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2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
gallic acid + H2O2
?
-
-
-
?
Mn2+ + 2,6-dimethoxyphenol + H2O2
?
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Mn2+ + H2O2
Mn3+ + H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
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
-
-
?
Amplex Red + H2O2
?
-
-
-
-
?
bromocresol green + H2O2
?
-
-
-
-
?
bromocresol purple + H2O2
?
-
-
-
-
?
bromophenol blue + H2O2
?
-
-
-
-
?
bromophenol red + H2O2
?
-
-
-
-
?
bromothymol blue + H2O2
?
-
-
-
-
?
Co2+ + H+ + H2O2
Co3+ + H2O
-
reduction of enzyme compound II, oxidation at 2% the rate of Mn2+ oxidation
-
?
ferrocyanide + H+ + H2O2
ferricyanide + H2O
-
-
-
-
r
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
-
-
-
-
?
m-cresol purple + H2O2
?
-
-
-
-
?
Mn(III)-tartrate + H2O
Mn(II)-tartrate + H+ + H2O
-
-
-
-
r
Mn2+ + H+ + H2O2
Mn3+ + H2O
Mn2+ + H2O2 + oxytetracycline
Mn3+ + ?
-
-
-
-
?
Mn2+ + H2O2 + tetracycline
Mn3+ + ?
-
-
-
-
?
o-cresol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
thymol blue + H2O2
?
-
-
-
-
?
vanillylacetone + H2O2
?
-
-
-
-
?
additional information
?
-
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes curcumin
?
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
-
-
Mn3+ oxidizes lignin
?
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 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
-
-
Mn3+ oxidizes guaiacol
?
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
-
?
additional information
?
-
structural properties
-
-
?
additional information
?
-
-
structural properties
-
-
?
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
?
-
-
-
-
-
?
additional information
?
-
-
no oxidation of Co2+
-
-
?
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
?
-
-
structural properties
-
-
?
additional information
?
-
-
structural properties
-
-
?
additional information
?
-
-
structural properties
-
-
?
additional information
?
-
-
structural properties
-
-
?
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
?
-
-
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
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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 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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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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catalytic cycle with oxidized intermediates MnP compound I and II
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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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catalytic cycle with oxidized intermediates MnP compound I and II
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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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no activity with veratryl alcohol
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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 ferrocyanide
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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 ferrocyanide
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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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enzyme oxidizes phenol red
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additional information
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enzyme oxidizes phenol red
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additional information
?
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enzyme oxidizes phenol red
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additional information
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enzyme oxidizes bromide
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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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no oxidation of Ni2+
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additional information
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no oxidation of Ni2+
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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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manganese peroxidase (MnP) is applied to induce the in vitro oxidation of the broad-spectrum antibiotic sulfamethoxazole (SMX). 87.04% of the SMX is transformed following first-order kinetics (kobs = 0.438/h) within 6 h when 40 U/l of MnP is added. The reaction kinetics are investigated under different conditions, including pH, MnP activity, and H2O2 concentration. The active species Mn3+ is responsible for the oxidation of SMX, and the Mn3+ production rate is monitored to reveal the interaction among MnP, Mn3+, and SMX, computational analysis, overview. Possible oxidation pathways of SMX are proposed based on single-electron transfer mechanism, which primarily included the S-N bond cleavage, the C-S bond cleavage, and one electron loss without bond breakage. It is then transformed to hydrolysis, N-H oxidation, self-coupling, and carboxylic acid coupling products. SMX stepwise undergoes an N-H oxidation and eventually converts into nitroso benzene and a nitro benzene compound. In addition, the sulfamethoxazole cation radical can also turn into self-coupling products, such as SMX-dimer
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Paszczynski, A.; Huynh, V.B.; Crawford, R.L.
Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium
Arch. Biochem. Biophys.
244
750-765
1986
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F 1767
brenda
Aitken, M.; Irvine, R.L.
Stability testing of ligninase and Mn-peroxidase from Phanerochaete chrysosporium
Biotechnol. Bioeng.
34
1251-1260
1989
Phanerodontia chrysosporium, Phanerodontia chrysosporium VKM F-1767
brenda
Glenn, J.K.; Akileswaran, L.; Gold, M.H.
Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium
Arch. Biochem. Biophys.
251
688-696
1986
Phanerodontia chrysosporium
brenda
Wariishi, H.; Akileswaran, L.; Gold, M.H.
Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle
Biochemistry
27
5365-5370
1988
Phanerodontia chrysosporium
brenda
Wariishi, H.; Dunford, H.B.; MacDonald, I.D.; Gold, M.H.
