.5
0.0031
Reactive Black 5
pH 3.5, 25°C, mutant M247F
0.0034
Reactive Black 5
pH 3.5, 25°C, wild-type
0.0034
Reactive Black 5
native recombinant enzyme
0.0036
Reactive Black 5
-
mutant H232F, pH 3.5
0.0048
Reactive Black 5
pH 3.5, 25°C
0.0049
Reactive Black 5
pH 3.5, 25°C, mutant R257A/A260F
0.0049
Reactive Black 5
mutant enzyme R257A/A260F
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
0.007
Reactive Black 5
at pH 3.0 and 25°C
0.2
syringol
-
pH 3.0, isoenzyme PS1
1
syringol
-
pH 3.0, isoenzyme PS3
0.005
vanillylidenacetone
-
presence of Mn2+, isoenzyme MP-1, pH 5.0
0.005
vanillylidenacetone
-
presence of Mn2+, isoenzyme MP-2, pH 5.0
1.65
veratryl alcohol
pH 3.0, 25°C, mutant S158E
2.41
veratryl alcohol
-
mutant P76H, pH 3.0
2.75
veratryl alcohol
-
wild-tpye, pH 3.0
3
veratryl alcohol
-
absence of Mn2+, isoenzyme MP-2, pH 3.0
3.5
veratryl alcohol
-
absence of Mn2+, isoenzyme MP-1, pH 3.0
3.5
veratryl alcohol
-
pH 3.0, isoenzyme PS1
3.58
veratryl alcohol
-
mutant H232F, pH 3.0
4.09
veratryl alcohol
pH 3.0, 25°C
4.11
veratryl alcohol
pH 3.0, 25°C, mutant M247F
4.13
veratryl alcohol
pH 3.0, 25°C, wild-type
4.13
veratryl alcohol
native recombinant enzyme
5.11
veratryl alcohol
pH 3.0, 25°C, mutant A260F
5.68
veratryl alcohol
pH 3.0, 25°C, mutant K264A
5.96
veratryl alcohol
pH 3.0, 25°C, mutant S158D
6.99
veratryl alcohol
pH 3.0, 25°C, mutant M247L
13.5
veratryl alcohol
pH 3.0, 25°C, mutant R257A/A260F
13.5
veratryl alcohol
pH 3.0, 25°C, mutant R257L
13.5
veratryl alcohol
mutant enzyme R257A/A260F
14.2
veratryl alcohol
pH 3.0, 25°C, mutant R257K
54.7
veratryl alcohol
pH 3.0, 25°C, mutant R257D
additional information
additional information
kinetic parameters for wild-type enzyme and five selected mutant variants with dye substrates, comparisons, overview
-
additional information
additional information
-
kinetic parameters for wild-type enzyme and five selected mutant variants with dye substrates, comparisons, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.7 - 365
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
4.6 - 293
2,6-dimethoxyphenol
47
manganese(II)-substituted polyoxometalate
-
in 0.1 M sodium tartrate, pH 5.0, at 20°C
-
4 - 19
methoxyhydroquinone
4
p-dimethoxybenzene
-
pH 3.0, isoenzyme PS1
0.4 - 11.8
Reactive Black 5
4 - 27.3
veratryl alcohol
0.7
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant M247F
4.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant M247L
5.4
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C
5.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant A260F
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
13.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
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
4.6
2,6-dimethoxyphenol
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
4.8
2,6-dimethoxyphenol
mutant P141G, high efficiency site, pH 3.5, 25°C
5.6
2,6-dimethoxyphenol
wild-type, high efficiency site, pH 3.5, 25°C
6.2
2,6-dimethoxyphenol
mutant P76G, high efficiency site, pH 3.5, 25°C
7.6
2,6-dimethoxyphenol
mutant K215Q, high efficiency site, pH 3.5, 25°C
9.3
2,6-dimethoxyphenol
mutant K176G, high efficiency site, pH 3.5, 25°C
9.5
2,6-dimethoxyphenol
mutant K215G, high efficiency site, pH 3.5, 25°C
9.8
2,6-dimethoxyphenol
mutant F142G, high efficiency site, pH 3.5, 25°C
10
2,6-dimethoxyphenol
mutant E140G, high efficiency site, pH 3.5, 25°C
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
29.8
2,6-dimethoxyphenol
wild-type, low efficiency site, pH 3.5, 25°C
47.6
2,6-dimethoxyphenol
mutant W164S, low efficiency site, pH 3.5, 25°C
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
74.5
2,6-dimethoxyphenol
mutant K215Q, low efficiency site, pH 3.5, 25°C
98
2,6-dimethoxyphenol
wild-type, pH 3.5, temperature not specified in the publication
98
2,6-dimethoxyphenol
at pH 3.0 and 25°C
141
2,6-dimethoxyphenol
mutant P141G, low efficiency site, pH 3.5, 25°C
231.6
2,6-dimethoxyphenol
mutant K176G, low efficiency site, pH 3.5, 25°C
293
2,6-dimethoxyphenol
mutant E140G, low efficiency site, pH 3.5, 25°C
7.2
4-hydroquinone
mutant K215G, high efficiency site, pH 3.5, 25°C
8
4-hydroquinone
mutant K176D, high efficiency site, pH 3.5, 25°C
8
4-hydroquinone
mutant P76G, high efficiency site, pH 3.5, 25°C
