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all enzymes1.11.1.13: manganese peroxidase
This is an abbreviated version!
For detailed information about manganese peroxidase, go to the full flat file.
Word Map on EC 1.11.1.13
-
1.11.1.13
-
lignin
-
laccase
-
fungus
-
phanerochaete
-
ligninolytic
-
chrysosporium
-
white-rot
-
peroxidases
-
decolor
-
basidiomycete
-
pleurotus
-
trametes
-
versicolor
-
lignin-degrading
-
veratryl
-
ostreatus
-
straw
-
bjerkandera
-
mniii
-
delignification
-
sawdust
-
ceriporiopsis
-
kraft
-
2,6-dimethoxyphenol
-
subvermispora
-
lentinula
-
adusta
-
phlebia
-
eryngii
-
remazol
-
sordida
-
irpex
-
lignocellulolytic
-
lignin-modifying
-
lacteus
-
non-phenolic
-
tigrinus
-
wood-rotting
-
biotreatment
-
nutrition
-
ligninase
-
decolourisation
-
degradation
-
dye-decolorizing
-
sajor-caju
-
environmental protection
-
mnso4
-
synthesis
-
low-nitrogen
-
1-hydroxybenzotriazole
-
paper production
-
biotechnology
-
biobleaching
-
industry
-
delignified
-
coriolus
-
biosorption
-
biofuel production
- 1.11.1.13
- lignin
- laccase
- fungus
- phanerochaete
-
ligninolytic
- chrysosporium
-
white-rot
- peroxidases
-
decolor
-
basidiomycete
- pleurotus
- trametes
- versicolor
-
lignin-degrading
-
veratryl
- ostreatus
- straw
- bjerkandera
-
mniii
-
delignification
- sawdust
-
ceriporiopsis
-
kraft
- 2,6-dimethoxyphenol
- subvermispora
- lentinula
- adusta
- phlebia
- eryngii
-
remazol
- sordida
- irpex
-
lignocellulolytic
-
lignin-modifying
- lacteus
-
non-phenolic
- tigrinus
-
wood-rotting
-
biotreatment
- nutrition
-
ligninase
-
decolourisation
- degradation
-
dye-decolorizing
- sajor-caju
- environmental protection
- mnso4
- synthesis
-
low-nitrogen
- 1-hydroxybenzotriazole
- paper production
- biotechnology
-
biobleaching
- industry
-
delignified
-
coriolus
-
biosorption
- biofuel production
Reaction
2 Mn(II)
+
2 H+
+
Synonyms
hybrid Mn-peroxidase, L-MnP, LeMnP2, manganese peroxidase, manganese-dependent peroxidase, Mn-dependent (NADH-oxidizing) peroxidase, Mn2+: hydrogen peroxide oxidoreductase, Mn2+:hydrogen peroxide oxidoreductase, MnP, MnP 1, MnP II, MnP-GY, MnP-PGY, mnp1, MnP2, MnP3, MnP6, MP, multifunctional manganese peroxidase, Nf b19 MNP2, peroxidase, manganese, peroxidase-M2
ECTree
1.11.1.13 manganese peroxidaseAdvanced search results
results (
results (
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in table
81
29
230
14
13
14
272
48
120
Substrates Products
Substrates Products on EC 1.11.1.13 - manganese peroxidase
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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
2,2'-azino-bis(3-ethylbenzothiazoline)-6-sulphonate + H2O2
?
-
reaction with and without Mn2+
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid + H2O2 + Mn2+
?
-
-
-
-
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
benzo[a]pyrene + ?
?
-
key enzyme in degradation of benzo[a]pyrene and other polycyclic aromatic hydrocarbons
-
-
?
benzo[a]pyrene + ?
benzo[a]pyrene-1,6-quinone + ?
-
oxidation in presence of Tween 80
-
-
?
Co2+ + H+ + H2O2
Co3+ + H2O
-
reduction of enzyme compound II, oxidation at 2% the rate of Mn2+ oxidation
-
?
Mn2+ + di(2-methylpent-2-enyl) sulfide + H+
Mn3+ + 2,4-dimethylthiophene + 2-methyl-2-pentenal + H2O
-
-
-
-
?
veratryl alcohol + H2O2 + Mn2+
?