Manganese peroxidase from the lignin-degrading basidiomycete Phanerochaete chrysosporium. Transient state kinetics and reaction mechanism
J. Biol. Chem.
264
3335-3340
1989
Phanerodontia chrysosporium
brenda
Dass, S.B.; Reddy, C.A.
Characterization of extracellular peroxidases produced by acetate-buffered cultures of the lignin-degrading basidiomycete Phanerochaete chrysosporium
FEMS Microbiol. Lett.
69
221-224
1990
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F 1767
brenda
Banci, L.; Bertini, I.; Pease, E.A.; Tien, M.; Turano, P.
1H NMR investigation of manganese peroxidase from Phanerochaete chrysosporium. A comparison with other peroxidases
Biochemistry
31
10009-10017
1992
Phanerodontia chrysosporium
brenda
Wariishi, H.; Valli, K.; Gold, M.H.
Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators
J. Biol. Chem.
267
23688-23695
1992
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Tuor, U.; Wariishi, H.; Schoemaker, H.E.; Gold, M.H.
Oxidation of phenolic arylglycerol beta-aryl ether lignin model compounds by manganese peroxidase from Phanerochaete chrysosporium: oxidative cleavage of an alpha-carbonyl model compound
Biochemistry
31
4986-4995
1992
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Pease, E.A.; Tien, M.
Heterogeneity and regulation of manganese peroxidases from Phanerochaete chrysosporium
J. Bacteriol.
174
3532-3540
1992
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F 1767
brenda
Harris, R.Z.; Wariishi, H.; Gold, M.H.; Ortiz de Montellano, P.R.
The catalytic site of manganese peroxidase. Regiospecific addition of sodium azide and alkylhydrazines to the heme group
J. Biol. Chem.
266
8751-8758
1991
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Popp, J.L.; Kirk, T.K.
Oxidation of methoxybenzenes by manganese peroxidase and by Mn3+
Arch. Biochem. Biophys.
288
145-148
1991
Phanerodontia chrysosporium, Lentinula edodes
brenda
Aitken, M.; Irvine, R.L.
Characterization of reactions catalyzed by manganese peroxidase from Phanerochaete chrysosporium
Arch. Biochem. Biophys.
276
405-414
1990
Phanerodontia chrysosporium, Phanerodontia chrysosporium VKM F-1767
brenda
Datta, A.; Bettermann, A.; Kirk, T.K.
Identification of a specific manganese peroxidase among ligninolytic enzymes secreted by Phanerochaete chrysosporium during wood decay
Appl. Environ. Microbiol.
57
1453-1460
1991
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F 1767
brenda
Wariishi, H.; Valli, K.; Renganathan, V.; Gold, M.H.
Thiol-mediated oxidation of nonphenolic lignin model compounds by manganese peroxidase of Phanerochaete chrysosporium
J. Biol. Chem.
264
14185-14191
1989
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Gold, M.H.; Glenn, J.K.
Manganese peroxidase from Phanerochaete chrysosporium
Methods Enzymol.
161
258-264
1988
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
-
brenda
Paszczynski, A.; Crawford, R.L.; Huynh, V.B.
Manganese peroxidase from Phanerochaete chrysosporium: Purification
Methods Enzymol.
161
264-270
1988
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F 1767
-
brenda
Gelpke, M.D.S.; Youngs, H.L.; Gold, M.H.
Role of arginine 177 in the MnII binding site of manganese peroxidase. Studies with R177D, R177E, R177N, and R177Q mutants
Eur. J. Biochem.
267
7038-7045
2000
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Miyazaki, C.; Takahashi, H.
Engineering of the H2O2-binding pocket region of a recombinant manganese peroxidase to be resistant to H2O2
FEBS Lett.
509
111-114
2001
Phanerodontia chrysosporium (Q02567), Phanerodontia chrysosporium, Phanerodontia chrysosporium MnP2 (Q02567)
brenda
Sarkar, S.; Martinez, A.T.; Martinez, M.J.
Biochemical and molecular characterization of a manganese peroxidase isoenzyme from Pleurotus ostreatus
Biochim. Biophys. Acta
1339
23-30
1997
Phanerodontia chrysosporium, Rigidoporus microporus, Lentinus tigrinus, Pleurotus eryngii, Pleurotus ostreatus, Pleurotus ostreatus CBS 411.71
brenda
Matsubara, M.; Suzuki, J.; Deguchi, T.; Miura, M.; Kitaoka, Y.
Characterization of manganese peroxidases from the hyperlignolytic fungus IZU-154
Appl. Environ. Microbiol.