9.71
4-hydroquinone
mutant F142G, high efficiency site, pH 3.5, 25°C
10.3
4-hydroquinone
wild-type, high efficiency site, pH 3.5, 25°C
11.4
4-hydroquinone
mutant K215Q, high efficiency site, pH 3.5, 25°C
11.6
4-hydroquinone
mutant K176G, high efficiency site, pH 3.5, 25°C
14.6
4-hydroquinone
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
15.6
4-hydroquinone
mutant P141G, high efficiency site, pH 3.5, 25°C
16.2
4-hydroquinone
mutant E140G, high efficiency site, pH 3.5, 25°C
19.2
4-hydroquinone
mutant F142G, low efficiency site, pH 3.5, 25°C
20
4-hydroquinone
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
20
4-hydroquinone
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
25.2
4-hydroquinone
mutant K176D, low efficiency site, pH 3.5, 25°C
25.8
4-hydroquinone
mutant K215G, low efficiency site, pH 3.5, 25°C
29.9
4-hydroquinone
mutant P76G, low efficiency site, pH 3.5, 25°C
35.1
4-hydroquinone
wild-type, low efficiency site, pH 3.5, 25°C
35.2
4-hydroquinone
mutant K215Q, low efficiency site, pH 3.5, 25°C
65.5
4-hydroquinone
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
70.6
4-hydroquinone
mutant K176G, low efficiency site, pH 3.5, 25°C
72.9
4-hydroquinone
mutant E140G, 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
108
4-hydroquinone
mutant P141G, low efficiency site, pH 3.5, 25°C
8
catechol
mutant W164S, pH 3.5, 25°C
75
catechol
mutant F142G, pH 3.5, 25°C
78
catechol
mutant P141G, pH 3.5, 25°C
80
catechol
mutant K176G, pH 3.5, 25°C
81
catechol
mutant K215Q, pH 3.5, 25°C
85
catechol
mutant K215G, pH 3.5, 25°C
94
catechol
mutant K176D, pH 3.5, 25°C
99
catechol
mutant P76G, pH 3.5, 25°C
105.6
catechol
mutant E140G/P141G, pH 3.5, 25°C
135.7
catechol
mutant E140G/P141G/K176G, pH 3.5, 25°C
164
catechol
mutant E140G, pH 3.5, 25°C
164.8
catechol
mutant E140G/W164S/K176G, pH 3.5, 25°C
185
catechol
wild-type, pH 3.5, 25°C
185.6
catechol
mutant E140G/K176G, pH 3.5, 25°C
9.3
guaiacol
mutant P141G, pH 3.5, 25°C
16.2
guaiacol
mutant K215G, pH 3.5, 25°C
17.5
guaiacol
mutant F142G, pH 3.5, 25°C
22.7
guaiacol
wild-type, pH 3.5, 25°C
23.8
guaiacol
mutant K215Q, pH 3.5, 25°C
26.2
guaiacol
mutant P76G, pH 3.5, 25°C
29.8
guaiacol
mutant K176D, pH 3.5, 25°C
30.6
guaiacol
mutant W164S, pH 3.5, 25°C
33.3
guaiacol
mutant K176G, pH 3.5, 25°C
34.8
guaiacol
mutant E140G, pH 3.5, 25°C
105.6
guaiacol
mutant E140G/P141G, pH 3.5, 25°C
135.7
guaiacol
mutant E140G/P141G/K176G, pH 3.5, 25°C
164.8
guaiacol
mutant E140G/W164S/K176G, pH 3.5, 25°C
185.6
guaiacol
mutant E140G/K176G, pH 3.5, 25°C
135
H2O2
wild-type, pH 3.5, temperature not specified in the publication
490
H2O2
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
4
methoxyhydroquinone
-
pH 3.0, isoenzyme PS1
19
methoxyhydroquinone
-
pH 3.0, isoenzyme PS3
2
Mn2+
25°C, pH 5, mutant E36A/E40A/D175A
2
Mn2+
25°C, pH 5, mutant E36A/E40A/D175A/P327ter
5
Mn2+
25°C, pH 5, mutant E36A/E40A
15
Mn2+
25°C, pH 5, mutant E40A
32
Mn2+
25°C, pH 5, mutant D175A
54
Mn2+
wild-type, pH 3.5, temperature not specified in the publication
54
Mn2+
at pH 5.0 and 25°C
75
Mn2+
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
78
Mn2+
-
pH 5.0, isoenzyme PS3
79
Mn2+
-
pH 5.0, isoenzyme PS1
85
Mn2+
25°C, pH 5, mutant E36A
103
Mn2+
25°C, pH 5, mutant E36D
145
Mn2+
25°C, pH 5, mutant E40D
164
Mn2+
mutant enzyme W164Y
207
Mn2+
-
mutant W164S, pH 5.0
207
Mn2+
mutant enzyme R257A/A260F
207
Mn2+
mutant enzyme W164S
216
Mn2+
mutant enzyme W164Y/R257A/A260F
247
Mn2+
-
mutant W164S/P76H, pH 5.0
275
Mn2+
native recombinant enzyme
291
Mn2+
-
mutant P76H, pH 5.0
298
Mn2+
-
wild-type, pH 5.0
298
Mn2+
-
0.000083 1/sec/mg, incubates 30 min at 37°C, pH 9.0, spectrophotometrically measured at 415 nm
308
Mn2+
-
mutant H232F, pH 5.0
320
Mn2+
-
mutant W164H, pH 5.0
328
Mn2+
mutant enzyme W164H
467
Mn2+
25°C, pH 5, mutant A173R
0.4
Reactive Black 5
pH 3.5, 25°C, mutant M247F
2.3
Reactive Black 5
pH 3.5, 25°C, mutant R257K
2.7
Reactive Black 5
pH 3.5, 25°C
3.1
Reactive Black 5
pH 3.5, 25°C, mutant A260F
3.3
Reactive Black 5
pH 3.5, 25°C, mutant M247L
4.2
Reactive Black 5
pH 3.5, 25°C, mutant K264A
4.6
Reactive Black 5
pH 3.5, 25°C, mutant S158E
4.7
Reactive Black 5
-
mutant H232F, pH 3.5
4.9
Reactive Black 5
pH 3.5, 25°C, mutant S158D
5