-
veratryl alcohol oxidation requires the simultaneous presence of H2O2 and Mn2+
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
the kcat value for the reaction is dependent of the Mn(III) chelator molecules malonate, lactate and oxalate, indicating that the enzyme oxidizes chelated Mn(II) to Mn(III)
-
-
?
2 Mn2+ + H2O2 + aflatoxin B1
2 Mn3+ + aflatoxin B1-8,9-dihydrodiol
-
maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol
-
-
?
2 Mn2+ + H2O2 + aflatoxin B1
2 Mn3+ + aflatoxin B1-8,9-dihydrodiol
-
maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol
-
-
?
2 veratryl alcohol + H2O2
2 veratraldehyde + H2O
no substrate of wild-type
-
-
?
2 veratryl alcohol + H2O2
2 veratraldehyde + H2O
no substrate of wild-type
-
-
?
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid) + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonate) + H2O2
?
-
in absence or presence of Mn2+
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonate) + H2O2
?
-
in absence or presence of Mn2+
-
-
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
?
no substrate of wild-type
-
-
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
?
no substrate of wild-type
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
-
-
-
-
?
2,4,6-trichlorophenol + H2O2
?
-
no oxidation in absence of Mn2+
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
reaction in absence or in presence of Mn2+
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
the highest relative activity for 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
the highest relative activity for 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
reaction in absence or in presence of Mn2+
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
the highest relative activity for 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate
-
-
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
-
3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester is the dominant product
-
-
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
-
3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester is the dominant product
-
-
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
-
-
-
-
-
H2O2 + 2,2'-azino-bis(3-ethyl)-benzothiazoline-6-sulfonic acid
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + 2,2'-azino-bis(3-ethyl)-benzothiazoline-6-sulfonic acid
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + 2,6-dimethoxyphenol
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + 2,6-dimethoxyphenol
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + guaiacol
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + guaiacol
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + Poly R-478
?
-
Mn2+ is required for reaction with Poly R-478 with MnP3
-
-
?
H2O2 + Poly R-478
?
-
MnP2 depolymerizes the polymeric azo dye,Poly R-478, regardless of the presence of Mn2+, to complete its catalytic cycle
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
-
product Mn3+ possibly migrates into polymer molecules, such as lignin, nylon and melanin, and initiates nonspecific oxidation, Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes o-phenylenediamine and p-anisidine, Mn3+ oxidizes o-dianisidine, Mn3+ oxidizes amines, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
single Mn2+ binding site in the vicinity of the heme
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes o-phenylenediamine and p-anisidine, Mn3+ oxidizes o-dianisidine, Mn3+ oxidizes amines, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes o-phenylenediamine and p-anisidine, Mn3+ oxidizes o-dianisidine, Mn3+ oxidizes amines, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
chelating organic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes phenolic lignin model compounds
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes phenolic lignin model compounds
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
in presence of Mn2+, H2O2 and glutathione MnP oxidizes by Mn3+ nonphenolic beta-aryl ether lignin model compounds, veratryl alcohol, anisyl alcohol, benzyl alcohol and thiols to thiyl radicals which abstracts a hydrogen from the substrate forming a benzylic radical, mechanism, glutathione can be replaced by dithiothreitol, dithioerythritol or cysteine
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes o-dianisidine
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes methoxy benzenes: 1,2,4-tri-, 1,2,3,5-tetra-, 1,2,4,5-tetra-, pentamethoxybenzene, veratryl alcohol is oxidized by thiyl radicals derived from Mn3+ oxidation of glutathione, not directly by Mn3+
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
oxidation and cleavage of a phenolic lignin model dimer and its products, MnP catalyzes C-alpha-C-beta cleavages, C-alpha-oxidation and alkyl-aryl cleavages of phenolic syringyl type beta-1 lignin structures via Mn3+
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes phenolic lignin model compounds
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes lignin
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes lignin
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes lignin, Mn3+ oxidizes a variety of phenols
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
each catalytic cycle step is irreversible
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillyl alcohol, Mn3+ oxidizes lignin, Mn3+-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction, Mn3+ oxidizes thiols, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines, the diffusible product is Mn3+, Mn3+ oxidizes amines, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
product Mn3+ is a nonspecific oxidant which in turn oxidizes a variety of organic compounds, Mn3+ oxidizes phenolic lignin model compounds
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
Mn3+ complexed to lactate or other alpha-hydroxy acids acts as an obligatory oxidation intermediate in the oxidation of various dyes and lignin model compounds, Mn3+-lactate complex oxidizes all dyes oxidized by the enzyme in presence of Mn2+: NADH, pinacyanol, phenol red and poly B-411, the diffusible product is Mn3+
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
Mn3+ oxidizes a variety of phenols
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
in presence of H2O2 enzyme oxidizes Mn2+ significantly faster than all other substrates, main function of enzyme is oxidation of Mn2+ to Mn3+
