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Information on EC 1.11.1.13 - manganese peroxidase and Organism(s) Phanerodontia chrysosporium and UniProt Accession Q02567
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1.11.1.13 manganese peroxidaseIUBMB Comments
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+ . The complexed Mn3+ ion can diffuse into the lignified cell wall, where it oxidizes phenolic components of lignin and other organic substrates . It is inactive with veratryl alcohol or nonphenolic substrates.
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Word Map
- 1.11.1.13
- lignin
- laccase
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ligninolytic
- phanerochaete
- chrysosporium
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white-rot
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basidiomycete
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decolor
- peroxidases
- pleurotus
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lignin-degrading
- trametes
- versicolor
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veratryl
- ostreatus
- straw
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mniii
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lignocellulosic
- bjerkandera
- sordida
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lignocellulolytic
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remazol
- subvermispora
- lacteus
- eryngii
- irpex
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lignin-modifying
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kraft
- sawdust
- phlebia
- adusta
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ceriporiopsis
- 1-hydroxybenzotriazole
- nutrition
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lignocellulose-degrading
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ligninase
- sajor-caju
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wood-rotting
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dye-decolorizing
- tigrinus
- mnso4
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biosorption
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delignification
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delignified
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biobleaching
- degradation
- synthesis
- lentinula
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biotreatment
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non-phenolic
- industry
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decolourisation
- 2,6-dimethoxyphenol
- paper production
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low-nitrogen
- environmental protection
- biotechnology
- biofuel production
The taxonomic range for the selected organisms is: Phanerodontia chrysosporium
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
manganese peroxidase, manganese-dependent peroxidase, lemnp2, il-mnp1, hybrid mn-peroxidase, short mnp, mnp-gy, peroxidase-m2, mnp-pgy, mrmnp1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Mn-dependent (NADH-oxidizing) peroxidase
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MnP
MP
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peroxidase, manganese
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peroxidase-M2
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MnP
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
mechanism
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2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
ping-pong mechanism
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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
the proton-coupled electron transfer (PCET) process dominates the catalytic circle of MnP and the transformation of Mn3+, density functional theory (DFT) calculations, overview. During the reaction of H2O2 in the active MnP system, a typical signal of DMPO-Mn3+ is observed, indicating that MnP catalyzes Mn2+ to Mn3+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY
114995-15-2
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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
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
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?
Co2+ + H+ + H2O2
Co3+ + H2O
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reduction of enzyme compound II, oxidation at 2% the rate of Mn2+ oxidation
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?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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-
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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-
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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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
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Mn3+ oxidizes 2,6-dimethoxyphenol
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Mn2+ + H+ + H2O2
Mn3+ + H2O
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Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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Mn3+ oxidizes o-dianisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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specifically oxidizes Mn2+
Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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specifically oxidizes Mn2+
chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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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
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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
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Mn2+ + H+ + H2O2
Mn3+ + H2O
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completion of MnP catalytic cycle requires Mn2+
Mn3+ complex oxidizes a variety of organic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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completion of MnP catalytic cycle requires Mn2+
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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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
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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
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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
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completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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oxidation of Mn2+ to Mn3+ at a redox potential of 1.5 V
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?
Mn2+ + H+ + H2O2
Mn3+ + H2O
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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
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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
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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
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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
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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
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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
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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
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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
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initial depolymerization of the lignin polymer
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?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Mn2+ is a component of woody plant tissues
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?
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
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?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
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-
?
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
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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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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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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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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
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-
?
additional information
?
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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
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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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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 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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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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?
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 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 a variety of organic compounds in presence, but not in absence of Mn2+
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?
additional information
?
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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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?
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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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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?
additional information
?
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enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
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?
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
-
-
?
additional information
?
-
-
large substrates have no ready access to the catalytic center
-
-
?
additional information
?
-
-
large substrates have no ready access to the catalytic center
-
-
?
additional information
?