62
4066-4072
1996
Phanerodontia chrysosporium, Deuteromycotina sp., Phanerodontia chrysosporium ME446
brenda
Palma, C.; Martinez, A.T.; Lema, J.M.; Martinez, M.J.
Different fungal manganese-oxidizing peroxidases: A comparison between Bjerkandera sp. and Phanerochaete chrysosporium
J. Biotechnol.
77
235-245
2000
Bjerkandera adusta, Bjerkandera sp., Phanerodontia chrysosporium, Pleurotus eryngii, Pleurotus ostreatus, Pleurotus pulmonarius, Bjerkandera sp. BOS55, Phanerodontia chrysosporium VKM F-1767
brenda
Hofrichter, M.
Review: Lignin conversion by manganese peroxidase (MnP)
Enzyme Microb. Technol.
30
454-466
2002
Abortiporus biennis, Agaricus bisporus, Agrocybe dura, Agrocybe praecox, Armillaria mellea, Armillaria ostoyae, Auricularia sp., Auricularia sp. M37, Bjerkandera adusta, Bjerkandera sp., Clitocybula dusenii, Coriolopsis trogii, Coriolus pruinosum, Cyathus stercoreus, Deuteromycotina sp., Dichomitus squalens, Flavodon flavus, Ganoderma lucidum, Gelatoporia subvermispora, Gymnopus dryophilus, Gymnopus quercophilus, Heterobasidion annosum, Hypholoma fasciculare, Hypholoma frowardii, Irpex lacteus, Kuehneromyces mutabilis, Lentinula edodes, Lentinus sajor-caju, Lentinus tigrinus, Merulius sp., Merulius sp. M15, Panaeolus sphinctrinus, Perenniporia tephropora, Phaeolus schweinitzii, Phallus impudicus, Phanerochaete flavidoalba, Phanerochaete laevis, Phanerochaete sordida, Phanerodontia chrysosporium, Phellinus trivialis, Phlebia brevispora, Phlebia radiata, Phlebia tremellosa, Physisporinus vitreus, Pleurotus eryngii, Pleurotus ostreatus, Pleurotus pulmonarius, Psilocybe cubensis, Rigidoporus microporus, Stropharia aeruginosa, Stropharia coronilla, Stropharia rugosoannulata, Trametes gibbosa, Trametes hirsuta, Trametes polyzona, Trametes versicolor
-
brenda
Kishi, K.; Hildebrand, D.P.; Kusters-van Someren, M.; Gettemy, J.; Mauk, A.G.; Gold, M.H.
Site-directed mutations at phenylalanine-190 of manganese peroxidase: Effects on stability, function, and coordination
Biochemistry
36
4268-4277
1997
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Reading, N.S.; Aust, S.D.
Engineering a disulfide bond in recombinant manganese peroxidase results in increased thermostability
Biotechnol. Prog.
16
326-333
2000
Phanerodontia chrysosporium
brenda
Youngs, H.L.; Sundaramoorthy, M; Gold, M.H.
Effects of cadmium on manganese peroxidase. Competitive inhibition of MnII oxidation and thermal stabilization of the enzyme
Eur. J. Biochem.
267
1761-1769
2000
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Sundaramoorthy, M.; Youngs, H.L.; Gold, M.H.; Poulos, T.L.
High-resolution crystal structure of manganese peroxidase: substrate and inhibitor complexes
Biochemistry
44
6463-6470
2005
Phanerodontia chrysosporium (Q02567)
brenda
Gu, L.; Lajoie, C.; Kelly, C.
Expression of a Phanerochaete chrysosporium manganese peroxidase gene in the yeast Pichia pastoris
Biotechnol. Prog.
19
1403-1409
2003
Phanerodontia chrysosporium
brenda
Christian, V.V.; Shrivastava, R.; Novotny, C.; Vyas, B.R.
Decolorization of sulfonphthalein dyes by manganese peroxidase activity of the white-rot fungus Phanerochaete chrysosporium
FEMS Microbiol. Rev.
48
771-774
2003
Phanerodontia chrysosporium
brenda
Podgornik, H.; Podgornik, A.
Separation of manganese peroxidase isoenzymes on strong anion-exchange monolithic column using pH-salt gradient
J. Chromatogr. B
799
343-347
2004
Phanerodontia chrysosporium, Phanerodontia chrysosporium MZKI B-223
brenda
Urek, R.O.; Pazarlioglu, N.K.
Purification and partial characterization of manganese peroxidase from immobilized Phanerochaete chrysosporium
Proc. Biochem.
39
2061-2068
2004
Phanerodontia chrysosporium
-
brenda
Jiang, F.; Kongsaeree, P.; Schilke, K.; Lajoie, C.; Kelly, C.