Mn3+ complexed to lactate or other alpha-hydroxy acids acts as an obligatory oxidation intermediate in the oxidation of various dyes and lignin model compounds, Mn3+-lactate complex oxidizes all dyes oxidized by the enzyme in presence of Mn2+: NADH, pinacyanol, phenol red and poly B-411, the diffusible product is Mn3+, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
role for Arg-177 in promoting efficient Mn2+ binding and oxidation by MnP
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates, Mn3+ oxidizes lignin
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ complex oxidizes a variety of organic substrates
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes phenolic lignin model compounds
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes phenolic lignin model compounds
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes vanillyl alcohol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes 2,6-dimethoxyphenol, Mn3+ oxidizes o-dianisidine, the diffusible product is Mn3+, Mn3+ oxidizes a variety of phenols
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidation of Mn2+ to Mn3+ at a redox potential of 1.5 V
-
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates, Mn3+ oxidizes phenolic lignin model compounds
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes syringic acid, 4-hydroxy-3-methoxycinnamic acid, isoeugenol, ascorbate, Mn3+ oxidizes vanillyl alcohol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes vanillyl alcohol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes o-dianisidine, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines, Mn3+ oxidizes p-cresol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
free divalent Mn is the substrate, not Mn2+-complexes
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillyl alcohol, Mn3+ oxidizes lignin, Mn3+-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction, Mn3+ oxidizes thiols, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines, the diffusible product is Mn3+, Mn3+ oxidizes amines, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Mn2+ is an obligatory substrate for MnP compound II, whereas compound I formation occurs with Mn2+, p-cresol and organic peroxides, e.g. peracetic acid, m-chloroperoxybenzoic acid and p-nitroperoxybenzoic acid
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines, Mn3+ oxidizes p-cresol, Mn3+ oxidizes amines, Mn3+ oxidizes a variety of phenols, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Mn2+ binds to a common site close to the delta-meso-carbon without blocking the approach of small molecules to the heme edge
Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates, Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Mn3+ complex oxidizes a variety of organic substrates, Mn3+ oxidizes phenolic lignin model compounds, Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates, Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
little or no enzyme activity in absence of Mn2+
Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes phenol red, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers
Mn3+ complex oxidizes a variety of organic substrates, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid, Mn3+ oxidizes 2,6-dimethoxyphenol, Mn3+ oxidizes o-dianisidine, the diffusible product is Mn3+, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
MnP isoenzymes serve different functions in lignin biodegradation, each may have a preferred substrate
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by veratryl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
initial depolymerization of the lignin polymer
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Mn2+ is a component of woody plant tissues
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
Mn3+ is stabilized by chelating agents, malonate is the most effective physiological chelator excreted by the fungus
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
freely diffusible, enzyme-generated Mn(III)-organic-acid complex is an catalyst for the oxidative depolymerization of lignin in wood
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation, the mechanism enables the fungus to oxidize structures within woods which are inaccessible to enzymes
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
-
-
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
in absence of H2O2 it may play a role in fungal peroxide production under ligninolytic conditions
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
little or no enzyme activity in absence of Mn2+
Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes phenol red
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillylacetone
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes curcumin
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
each catalytic cycle step is irreversible
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillyl alcohol, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Mn2+ binds to a common site close to the delta-meso-carbon without blocking the approach of small molecules to the heme edge
Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes phenolic lignin model compounds, in presence of Mn2+, H2O2 and glutathione MnP oxidizes by Mn3+ nonphenolic beta-aryl ether lignin model compounds, veratryl alcohol, anisyl alcohol, benzyl alcohol and thiols to thiyl radicals which abstracts a hydrogen from the substrate forming a benzylic radical, mechanism, glutathione can be replaced by dithiothreitol, dithioerythritol or cysteine, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes lignin
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes lignin, Mn3+ oxidizes a variety of phenols
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates, Mn3+ oxidizes guaiacol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Mn3+ complex oxidizes a variety of organic substrates, Mn3+ oxidizes phenolic lignin model compounds, Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes phenol red, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes several methoxylated and hydroxylated phenolic compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylideneacetone, Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes phenol red, Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
preferential degradation of lignin in wheat straw
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes syringaldazine, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ as the best substrate
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
preferential degradation of lignin in wheat straw
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ as the best substrate
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
-
?