Reactive Black 5
-
pH 3.0, isoenzyme PS1
5
Reactive Black 5
-
wild-type, pH 3.5
5
Reactive Black 5
-
0.0 M NaCl, 55.6 IgG relative content, 5.5% relative DNase activity
5.5
Reactive Black 5
pH 3.5, 25°C, wild-type
5.5
Reactive Black 5
native recombinant enzyme
6
Reactive Black 5
-
mutant P76H, pH 3.5
9.1
Reactive Black 5
pH 3.5, 25°C, mutant R257A/A260F
9.1
Reactive Black 5
mutant enzyme R257A/A260F
10.6
Reactive Black 5
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
11.6
Reactive Black 5
pH 3.5, 25°C, mutant R257L
11.8
Reactive Black 5
wild-type, pH 3.5, temperature not specified in the publication
11.8
Reactive Black 5
at pH 3.0 and 25°C
3
syringol
-
pH 3.0, isoenzyme PS3
6
syringol
-
pH 3.0, isoenzyme PS1
4
veratryl alcohol
-
pH 3.0, isoenzyme PS1
4.3
veratryl alcohol
pH 3.0, 25°C, mutant M247F
5
veratryl alcohol
pH 3.0, 25°C, mutant M247L
6.4
veratryl alcohol
pH 3.0, 25°C
7.5
veratryl alcohol
pH 3.0, 25°C, mutant A260F
8
veratryl alcohol
-
wild-type, pH 3.0
8
veratryl alcohol
-
H196A mutant, 30°C, pH 6.5
8.2
veratryl alcohol
pH 3.0, 25°C, mutant K264A
9.5
veratryl alcohol
pH 3.0, 25°C, wild-type
9.5
veratryl alcohol
native recombinant enzyme
9.6
veratryl alcohol
pH 3.0, 25°C, mutant S158D
9.6
veratryl alcohol
pH 3.0, 25°C, mutant S158E
10.9
veratryl alcohol
pH 3.0, 25°C, mutant R257K
11
veratryl alcohol
-
mutant P76H, pH 3.0
14
veratryl alcohol
-
mutant H232F, pH 3.0
17.9
veratryl alcohol
pH 3.0, 25°C, mutant R257A/A260F
17.9
veratryl alcohol
mutant enzyme R257A/A260F
19.6
veratryl alcohol
pH 3.0, 25°C, mutant R257D
27.3
veratryl alcohol
pH 3.0, 25°C, mutant R257L
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1 - 6480
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
1.3 - 283
2,6-dimethoxyphenol
8.9 - 1600
4-hydroquinone
7.36
manganese(II)-substituted polyoxometalate
-
in 0.1 M sodium tartrate, pH 5.0, at 20°C
-
1600 - 1900
Reactive Black 5
1.3 - 2.3
veratryl alcohol
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
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
1.3
2,6-dimethoxyphenol
mutant W164S, low efficiency site, pH 3.5, 25°C
1.9
2,6-dimethoxyphenol
mutant P141G, low efficiency site, pH 3.5, 25°C
2.8
2,6-dimethoxyphenol
wild-type, low efficiency site, pH 3.5, 25°C
2.9
2,6-dimethoxyphenol
mutant K215Q, low efficiency site, pH 3.5, 25°C
3.1
2,6-dimethoxyphenol
wild-type, pH 3.5, temperature not specified in the publication
3.1
2,6-dimethoxyphenol
at pH 3.0 and 25°C
3.8
2,6-dimethoxyphenol
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
6.4
2,6-dimethoxyphenol
mutant K176G, low efficiency site, pH 3.5, 25°C
7.8
2,6-dimethoxyphenol
mutant E140G, 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
31
2,6-dimethoxyphenol
mutant P141G, high efficiency site, pH 3.5, 25°C
44.6
2,6-dimethoxyphenol
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
71
2,6-dimethoxyphenol
wild-type, high efficiency site, pH 3.5, 25°C
91.3
2,6-dimethoxyphenol
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
93
2,6-dimethoxyphenol
mutant K176G, high efficiency site, pH 3.5, 25°C
97
2,6-dimethoxyphenol
mutant K215Q, high efficiency site, pH 3.5, 25°C
152
2,6-dimethoxyphenol
mutant F142G, high efficiency site, pH 3.5, 25°C
153
2,6-dimethoxyphenol
mutant E140G, high efficiency site, pH 3.5, 25°C
165
2,6-dimethoxyphenol
mutant K215G, high efficiency site, pH 3.5, 25°C
171
2,6-dimethoxyphenol
mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C
171
2,6-dimethoxyphenol
mutant P76G, high efficiency site, pH 3.5, 25°C
283
2,6-dimethoxyphenol
mutant K176D, high efficiency site, pH 3.5, 25°C
8.9
4-hydroquinone
mutant W164S, low efficiency site, pH 3.5, 25°C
25.3
4-hydroquinone
mutant K215G, low efficiency site, pH 3.5, 25°C
29.2
4-hydroquinone
mutant P76G, low efficiency site, pH 3.5, 25°C
31.4
4-hydroquinone
mutant K215Q, low efficiency site, pH 3.5, 25°C
49.1
4-hydroquinone
wild-type, low efficiency site, pH 3.5, 25°C
50.6
4-hydroquinone
mutant F142G, low efficiency site, pH 3.5, 25°C
55.6
4-hydroquinone
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
59.9
4-hydroquinone
mutant K176D, low efficiency site, pH 3.5, 25°C
67
4-hydroquinone
mutant K176G, low efficiency site, pH 3.5, 25°C
87.2
4-hydroquinone
mutant E140G, low efficiency site, pH 3.5, 25°C