-
-
presence of proximal and distal histidines at the active center
-
-
?
additional information
?
-
-
Mn2+-dependent oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
no other metal can substitute Mn2+
-
-
?
additional information
?
-
-
Mn2+-independent oxidation of small phenolic compounds, such as guaiacol and dimethoxyphenol, rates are greatly reduced compared with the Mn-mediated reaction
-
-
?
additional information
?
-
-
MnP oxidizes nitroaromatic compounds
-
-
?
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
?
additional information
?
-
-
enzyme oxidizes the polymeric dyes poly R-481 and poly B-411
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+
-
-
?
additional information
?
-
-
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
-
-
-
NATURAL SUBSTRATE
NATURAL 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
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
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
heme protein containing protoporphyrin IX, 0.7 heme per enzyme molecule, iron ions are coordinated with prosthetic groups as high-spin ferriheme complexes
heme
-
enzyme contains a pentacoordinated, essentially high-spin ferric heme
heme
-
one iron protoporphyrin IX prosthetic group per enzyme molecule
heme
-
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
heme
-
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme
-
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme
-
heme protein
heme
-
important cofactor for production of active recombinant enzyme. Amendment of yeast cultures with heme increases concentrations of active recombinant enzyme
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Cd2+ exhibizs octahedral, hexacoordinate ligation geom,etry similar to that of Mn2+. Cd2+ also binds to a putative second weak metal-binding site with tetrahedral geometry at the C-terminus of the protein
Sm3+
coordination of Sm(III) at the Mn-binding site is octacoordinate. The reversible binding of Sm(III) may be a useful model for the reversible binding of Mn(III) to the enzyme, which is too unstable to allow similar examination
Ca2+
Mn2+
additional information
-
11 ppm Mn2+ in growth medium induces MnP synthesis
Ca2+
-
MnP calcium binding site, calcium content: 4 mol per mol of native MnP, 2 mol per mol of recombinant and A48C/A63C double mutant MnP, calcium decreases the rate of thermal inactivation
Mn2+
-
Mn2+ causes a concentration-dependent increase in total enzyme activity, little or no activity in absence of Mn2+
Mn2+
-
the proposed role of Mn2+ chelators in the enzyme mechanism is to release Mn3+ from the enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2O2
1 mM, complete, irreversible inactivation of wild-type enzyme correlated with the production of methionine sulfoxide, full activity can be retained by engineering Asn-81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser
1,10-phenanthroline
-
inhibits competitive Mn(III)-malonate formation
Cd2+
-
competitive inhibitor to Mn2+, uncompetitive to H2O2, reversibly inhibits oxidation of Mn2+ and Mn3+-mediated oxidation of 2,6-dimethoxyphenol, but not oxidation of phenols in absence of Mn2+, Cd2+ inhibits reduction of compound I and II by Mn2+ at pH 4.5 and binds at the Mn2+-binding site, kinetics of inhibition
ethylhydrazine
-
time-dependent inactivation via delta-meso-ethylheme adduct at pH 7.0, slightly stimulated by Co2+
methylhydrazine
-
slow inactivation in presence of H2O2, concentration- and time-dependent, slightly stimulated by Co2+
nitrilotriacetate
-
inhibits competitive Mn(III)-malonate formation
Pc reducer
-
the activity of manganese peroxidase is inhibited by Pc reducer at concentrations higher than 0.2 mg/ml
-
phenylhydrazine
-
rapid inactivation, concentration-dependent, no heme adducts detectable, inactivation is slightly stimulated by Co2+
Superoxide dismutase
-
inhibits oxidation of vanillylacetone by about 80%
-
Co2+
-
at concentrations below 4 mM in presence of H2O2 competitive inhibitor to Mn2+, slightly stimulates NaN3 or alkylhydrazine inactivation
Cu2+
-
inhibits by catalyzing the H2O2-dependent reduction of Mn3+
diphosphate