Reactive Black 5 + H2O2
? + H2O
no substrate of wild-type
-
-
?
Reactive Black 5 + H2O2
? + H2O
no substrate of wild-type
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
-
additional information
?
-
-
Mn2+-dependent and Mn2+-independent peroxidase activities, substrates: 2,6-dimethoxyphenol, 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, guaiacol and veratryl alcohol
-
-
-
additional information
?
-
-
enzyme oxidizes 4-aminophenol and hydroquinone
-
-
-
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
-
-
-
additional information
?
-
-
in absence of Mn2+ enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, o-phenylenediamine and phenol red, the former two are stimulated, the latter is inhibited by Mn2+, guaiacol and pyrocatechol are oxidized only in presence of Mn2+
-
-
-
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
-
additional information
?
-
-
catalyzes the oxidation of Mn(II) to Mn(III), which in turn can oxidize phenolic substrates
-
-
-
additional information
?
-
-
no activity with veratryl alcohol
-
-
-
additional information
?
-
-
in absence of Mn2+ enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, o-phenylenediamine and phenol red, the former two are stimulated, the latter is inhibited by Mn2+, guaiacol and pyrocatechol are oxidized only in presence of Mn2+
-
-
-
additional information
?
-
-
Mn2+-dependent and Mn2+-independent peroxidase activities, substrates: 2,6-dimethoxyphenol, 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, guaiacol and veratryl alcohol
-
-
-
additional information
?
-
-
enzyme oxidizes 4-aminophenol and hydroquinone
-
-
-
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
-
additional information
?
-
-
Mn-mediated and Mn-independent activity on phenolic and non-phenolic aromatic substrates
-
-
-
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
-
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
-
-
-
additional information
?
-
-
Mn-mediated and Mn-independent activity on phenolic and non-phenolic aromatic substrates
-
-
-
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
-
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
-
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
-
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
-
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
-
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
-
additional information
?
-
-
no activity with veratryl alcohol
-
-
-
additional information
?
-
-
no oxidation of Fe2+, Cu2+, Zn2+
-
-
-
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
-
additional information
?
-
-
MnP oxidizes polycyclic aromatic hydrocarbons
-
-
-
additional information
?
-
-
MnP oxidizes chlorophenols and arsenic-containing warefare agents
-
-
-
additional information
?
-
-
enzyme oxidizes non-phenolic lignin-related compounds, including veratryl alcohol
-
-
-
additional information
?
-
-
enzyme is able to oxidatively depolymerize both dimeric lignin-model compounds and milled spruce-wood lignin
-
-
-
additional information
?
-
-
protein complex containing MnP, laccase and beta-glucosidase
-
-
-
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
-
enzyme oxidizes 3’,3’,5’,5’-tetramethylbenzidine
-
-
-
additional information
?
-
-
enzyme oxidizes veratryl alcohol and o-tolidine
-
-
-
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
-
-
-
additional information
?
-
-
in presence of H2O2 and Mn2+ the enzyme oxidizes lignin and lignin-model compounds
-
-
-
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
-
-
-
additional information
?
-
-
MnP oxidizes polycyclic aromatic hydrocarbons
-
-
-
additional information
?
-
-
catalytic cycle of enzyme, oxidation states: native enzyme via compound I via compound II to native enzyme, Mn2+ and phenols reduce MnP compound I to compound II, but only Mn2+ is a substrate for MnP compound II, Mn(II)/Mn(III) redox couple enables enzyme to rapidly oxidize terminal phenolic substrates
-
-
-
additional information
?