96.8
4-hydroquinone
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
97
4-hydroquinone
mutant P141G, 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
387
4-hydroquinone
mutant 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
600
4-hydroquinone
mutant K215G, high efficiency site, pH 3.5, 25°C
616
4-hydroquinone
mutant K176G, high efficiency site, pH 3.5, 25°C
656
4-hydroquinone
wild-type, high efficiency site, pH 3.5, 25°C
659
4-hydroquinone
mutant K215Q, high efficiency site, pH 3.5, 25°C
789
4-hydroquinone
mutant E140G, high efficiency site, pH 3.5, 25°C
800
4-hydroquinone
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
800
4-hydroquinone
mutant P76G, high efficiency site, pH 3.5, 25°C
1600
4-hydroquinone
mutant F142G, high efficiency site, pH 3.5, 25°C
1
catechol
mutant W164S, pH 3.5, 25°C
10.1
catechol
mutant E140G/P141G, pH 3.5, 25°C
14.5
catechol
mutant F142G, pH 3.5, 25°C
15
catechol
mutant P141G, pH 3.5, 25°C
19.9
catechol
mutant K215G, pH 3.5, 25°C
20.1
catechol
mutant K215Q, pH 3.5, 25°C
20.7
catechol
mutant P76G, pH 3.5, 25°C
21.6
catechol
mutant K176G, pH 3.5, 25°C
28.8
catechol
mutant E140G/P141G/K176G, pH 3.5, 25°C
36.7
catechol
wild-type, pH 3.5, 25°C
38.4
catechol
mutant E140G, pH 3.5, 25°C
48.4
catechol
mutant E140G/W164S/K176G, pH 3.5, 25°C
50.9
catechol
mutant K176D, pH 3.5, 25°C
70.7
catechol
mutant E140G/K176G, pH 3.5, 25°C
0.6
guaiacol
mutant E140G/P141G, pH 3.5, 25°C
0.7
guaiacol
mutant W164S, pH 3.5, 25°C
1.3
guaiacol
mutant P141G, pH 3.5, 25°C
1.4
guaiacol
mutant E140G/P141G/K176G, pH 3.5, 25°C
1.6
guaiacol
mutant F142G, pH 3.5, 25°C
1.6
guaiacol
mutant K215G, pH 3.5, 25°C
1.6
guaiacol
mutant P76G, pH 3.5, 25°C
2
guaiacol
mutant K176G, pH 3.5, 25°C
2
guaiacol
mutant K215Q, pH 3.5, 25°C
2
guaiacol
wild-type, pH 3.5, 25°C
4.2
guaiacol
mutant K176D, pH 3.5, 25°C
9.3
guaiacol
mutant E140G/W164S/K176G, pH 3.5, 25°C
17.1
guaiacol
mutant E140G/K176G, pH 3.5, 25°C
17.6
guaiacol
mutant E140G, 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
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
1190
Mn2+
at pH 5.0 and 25°C
1380
Mn2+
mutant enzyme R257A/A260F
1520
Mn2+
native recombinant enzyme
1900
Mn2+
mutant enzyme W164S
2110
Mn2+
mutant enzyme W164Y
2470
Mn2+
mutant enzyme W164H
2850
Mn2+
mutant enzyme W164Y/R257A/A260F
1600
Reactive Black 5
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
1610
Reactive Black 5
native recombinant enzyme
1670
Reactive Black 5
wild-type, pH 3.5, temperature not specified in the publication
1670
Reactive Black 5
at pH 3.0 and 25°C
1900
Reactive Black 5
mutant enzyme R257A/A260F
1.3
veratryl alcohol
mutant enzyme R257A/A260F
2.3
veratryl alcohol
native recombinant enzyme
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V160I/A260G
site-directed mutagenesis, the mutant MV4 shows increased dye degradation activity compared to the wild-type enzymen with Evans blue, Amido black 10B, and especially with Guinea green B
V160I/A260V
site-directed mutagenesis, the mutant MV5 shows increased dye degradation activity compared to the wild-type enzyme with Evans blue, and Guinea green B, but not with Amido black 10B
V160L/A260S
site-directed mutagenesis, the mutant MV1 shows increased dye degradation activity compared to the wild-type enzyme
V160Y
site-directed mutagenesis, the mutant MV2 shows increased dye degradation activity compared to the wild-type enzyme with Evans blue and Amido black 10B, but not with Guinea green B
V160Y/A260R
site-directed mutagenesis, the mutant MV3 shows increased dye degradation activity compared to the wild-type enzyme with Evans blue and Amido black 10B, but not with Guinea green B
A173R
kcat/KM for Mn2+ is 1.4fold lower than wild-type value, kcat/Km for veratryl alcohol is 1.4fold higher than wild-type value, kcat/Km for Reactive Black 5 is 1.3fold higher than wild-type value
A260F
kinetics similar to wild-type
A260F/R257A
site-directed mutagenesis
D175A
kcat/KM for Mn2+ is 842fold lower than wild-type value, kcat/Km for veratryl alcohol is3.2 fold higher than wild-type value, kcat/Km for Reactive Black 5 is 1.8fold higher than wild-type value
D22N/T45A/E83G/I103V/G107S/P141A/F186L
site-directed mutagenesis
E140G
substitution of bulky residue at the main heme access channel, kinetic analysis
