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Enzyme Nomenclature
Information on EC 1.11.1.13 - manganese peroxidase
for references in articles please use BRENDA:EC1.11.1.13
Word Map on EC 1.11.1.13
- 1.11.1.13
-
lignin
- laccase
- fungus
- phanerochaete
- chrysosporium
-
ligninolytic
-
white-rot
-
basidiomycete
-
decolor
- peroxidases
- pleurotus
- trametes
- versicolor
-
lignin-degrading
-
veratryl
-
straw
- ostreatus
-
mniii
- bjerkandera
- eryngii
- lacteus
- subvermispora
-
ceriporiopsis
-
kraft
- lentinula
-
hardwood
- 2,6-dimethoxyphenol
- phlebia
- irpex
-
remazol
-
delignification
-
sawdust
-
lignocellulolytic
- adusta
- sordida
-
pycnoporus
-
coriolus
-
biosorption
- environmental protection
- mnso4
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bagasse
-
wood-rotting
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biotreatment
- nutrition
- biotechnology
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delignified
-
low-nitrogen
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ligninase
- tigrinus
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dye-decolorizing
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biobleaching
- biofuel production
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decolourisation
- synthesis
- paper production
- industry
- degradation
-
non-phenolic
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.11.1.13
-
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RECOMMENDED NAME
GeneOntology No.
manganese peroxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
mechanism; shows properties of a peroxidase and an oxidase
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
mechanism; ping-pong mechanism
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
mechanism
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
shows properties of a peroxidase and an oxidase
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2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
shows properties of a peroxidase and an oxidase
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2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
mechanism; mechanism; ping-pong mechanism
-
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2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
mechanism; mechanism; ping-pong mechanism
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2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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-
-
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reduction
oxidation
-
-
-
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reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
Mn(II):hydrogen-peroxide oxidoreductase
A hemoprotein. The enzyme from white rot basidiomycetes is involved in the oxidative degradation of lignin. The enzyme oxidizes a bound Mn2+ ion to Mn3+ in the presence of hydrogen peroxide. The product, Mn3+, is released from the active site in the presence of a chelator (mostly oxalate and malate) that stabilizes it against disproportionation to Mn2+ and insoluble Mn4+ [4]. The complexed Mn3+ ion can diffuse into the lignified cell wall, where it oxidizes phenolic components of lignin and other organic substrates [1]. It is inactive with veratryl alcohol or nonphenolic substrates.
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CAS REGISTRY NUMBER
COMMENTARY
114995-15-2
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Deuteromycotina sp.
precursor. Molecular characterization of the basidiomycete isolate Nematoloma frowardii b19 and its manganese peroxidase places the fungus in the corticioid genus Phlebia
SwissProt
-
-
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3 isoenzymes: Mn2+-inducible MnP1 and MnP3, partly constitutive MnP2
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-
Deuteromycotina sp.
fungi IZU-154, FERM BP-1859, hyperlignolytic fungus IZU-154, belongs to the family Deuteromycotina and is deposited as the strain name of NK-1148, 4 isoenzymes
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white rot fungus, strains L-14807, L-15225, FP-104027, FP-90031-sp, FP-105752
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precursor. Molecular characterization of the basidiomycete isolate Nematoloma frowardii b19 and its manganese peroxidase places the fungus in the corticioid genus Phlebia
SwissProt
dikaryotic strain TMI 800, protein complex containing MnP, laccase and beta-glucosidase activities; white rot basidomycete, produces edible shiitake mushroom
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syn. Lentinus edodes, heterodikaryon strain 861; white rot basidomycete, produces edible shiitake mushroom
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-
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439832, 439851, 439853, 658331, 658782, 660342, 684525, 685714, 685720, 711491, 712142, 742929, 743019
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; isoenzymes H3, H4 and H5; isozyme profile depends on type of nutrient limitation and growth phase: no H5 in C-limited cultures, manganese increases H3-production; overproducing strain PSBL-1; white rot basidomycete
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; MnP exists as several closely related isoenzymes; white rot basidomycete
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; white rot basidomycete
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white rot fungus, syn. Corticium sordidum, strain HHB-8922-sp, 3 isoenzymes: MnPI, MnPII and MnPIII
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white rot fungus, strain CBS 613.91, 2 isoenzymes: MnP1 and MnP2
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; importance of media composition in the production of different isoenzymes; white rot basidomycete, 3 isoenzymes: MnP1, MnP2 and MnP3
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3 isoenzymes: Mn2+-inducible MnP1 and MnP3, partly constitutive MnP2
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70% degree of identity of 3 studied isozymes; syn. Coriolus versicolor, white rot basidomycete, strain PRL 572, 5 isoenzymes
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syn. Coriolus versicolor, white rot basidomycete, strain PRL 572, 5 isoenzymes
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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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
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-
?
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
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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
-
-
-
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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
-
-
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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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primary reaction product of peroxidation with H2O2 is enzyme compound I, formation of compound II from I follows second-order kinetic
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enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
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enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
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enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
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in absence of Mn2+ the enzyme oxidizes pinacyanol as most easily oxidized dye at 1.7% of the rate of the Mn2+ oxidation
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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additional information
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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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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in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
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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 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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catalytic cycle with oxidized intermediates MnP compound I and II
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catalytic cycle with oxidized intermediates MnP compound I and II
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catalytic cycle with oxidized intermediates MnP compound I and II
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catalytic cycle with oxidized intermediates MnP compound I and II
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catalytic cycle with oxidized intermediates MnP compound I and II
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catalytic cycle with oxidized intermediates MnP compound I and II
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no activity with veratryl alcohol
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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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large substrates have no ready access to the catalytic center
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large substrates have no ready access to the catalytic center
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presence of proximal and distal histidines at the active center
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Mn2+-dependent oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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Mn2+-independent oxidase activity on NAD(P)H
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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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no other metal can substitute Mn2+
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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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MnP oxidizes nitroaromatic compounds
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enzyme oxidizes 2,6-dimethoxyphenol
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enzyme oxidizes the polymeric dyes poly R-481 and poly B-411
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