-
-
catalytic cycle of enzyme, oxidation states: native enzyme via compound I via compound II to native enzyme, Mn2+ and phenols reduce MnP compound I to compound II, but only Mn2+ is a substrate for MnP compound II, Mn(II)/Mn(III) redox couple enables enzyme to rapidly oxidize terminal phenolic substrates
-
-
-
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
-
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
-
additional information
?
-
-
in absence of H2O2 the enzyme shows Mn-dependent oxidase activity against glutathione, dithiothreitol and dihydroxymaleic acid, forming H2O2 at the expense of oxygen
-
-
-
additional information
?
-
-
in absence of H2O2 the enzyme shows Mn-dependent oxidase activity against glutathione, dithiothreitol and dihydroxymaleic acid, forming H2O2 at the expense of oxygen
-
-
-
additional information
?
-
-
primary reaction product of peroxidation with H2O2 is enzyme compound I, formation of compound II from I follows second-order kinetic
-
-
-
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
-
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
-
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
-
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes pinacyanol as most easily oxidized dye at 1.7% of the rate of the Mn2+ oxidation
-
-
-
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
-
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
-
-
-
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
-
-
-
additional information
?
-
-
in presence of H2O2 and Mn2+ the enzyme oxidizes a variety of phenolic compounds, especially vinyl and syringyl side-chain substituted substrates
-
-
-
additional information
?
-
-
in presence of H2O2 and Mn2+ the enzyme oxidizes a variety of phenolic compounds, especially vinyl and syringyl side-chain substituted substrates
-
-
-
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
-
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
-
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
-
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
-
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
-
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
-
additional information
?
-
-
no activity with veratryl alcohol
-
-
-
additional information
?
-
-
catalytic cycle: MnP is oxidized by H2O2 to compound I, Mn2+, ferrocyanide or phenols reduce compound I to compound II, which is reduced to the ferric state by Mn2+ or ferrocyanide, but not by phenols, Mn2+ completes the cycle, substrates are oxidized via delta-meso heme edge of the enzyme, model of the active site
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additional information
?
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large substrates have no ready access to the catalytic center
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additional information
?
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large substrates have no ready access to the catalytic center
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additional information
?
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presence of proximal and distal histidines at the active center
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additional information
?
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Mn2+-dependent oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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additional information
?
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Mn2+-independent oxidase activity on NAD(P)H
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additional information
?
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in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
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additional information
?
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in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
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additional information
?
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in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
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additional information
?
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in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
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additional information
?
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no other metal can substitute Mn2+
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additional information
?
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Mn2+-independent oxidation of small phenolic compounds, such as guaiacol and dimethoxyphenol, rates are greatly reduced compared with the Mn-mediated reaction
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additional information
?
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MnP oxidizes nitroaromatic compounds
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additional information
?
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enzyme oxidizes 2,6-dimethoxyphenol
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additional information
?
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enzyme oxidizes the polymeric dyes poly R-481 and poly B-411
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additional information
?
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in presence of Mn2+ enzyme oxidizes various organic compounds
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additional information
?
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in presence of Mn2+ enzyme oxidizes various organic compounds
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additional information
?
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in presence of Mn2+ enzyme oxidizes various organic compounds
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additional information
?
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in presence of Mn2+ enzyme oxidizes various organic compounds
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additional information
?
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in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+
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additional information
?
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enzyme oxidizes phenol red
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additional information
?
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in presence of Mn2+ enzyme oxidizes various organic compounds
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additional information
?
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in absence of H2O2 the enzyme shows Mn-dependent oxidase activity against glutathione, dithiothreitol and dihydroxymaleic acid, forming H2O2 at the expense of oxygen
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additional information
?
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in presence of H2O2 and Mn2+ the enzyme oxidizes a variety of phenolic compounds, especially vinyl and syringyl side-chain substituted substrates
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additional information
?
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in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
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additional information
?
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in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+
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additional information
?
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catalytic cycle with oxidized intermediates MnP compound I and II
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additional information
?
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large substrates have no ready access to the catalytic center
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additional information
?
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enzyme oxidizes 2,6-dimethoxyphenol
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additional information
?
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presence of proximal and distal histidines at the active center
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additional information
?
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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additional information
?