E140G/K176G
variant attains catalytic efficiencies for oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) at the heme channel similar to those of the exposed tryptophan site W164
E140G/P141G
substitution of bulky residue at the main heme access channel, kinetic analysis
E140G/P141G/K176G
variant attains catalytic efficiencies for oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) at the heme channel similar to those of the exposed tryptophan site W164
E140G/P182S/Q229P
site-directed mutagenesis, the mutant BB-8 is active over an enhanced pH range compared to wild-type and displays strong hyperactivation after incubation at alkaline pH with a 3fold increase in activity, The active pH range for mutant BB-8 is expanded considerably for several substrates, including ABTS, sinapic acid and guaiacol. Consequently, BB-8 is active in the acid range (pH 3-4) and remarkably, in the pH interval from 5 to 9 in which the activity of the parental VP is negligible. The kinetic parameters measured for ABTS reveals enhanced catalytic efficiency at acid pH as result of increased affinity, which permits BB-8 to remain active at basic pHs. This effect is mostly attributed to the E140G mutation that enables the mutant to work with similar catalytic efficiency at pH 6 as the parental type at pH 3.5, due to the widening of the heme channel. Whilst the activity against Mn2+ is diminished due to the P182S mutation introduced close to this catalytic site, this mutation offers the first experimental insight into the role of the Mn2+ site for the direct (non-mediated) oxidation of ABTS at neutral/basic pH
E140G/W164S/K176G
variant attains catalytic efficiencies for oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) at the heme channel similar to those of the exposed tryptophan site W164
E36A
kcat/KM for Mn2+ is 258fold lower than wild-type value, kcat/Km for veratryl alcohol is identical to wild-type value, kcat/Km for Reactive Black 5 is 1.2fold higher than wild-type value
E36A/E40A
kcat/KM for Mn2+ is 16000fold lower than wild-type value, kcat/Km for veratryl alcohol is 1.3fold higher than wild-type value, kcat/Km for Reactive Black 5 is 1.1fold higher than wild-type value
E36A/E40A/D175A
kcat for Mn2+ is 149fold lower than wild-type value, kcat/Km for veratryl alcohol is nearly identical to wild-type value, kcat/Km for Reactive Black 5 is 2fold higher than wild-type value
E36A/E40A/D175A/P327ter
kcat for Mn2+ is 149fold lower than wild-type value, kcat/Km for veratryl alcohol is 1.6fold lower than wild-type value, kcat/Km for Reactive Black 5 is 2.4fold higher than wild-type value
E36D
kcat/KM for Mn2+ is 77fold lower than wild-type value, kcat/Km for veratryl alcohol is 1.3fold higher than wild-type value, kcat/Km for Reactive Black 5 is 3.5fold higher than wild-type value
E37K/H39R/V160A/T184M/Q202L/D213A/G330R
site-directed mutagenesis of enzyme mutant E37K/V160A/T184M/Q202L introducing three additional stabilizing point mutations, the final mutant (2-1B) shows an overall enhancement of 8°C in kinetic thermostability compared to wild-type enzyme, the specific activity increases 2.5fold, and the expression rate is enhanced by 52 fold. The thermostability mutant 2-1B displays remarkable stability at alkaline pH (with a residual activity above 60% at pH 9 after 120 h of incubation), which is rather unusual in fungal peroxidases. Although 2-1B is stable at alkaline conditions, there is hardly any activity at its three catalytic sites at basic pH
E40A
kcat/KM for Mn2+ is 1231fold lower than wild-type value, kcat/Km for veratryl alcohol is 1.2fold lower than wild-type value, kcat/Km for Reactive Black 5 is nearly identical to wild-type value
E40D
kcat/KM for Mn2+ is 54fold lower than wild-type value, kcat/Km for veratryl alcohol is 1.3fold lower than wild-type value, kcat/Km for Reactive Black 5 is 2.4fold higher than wild-type value
F142G
substitution of bulky residue at the main heme access channel, kinetic analysis
H232F
-
not involved in long-range electron transfer
K176D
substitution of bulky residue at the main heme access channel, kinetic analysis
K176G
substitution of bulky residue at the main heme access channel, kinetic analysis