Effects of pH and temperature on recombinant manganese peroxidase production and stability
Appl. Biochem. Biotechnol.
146
15-27
2008
Phanerodontia chrysosporium
brenda
Jiang, F.; Kongsaeree, P.; Charron, R.; Lajoie, C.; Xu, H.; Scott, G.; Kelly, C.
Production and separation of manganese peroxidase from heme amended yeast cultures
Biotechnol. Bioeng.
99
540-549
2008
Phanerodontia chrysosporium
brenda
Kwon, H.; Chung, E.; Oh, J.; Lee, C.; Ahn, I.
Optimized production of lignolytic manganese peroxidase in immobilized cultures of Phanerochaete chrysosporium
Biotechnol. Bioprocess Eng.
13
108-114
2008
Phanerodontia chrysosporium
-
brenda
Hwang, S.; Lee, C.H.; Ahn, I.S.; Park, K.
Manganese peroxidase-catalyzed oxidative degradation of vanillylacetone
Chemosphere
72
572-577
2008
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
brenda
Zhang, X.; Wang, Y.; Wang, L.; Chen, G.; Liu, W.; Gao, P.
Site-directed mutagenesis of manganese peroxidase from Phanerochaete chrysosporium in an in vitro expression system
J. Biotechnol.
139
176-178
2009
Phanerodontia chrysosporium (Q02567), Phanerodontia chrysosporium
brenda
Ruiz-Duenas, F.J.; Morales, M.; Garcia, E.; Miki, Y.; Martinez, M.J.; Martinez, A.T.
Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases
J. Exp. Bot.
60
441-452
2009
Phanerodontia chrysosporium (Q02567)
brenda
Hu, M.; Zhang, W.; Wu, Y.; Gao, P.; Lu, X.
Characteristics and function of a low-molecular-weight compound with reductive activity from Phanerochaete chrysosporium in lignin biodegradation
Biores. Technol.
100
2077-2081
2009
Phanerodontia chrysosporium
brenda
Vassilev, N.; Requena, A.; Nieto, L.; Nikolaeva, I.; Vassileva, M.
Production of manganese peroxidase by Phanerochaete chrisosporium grown on medium containing agro-wastes/rock phosphate and biocontrol properties of the final product
Ind. Crops Prod.
30
28-32
2009
Phanerodontia chrysosporium
brenda
Ninomiya, R.; Zhu, B.; Kojima, T.; Iwasaki, Y.; Nakano, H.
Role of disulfide bond isomerase DsbC, calcium ions, and hemin in cell-free protein synthesis of active manganese peroxidase isolated from Phanerochaete chrysosporium
J. Biosci. Bioeng.
117
652-657
2014
Phanerodontia chrysosporium
brenda
Wen, X.; Jia, Y.; Li, J.
Enzymatic degradation of tetracycline and oxytetracycline by crude manganese peroxidase prepared from Phanerochaete chrysosporium
J. Hazard. Mater.
177
924-928
2010
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
brenda
Ding, Y.; Cui, K.; Guo, Z.; Cui, M.; Chen, Y.
Manganese peroxidase mediated oxidation of sulfamethoxazole integrating the computational analysis to reveal the reaction kinetics, mechanistic insights, and oxidation pathway
J. Hazard. Mater.
415
125719
2021
Phanerodontia chrysosporium, Phanerodontia chrysosporium CCTCC AF96007, Phanerodontia chrysosporium BKMF-1767
brenda
Chowdhary, P.; Shukla, G.; Raj, G.; Ferreira, L.; Bharagava, R.
Microbial manganese peroxidase a ligninolytic enzyme and its ample opportunities in research
SN Appl. Sci.
1
45
2019
Acinetobacter baumannii, Alcaligenes faecalis, Bacillus cereus, Bacillus subtilis, Gelatoporia subvermispora, Ganoderma lucidum, Ganoderma lucidum (A0A1I9KRQ0), Irpex lacteus, Irpex lacteus (A0A1S6KK55), Irpex lacteus (S4W784), Schizophyllum commune, Trametes villosa, Trametes sp. 48424, Cerrena unicolor (A0A7D5FUQ6), Agrocybe praecox (G4WG41), Phanerodontia chrysosporium (Q02567), Phlebia radiata (Q70LM3), Irpex lacteus CD2 (A0A1S6KK55), Irpex lacteus F17 (S4W784), Irpex lacteus CCBAS238, Schizophyllum commune IBL-06, Ganoderma lucidum IBL-05, Cerrena unicolor BBP6 (A0A7D5FUQ6)
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brenda