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catalytic cycle: MnP is oxidized by H2O2 to compound I, Mn2+, ferrocyanide or phenols reduce compound I to compound II, which is reduced to the ferric state by Mn2+ or ferrocyanide, but not by phenols, Mn2+ completes the cycle, substrates are oxidized via delta-meso heme edge of the enzyme, model of the active site
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additional information
?
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enzyme oxidizes ferrocyanide
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additional information
?
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enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
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additional information
?
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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additional information
?
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in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
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additional information
?
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in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
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additional information
?
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no other metal can substitute Mn2+
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additional information
?
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catalytic cycle with oxidized intermediates MnP compound I and II
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additional information
?
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enzyme oxidizes ferrocyanide
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additional information
?
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enzyme oxidizes bromide
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additional information
?
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catalytic cycle with oxidized intermediates MnP compound I and II
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additional information
?
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enzyme oxidizes ferrocyanide
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additional information
?
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catalytic cycle with oxidized intermediates MnP compound I and II
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additional information
?
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Mn2+-independent oxidation of small phenolic compounds, such as guaiacol and dimethoxyphenol, rates are greatly reduced compared with the Mn-mediated reaction
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additional information
?
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catalytic cycle with oxidized intermediates MnP compound I and II
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additional information
?
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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additional information
?
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catalytic cycle with oxidized intermediates MnP compound I and II
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additional information
?
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Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
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additional information
?
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enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
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additional information
?
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no activity with veratryl alcohol
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additional information
?
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no activity with veratryl alcohol
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additional information
?
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MnP oxidizes polycyclic aromatic hydrocarbons
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additional information
?
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poor substrates: benzoate, benzaldehyde or benzyl alcohol
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additional information
?
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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additional information
?
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in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
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additional information
?
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catalytic cycle with oxidized intermediates MnP compound I and II
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additional information
?
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Mn-dependent oxidation of phenols requires superoxide anion and H2O2, phenolic hydroxyl group is essential
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additional information
?
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in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
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additional information
?
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in presence of Mn2+ enzyme oxidizes various organic compounds
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additional information
?
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Phlebia radiata 79 / ATCC 64658
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poor substrates: benzoate, benzaldehyde or benzyl alcohol
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additional information
?
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Phlebia radiata 79 / ATCC 64658
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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additional information
?
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in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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additional information
?
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in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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additional information
?
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Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
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additional information
?
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Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
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additional information
?
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Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
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additional information
?
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Mn2+-independent peroxidase activity against phenolic substrates, e.g. phenol red
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additional information
?
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-
Mn2+-dependent oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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-
-
additional information
?
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-
Mn2+-independent oxidase activity on NAD(P)H
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-
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additional information
?
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Mn2+-independent oxidase activity on NAD(P)H
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additional information
?
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MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
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additional information
?
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in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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-
-
additional information
?
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-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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-
-
additional information
?
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-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
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-
-
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
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-
-
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
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-
-
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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-
-
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
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-
-
additional information
?
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-
Mn2+-independent oxidase activity on NAD(P)H
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-
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additional information
?
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Mn2+-dependent and Mn2+-independent peroxidase activities when tested on the phenolic substrates 2,6-dimethoxyphenol, 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, guaiacol and syringaldazine, more rapid oxidation in presence of Mn2+
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additional information
?
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in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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-
-
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
-
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
-
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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-
-
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
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-
-
additional information
?
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-
Mn2+-independent oxidase activity on NAD(P)H
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additional information
?
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the enzyme efficiently decolorized azo dyes such as Congo Red, Orange G and Orange IV
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additional information
?
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the enzyme efficiently decolorized azo dyes such as Congo Red, Orange G and Orange IV
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additional information
?
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MnP oxidizes nitroaromatic compounds
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additional information
?
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the enzyme is essential for lignin degradation
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additional information
?
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the enzyme is essential for lignin degradation
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additional information
?
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the enzyme is essential for lignin degradation
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additional information
?
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the enzyme is essential for lignin degradation
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additional information
?
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lingnin containing agricultural waste, like almond shells, hazelnut husks, clover straw, sunflower stems and hazelnut cobs are used as substrate for submerged cultures
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additional information
?
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the enzyme is essential for lignin degradation
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additional information
?
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no oxidation of veratryl alcohol
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Information