-
inhibits oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
diphosphate
-
diphosphate, as a Mn(III) complexing agent can negatively influence the oxidation capacity of Mn3+, which is used to verify the contribution of Mn3+ and other active species to the degradation of SMX
H2O2
-
inhibitory at high concentrations, phenol red is the most sensitive, vanillylacetone the least sensitive substrate to inhibition, Mn2+ protects against inhibition
H2O2
-
inactivation fits a first-order decay, rapid initial inactivation step
NaN3
-
complete inactivation within 2 min in presence of H2O2, accompanied by azidyl radical formation, prosthetic heme is converted to meso-azido adduct which is more rapidly oxidized by H2O2 than prosthetic heme, 2 equivalents of azide are oxidized before the enzyme molecule is inactivated, inactivation is slightly stimulated by Co2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2O2
-
H2O2-dependent
394594, 394601, 439814, 439815, 439816, 439817, 439820, 439821, 439822, 439823, 439824, 439825, 439826, 439828, 439831, 439832, 439833
Pc reducer
-
the activity of manganese peroxidase is promoted by Pc reducer at concentrations less than 0.2 mg/ml
-
Polyglutamate
-
slightly activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential
succinate
-
activates, stabilizes Mn3+ less effective than citrate or lactate
alpha-hydroxy acid
-
activates by chelating and stabilizing Mn3+ rather than activating the enzyme
alpha-hydroxy acid
-
stimulates by chelating Mn3+ and stabilizing its high redox potential
citrate
-
stimulates by chelating Mn3+ and stabilizing its high redox potential
citrate
-
activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential
L-Tartrate
-
activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential
Lactate
-
stimulates by complexing with and stabilizing Mn3+
Lactate
-
activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential
malonate
-
activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential, most effective physiological chelator excreted by the fungus
malonate
-
stabilizes Mn3+ at a relatively high redox potential and facilitate oxidation of organic substrates
oxalate
-
activates by chelating and stabilizing Mn3+
additional information
-
dramatic stimulation by chelating organic acids as C2- and C3-dicarboxylic or alpha-hydroxyl acids facilitate the dissociation of Mn(III) from manganese-enzyme complex, greater activation with weakly binding chelators with a low binding constant, e.g. lactate or tartrate
-
additional information
-
succinate, formate and acetate do not stabilize Mn3+
-
additional information
-
succinate is no Mn3+ chelator and activator
-
additional information
-
1 mM verartryl alcohol in growth medium increases activity 2fold
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
additional information
-
0.039 - 0.041
H2O2
-
MnP1 from mutants F190Y, F190L, F190I and F190A
0.074 - 0.08
Mn2+
-
MnP1 from mutants F190Y, F190L, F190I and F190A
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24
Mn2+
-
A48C/A63C double mutant MnP after thermal treatment at 37°C for 15 min
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
transient-state inhibition constants
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
0.055 U/ml, R42A mutant, in the presence of 2,6-dimethoxyphenol
additional information
-
0.055 U/ml, R42A mutant, in the presence of 2,6-dimethoxyphenol
additional information
0.069 U/ml, N131D mutant, in the presence of 2,6-dimethoxyphenol
additional information
-
0.069 U/ml, N131D mutant, in the presence of 2,6-dimethoxyphenol
additional information
0.076 U/ml, wild-type enzyme, in the presence of 2,6-dimethoxyphenol
additional information
-
0.076 U/ml, wild-type enzyme, in the presence of 2,6-dimethoxyphenol
additional information
-
216-467, 1 unit: initial increase in absorbance of 1.0 per min at 465 nm
additional information
-
216-467, 1 unit: initial increase in absorbance of 1.0 per min at 465 nm
additional information
-