K215G
substitution of bulky residue at the main heme access channel, kinetic analysis
K215Q
substitution of bulky residue at the main heme access channel, kinetic analysis
K264A
kinetics similar to wild-type
M247F
92% decrease in efficiency for oxidizing Reactive Black 5
M247L
kinetics similar to wild-type
N11D/G35K/E40K/T45A/S86R/P141A/F186L/T323I
site-directed mutagenesis
N256D/R257D/A260F
unstable, complete loss of activity
P141G
substitution of bulky residue at the main heme access channel, kinetic analysis
P76G
substitution of bulky residue at the main heme access channel, kinetic analysis
P76H
-
not involved in long-range electron transfer
R257K
65% decrease in efficiency for oxidizing veratryl alcohol
R257L
3-fold increase in Km value for veratryl alcohol
S158D
kinetics similar to wild-type
S158E
kinetics similar to wild-type
S158E/R257D
unstable, complete loss of activity
W164S/P76H
-
no enzymic activity with veratryl alcohol or Reactive Black 5
W164X
site-directed mutagenesis, no activity at the catalytic Trp164 at basic pH due to the fact that the reduction potential of the Trp164 radical decreases as the pH increases, hindering the oxidation of high-redox potential substrates at neutral/basic pH. The long-range electron transfer pathway from Trp164 to the heme is permanently cancelled out at pHs above pH 5.0, thereby diverting the oxidative route for the oxidation of low-redox potential substrates to the other two catalytic sites at the time that the oxidation of high-redox potential compounds is supressed
W164Y
site-directed mutagenesis, substitution of Trp-164 by a histidine, serine, or tyrosine residues causes a complete loss of activity on veratryl alcohol and Reactive Black 5
W164Y/R257A/A260F
site-directed mutagenesis, substitution of Trp-164 by a histidine, serine, or tyrosine residues causes a complete loss of activity on veratryl alcohol and Reactive Black 5
E37K/V160A/T184M/Q202L
mutant obtained by directed evolution, increase in activity and temperature stability
E37K/V160A/T184M/Q202L
site-directed mutagenesis, the secretion of the mutant enzyme from recombinant Saccharomyces cerevisiae improves 129fold compared to wild-type, yielding 22 mg/l of active, soluble and stable enzyme, overexpression in Pichia pastoris, the enzyme is secreted
R257A/A260F
site-directed mutagenesis
R257A/A260F
43% decrease in efficiency for oxidizing veratryl alcohol
R257D
83% decrease in efficiency for oxidizing veratryl alcohol
R257D
versatile peroxidase activity on Reactive Black 5 is eliminated by the R257D mutation
W164H
-
no enzymic activity with veratryl alcohol or Reactive Black 5
W164H
site-directed mutagenesis, substitution of Trp-164 by a histidine, serine, or tyrosine residues causes a complete loss of activity on veratryl alcohol and Reactive Black 5
W164S
complete loss of activity
W164S
-
no enzymic activity with veratryl alcohol or Reactive Black 5
W164S
site-directed mutagenesis, substitution of Trp-164 by a histidine, serine, or tyrosine residues causes a complete loss of activity on veratryl alcohol and Reactive Black 5
W164S
loss activity. Residue is responsible for high redox potential substrate oxidation
additional information
improvement of degradation of azo dyes by versatile peroxidase through saturation mutagenesis and application in form of VP-coated yeast cell walls. Via saturation mutagenesis, two amino acids in the catalytic tryptophan environment of the enzyme are altered (V160 and A260). Library screening with three azo dyes reveals that these two positions have a significant influence on substrate specificity. Enzyme variants with up to 16fold higher catalytic efficiency for different azo dyes are isolated and sequenced. Immobilization of versatile peroxidase on the surface of yeast cells in purified cell wall fragments after lysis, the enzyme VP embedded in the cell wall retains about 70 % of its initial activity after 10 cycles of dye degradation each lasting 12 h
additional information
-