425 U/l of MnP is extracted from the liquid fermentation medium of Phanerochaete chrysosporium and exhibits an efficient catalytic performance for SMX transformation. Optimal activity when the external parameters are designed at pH 5.0, an enzyme activity above 40 U/l, and an H2O2 concentration of 0.2 mM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
decolorization of bromocresol green, bromophenol red, bromothymol blue, o-cresol red, m-cresol purple, phenol red and thymol blue
4.5
4.8
additional information
4.5
-
oxidation of 2,2-azino-bis-3-ethyl-6-benzothiazolinesulfonate
additional information
-
isozyme H5: pI 4.2, isoenzyme H4: pI 4.5, isoenzyme H3: pI 4.9
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.1 - 6.1
-
veratryl alcohol oxidation, activity increases with increasing pH
3.1 - 8.3
-
in presence of H2O2 the formation of enzyme compound I is independent of pH over the range
3.5 - 6
-
pH 3.5: about 30% of maximal activity, pH 4.0: about 70% of maximal activity, pH 6.0: about 45% of maximal activity
4 - 5.5
-
about half-maximal activity at pH 4.0 and 5.5, 2,2-azino-bis-3-ethyl-6-benzothiazolinesulfonate-oxidation
4.5 - 5.7
-
about 65% of maximal activity at pH 4.5 and about 50% at pH 5.7, Mn(III)-lactate formation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
-
25°C: about 80% of maximal activity, 45°C: about 60% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
grown on wheat straw, rice straw, agriculture byproducts, or agro-industrial wastes
-
higher concentrations of foam and lower levels of spore inoculums result in the formation of scattered mycelial pellets, increased autolysis of chlamydospore-like cells (a reservoir of MnP), and a higher activity of MnP. Even though MnP is a secondary metabolite, the addition of 5times more glucose and diammonium tartrate, as carbon and nitrogen sources, results in a 4fold increase in the dry cell mass. MnP activity decreases under these conditions to less than half, due to the formation of increasingly dense pellets and the inhibited lysis of chlamydospore-like cells
-
shallow stationary culture growing on N-limited medium
-
production of ligninolytic enzyme MnP in liquid fermentation medium of Phanerochaete chrysosporium strain BKMF-1767
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase (MnP) is the most common lignin-degrading enzyme produced by white-rot basidiomycetes fungi. It can catalyze Mn2+ into Mn3+ by the addition of H2O2 or organic peroxide, and it can mediate the oxidation of a substrate
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PEM1_PHACH
378
0
39557
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
45000
46000
46000
-
-
46000
-
x * 46000, wild-type and mutants R177D, R177E, R177N and R177Q, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
-
x * 46000, wild-type and mutants R177D, R177E, R177N and R177Q, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
native MnP is glycosylated, but not recombinant MnP
glycoprotein
glycoprotein
-
-
glycoprotein
-
glycoprotein with one recognition sequence for N-linked carbohydrate at Asp-217, residue at position 10 is a potential site for O-glycosylation
glycoprotein
-
with 3 potential N-glycosylation sites, but only Asn-131 binds to carbohydrate
glycoprotein
-
the recombinant enzyme produced by ZBMNP16 is hyperglycosylated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, enzyme-Mn(II) structure at 1.45 A resolution, enzyme -Cd(II) structure, enzyme-Sm(III) structure, metal-free structure
manganese peroxidase crystallizes in the presence of Mn2+, where three homologous residues (Glu35, Glu39, and Asp179) participate in metal co-ordination, opening of the glutamate side-chains is not observed in manganese peroxidase crystals grown in the absence of Mn2+
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
M273L
mutant with high H2O2 resistance, i.e. 4.1fold higher than that of wild-type, Met-273 is located near the active site pocket and is converted to a non-oxidizable Leu
N131D
mutant displays a similar catalysis pattern to that of wild-type enzyme, Asn131 is the only potential glycosylation site
N81S
mutant enzyme is not inhibited by 1 mM H2O2, H2O2-dependency is 5.5fold higher than that of wild-type, engineering of Asn-81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser
R42A
mutant displays a similar catalysis pattern to that of wild-type enzyme, Arg42 is forming the peroxide binding pocket
A48C/A63C
-
A48C and A63C double mutant with an engineered disulfide bond near the distal calcium binding site to restrict the movement of helix B upon loss of calcium and to stabilize against this loss, thermal and pH-stability is improved compared with that of native and recombinant MnP, thermally treated enzyme contains one calcium and retains a percentage of its activity
F190A
-
mutant MnP: apparent Km-value for ferrocyanide oxidation is 1/8 of that for wild-type MnP and kcat is 4fold greater than that for wild-type enzyme, mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are dramatically increased compared with those for the wild-type MnP
F190I
-
mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
F190L
-
rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
R177A
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
R177D
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177E
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177K
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
R177N
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177Q
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
S168W
-
mutant can oxidize both Mn2+ and typical lignin peroxidase substrates such as veratryl alcohol
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
8
-
recombinant MnP: inactivation within 1 min, native MnP: inactivation within 15 min, A48C/A63C double mutant MnP: 1 h, 80% loss of activity
439853
additional information
-
recombinant MnP is more sensitive than native MnP as a result of lack of glycosylation
439853
4.5
-
recombinant MnP, native MnP and A48C/A63C double mutant MnP are stable
439853
4.5
-
in supernatant from pH 4.5 fermentations, 25% of activity of the recombinant enzyme is lost during the first 6 h, and another 25% decrease occurrs in the following 18 h. A much higher rate of loss of recombinant enzyme activity is observed in whole pH 4.5 culture, from which the yeast cells are not removed via centrifugation, than in either of the cell-free supernatants. The rate of loss of rMnP activity in pH 4.5 bioreactor cultures and culture supernatant is higher in samples obtained after 72 h of fermentation than in samples taken after 48 h
684525
6
-
native and A48C/A63C double mutant MnP: 1 h, less than 40% loss of activity
439853
6
-
recombinant MnP produced by Pichia pastoris alphaMnP1-1 in pH 6 fed-batch fermentations is not stable in pure pH 6.0 buffers. In 0.01 M potassium phosphate buffer, activity of the recombinant enzyme decreases by 25% in 4 h. Half-lives of 6.7, 3.4, and 0.4 h for 0.01 M phosphate, 0.1 M phosphate, and 0.01 M sodium citrate buffers, respectively. In culture supernatants obtained from pH 6.0 bioreactor fermentations, the recombinant enzyme is stable for up to 6 h before a measurable loss of activity occurrs, and only 25% of the initial activity is lost after 24 h incubation
684525
7
-
native MnP: 1 h, 80% loss of activity, A48C/A63C double mutant MnP: 1 h, 60% loss of activity
439853
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
complete inactivation after 5 min, 20% of original activity recovered after storage of heat-inactivated protein for 1 h at 0°C, no reactivation possible after boiling for 20 min
37
-
recombinant MnP: 5 min, 50% loss of activity, A48C/A63C double mutant MnP: relatively stable
49
-
wild-type MnP, MnP F190Y and MnP F190L: 330 s, 50% loss of activity, MnP F190I: 30 s, 50% loss of activity, MnP F190A: 5 s, complete loss of activity
52
-
recombinant MnP: 20 s, 50% loss of activity, A48C/A63C double mutant MnP: 2 min, 50% loss of activity
55
additional information
55
-
pH 4.5, 1.4 min, 50% loss of activity, both Mn2+ and Cd2+ protect MnP from thermal denaturation more efficiently than Ca2+ at pH 4.5, extending the half-life more than 2fold at 1 mM, combination of 0.5 mM Mn2+ and 0.5 mM Cd2+ extends the half-life more than 10fold
55
-