improvement of degradation of azo dyes by versatile peroxidase through saturation mutagenesis and application in form of VP-coated yeast cell walls. Via saturation mutagenesis, two amino acids in the catalytic tryptophan environment of the enzyme are altered (V160 and A260). Library screening with three azo dyes reveals that these two positions have a significant influence on substrate specificity. Enzyme variants with up to 16fold higher catalytic efficiency for different azo dyes are isolated and sequenced. Immobilization of versatile peroxidase on the surface of yeast cells in purified cell wall fragments after lysis, the enzyme VP embedded in the cell wall retains about 70 % of its initial activity after 10 cycles of dye degradation each lasting 12 h
additional information
an engineered N-terminally truncated variant of mutant E37K/V160A/T184M/Q202L displays similar biochemical properties to those of the non-truncated counterpart in terms of kinetics, stability and spectroscopic features. Additional cycles of evolution raised the melting temperature by 8 degrees and significantly increased the enzyme's stability at alkaline pHs. In addition, the Km for H2O2 is enhanced up to 15fold while the catalytic efficiency is maintained, and there is an improvement in peroxide stability
additional information
-
an engineered N-terminally truncated variant of mutant E37K/V160A/T184M/Q202L displays similar biochemical properties to those of the non-truncated counterpart in terms of kinetics, stability and spectroscopic features. Additional cycles of evolution raised the melting temperature by 8 degrees and significantly increased the enzyme's stability at alkaline pHs. In addition, the Km for H2O2 is enhanced up to 15fold while the catalytic efficiency is maintained, and there is an improvement in peroxide stability
additional information
due to its broad substrate scope and minor requirements, versatile peroxidase is an extremely attractive blueprint to be designed by the directed evolution tool-box, directed evolution for functional expression in Saccharomyces cerevisiae, directed evolution for activity at alkaline pH, overview
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Martinez, M.J.; Ruiz-Duenas, F.J.; Guillen, F.; Martinez, A.T.
Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii
Eur. J. Biochem.
237
424-432
1996
Pleurotus eryngii
brenda
Ruiz-Duenas, F.J.; Guillen, F.; Camarero, S.; Perez-Boada, M.; Martinez, M.J.; Martinez, A.T.
Regulation of peroxidase transcript levels in liquid cultures of the ligninolytic fungus Pleurotus eryngii
Appl. Environ. Microbiol.
65
4458-4463
1999
Pleurotus eryngii
brenda
Ruiz-Duenas, F.J.; Martinez, M.J.; Martinez, A.T.
Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn(2+) and different aromatic substrates
Appl. Environ. Microbiol.
65
4705-4707
1999
Pleurotus eryngii (O94753)
brenda
Ruiz-Duenas, F.J.; Camarero, S.; Perez-Boada, M.; Martinez, M.J.; Martinez, A.T.
A new versatile peroxidase from Pleurotus
Biochem. Soc. Trans.
29
116-122
2001
Pleurotus eryngii
brenda
Gomez-Toribio, V.; Martinez, A.T.; Martinez, M.J.; Guillen, F.
Oxidation of hydroquinones by the versatile ligninolytic peroxidase from Pleurotus eryngii. H2O2 generation and the influence of Mn2+
Eur. J. Biochem.
268
4787-4793
2001
Pleurotus eryngii
brenda
Camarero, S.; Ruiz-Duenas, F.J.; Sarkar, S.; Martinez, M.J.; Martinez, A.T.
The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases
FEMS Microbiol. Lett.
191
37-43
2000
Pleurotus eryngii (Q9UVP6), Pleurotus eryngii
brenda
Camarero, S.; Sarkar, S.; Ruiz-Duenas, F.J.; Martinez, M.J.; Martinez, A.T.
Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites
J. Biol. Chem.
274
10324-10330
1999
Pleurotus eryngii
brenda
Pogni, R.; Baratto, M.C.; Teutloff, C.; Giansanti, S.; Ruiz-Duenas, F.J.; Choinowski, T.; Piontek, K.; Martinez, A.T.; Lendzian, F.; Basosi, R.
A tryptophan neutral radical in the oxidized state of versatile peroxidase from Pleurotus eryngii: a combined multifrequency EPR and density functional theory study
J. Biol. Chem.
281
9517-9526
2006
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Banci, L.; Camarero, S.; Martinez, A.T.; Martinez, M.J.; Perez-Boada, M.; Pierattelli, R.; Ruiz-Duenas, F.J.
NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii
J. Biol. Inorg. Chem.
8
751-760
2003
Pleurotus eryngii
brenda
Perez-Boada, M.; Ruiz-Duenas, F.J.; Pogni, R.; Basosi, R.; Choinowski, T.; Martinez, M.J.; Piontek, K.; Martinez, A.T.
Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways
J. Mol. Biol.
354
385-402
2005
Pleurotus eryngii
brenda
Ruiz-Duenas, F.J.; Morales, M.; Perez-Boada, M.; Choinowski, T.; Martinez, M.J.; Piontek, K.; Martinez, A.T.
Manganese oxidation site in Pleurotus eryngii versatile peroxidase: a site-directed mutagenesis, kinetic, and crystallographic study
Biochemistry
46
66-77
2007
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Ruiz-Duenas, F.J.; Morales, M.; Mate, M.J.; Romero, A.; Martinez, M.J.; Smith, A.T.; Martinez, A.T.
Site-directed mutagenesis of the catalytic tryptophan environment in Pleurotus eryngii versatile peroxidase
Biochemistry
47
1685-1695
2008
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Eibes, G.M.; Lu-Chau, T.A.; Ruiz-Duenas, F.J.; Feijoo, G.; Martinez, M.J.; Martinez, A.T.; Lema, J.M.
Effect of culture temperature on the heterologous expression of Pleurotus eryngii versatile peroxidase in Aspergillus hosts
Bioprocess Biosyst. Eng.
32
129-134
2009
Pleurotus eryngii
brenda
Ruiz-Duenas, F.J.; Pogni, R.; Morales, M.; Giansanti, S.; Mate, M.J.; Romero, A.; Martinez, M.J.; Basosi, R.; Martinez, A.T.
Protein radicals in fungal versatile peroxidase: catalytic tryptophan radical in both compound I and compound II and studies on W164Y, W164H, and W164S variants
J. Biol. Chem.
284
7986-7994
2009
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Ruiz-Duenas, F.J.; Morales, M.; Garcia, E.; Miki, Y.; Martinez, M.J.; Martinez, A.T.
Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases
J. Exp. Bot.
60
441-452
2009
Pleurotus eryngii (O94753)
brenda
Marques, G.; Gamelas, J.A.; Ruiz-Duenas, F.J.; del Rio, J.C.; Evtuguin, D.V.; Martinez, A.T.; Gutierrez, A.
Delignification of eucalypt kraft pulp with manganese-substituted polyoxometalate assisted by fungal versatile peroxidase
Biores. Technol.
101
5935-5940
2010
Pleurotus eryngii
brenda
Garcia-Ruiz, E.; Gonzalez-Perez, D.; Ruiz-Duenas, F.J.; Martinez, A.T.; Alcalde, M.
Directed evolution of a temperature-, peroxide- and alkaline pH-tolerant versatile peroxidase
Biochem. J.
441
487-498
2012
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Bao, X.; Liu, A.; Lu, X.; Li, J.J.
Direct over-expression, characterization and H2O2 stability study of active Pleurotus eryngii versatile peroxidase in Escherichia coli
Biotechnol. Lett.
34
1537-1543
2012
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Morales, M.; Mate, M.J.; Romero, A.; Martinez, M.J.; Martinez, A.T.; Ruiz-Duenas, F.J.
Two oxidation sites for low redox potential substrates: a directed mutagenesis, kinetic, and crystallographic study on Pleurotus eryngii versatile peroxidase
J. Biol. Chem.
287
41053-41067
2012
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Gonzalez-Perez, D.; Garcia-Ruiz, E.; Ruiz-Duenas, F.; Martinez, A.; Alcalde, M.
Structural determinants of oxidative stabilization in an evolved versatile peroxidase
ACS Catal.
4
3891-3901
2014
Pleurotus eryngii (O94753)
-
brenda
Ravichandran, A.; Sridhar, M.
Insights into the mechanism of lignocellulose degradation by versatile peroxidases
Curr. Sci.
113
35-42
2017
Bjerkandera adusta, Pleurotus eryngii, Pleurotus ostreatus, Bjerkandera fumosa
-
brenda
Saez-Jimenez, V.; Fernandez-Fueyo, E.; Medrano, F.J.; Romero, A.; Martinez, A.T.; Ruiz-Duenas, F.J.
Improving the pH-stability of versatile peroxidase by comparative structural analysis with a naturally-stable manganese peroxidase
PLoS ONE
10
e0140984
2015
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Palma, C.; Lloret, L.; Sepulveda, L.; Contreras, E.
Production of versatile peroxidase from Pleurotus eryngii by solid-state fermentation using agricultural residues and evaluation of its catalytic properties
Prep. Biochem. Biotechnol.
46
200-207
2016
Pleurotus eryngii
brenda
Gonzalez-Perez, D.; Alcalde, M.
The making of versatile peroxidase by directed evolution
Biocatal. Biotransform.
36
1-11
2018
Pleurotus eryngii (O94753)
-
brenda
Durdic, K.I.; Ostafe, R.; Durdevic Delmas, A.; Popovic, N.; Schillberg, S.; Fischer, R.; Prodanovic, R.
Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls
Enzyme Microb. Technol.
136
109509
2020
Pleurotus eryngii (Q9UVP6), Pleurotus eryngii
brenda