pH 4.5, 3 min, wild-type enzyme loses about 75% of the initial activity, 50% loss of activity after 3 min in presence of 1 mM ferric chloride. pH 4.5, 2 min, recombinant enzyme loses about 90% of the initial activity, about 45% loss of activity in presence of 1 mM ferric chloride
additional information
very sensitive to thermal treatment
additional information
-
Mn2+ protects against thermal inactivation, probably due to active site protection
additional information
-
susceptible to thermal inactivation due to the loss of calcium, calcium content after thermal treatment at 37°C for 15 min: 1.5 mol per mol of native MnP, 1 mol per mol of recombinant MnP and 1.3 mol per mol of A48C/A63C double mutant MnP, biphasic inactivation kinetics, recombinant MnP is more sensitive than native MnP as a result of the lack of glycosylation, calcium decreases the rate of thermal inactivation and reactivates MnP up to 50% of its original activity, while EGTA increases the rate of inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is more stable in carbon-limited cultures than in nitrogen-limited cultures
-
heat-inactivated protein, 100°C for 5 min, regains 80% of original activity by storage at 0°C for 1 h
-
no inactivation after 5 h in 50 mM Na-tartrate buffer, pH 4.5, with 2 mM nitrilotriacetate, 0.5 mM iodoacetamide or 2 mM PMSF
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, pH 4.5, purified enzyme in 50 mM Na-tartrate buffer is stable for 1 week
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of recombinant MnP, expressed in Escherichia coli
-
-
affinity chromatography on blue agarose: isozyme H4 95% pure, followed by preparative isoelectric focusing: isozymes H3 and H5 pure
-
purification of MnPs from the mutants F190Y, F190L, F190I and F190A
-
purification of recombinant A48C/A63C double mutant MnP, expressed in Escherichia coli
-
purification of the mutant enzymes R177D, R177E, R177N and R177Q
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA encoding MnP2 is cloned and expressed in Escherichia coli BL21(DE3)LysS
into the vector pET-22b, used for in vitro transcription and translation in a wheat germ extract system
cDNA sequences of several MnP-encoding genes, including mnp1, mnp2 and mnp3
-
expression in Pichia pastoris alphaMnP-1. Production of recombinant manganese peroxidase is highest at pH 6, with rMnP concentrations in the medium declining rapidly at pH less than 5.5, although cell growth rates are similar from pH 4-7
-
expression of A48C/A63C double mutant mnp gene in Escherichia coli XL-1 Blue
-
isoenzymes H3, H4 and H5 are encoded by different genes and differentially regulated
-
mutant genes F190Y, F190L, F190I and F190A are subcloned and expressed in Escherichia coli XL-1 Blue and DH5alphaF
-
three differentexpression vectors are constructed: pZBMNP contains the native Phanerochaete chrysosporium fungal secretion signal, palphaAMNP contains an alpha-factor secretion signal derived from Saccharomyces cerevisiae, and pZBIMNP has no secretion signal and is used for intracellular expression
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the optimum temperature for MnP production is 37°C. The amount of MnP registered at this temperature is 2.4 and 2.1times higher than that obtained in the treatments incubated at 30°C
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
degradation
Mn peroxidases are of much interest biotechnologically because of their potentially applications in bioremdeial waste treatment and in catalyzing difficult chemical transfromations
environmental protection
paper production
mediated system of degradation is potentially valuable for pulp and paper industries
biofuel production
-
applications of recombinant enzyme in the pulp and paper industry and in the processing of lignocellulosic materials for ethanol and biofuels production
degradation
-
crude enzyme is able to degrade the antibiotics tetracycline and oxytetracycline. 72.5% of 50 mg/l of tetracycline and 84.3% of 50 mg/l oxytetracycline is degraded by 40 U/l of amnganese peroxidase, within 4 h. With the pH at 3.0-4.8, the temperature at 37-40°C, the Mn2+ concentration between 0.1 and 0.4 mM, the H2O2 concentration of 0.2 mM, and the enzyme-substrate ratio above 2.0 U/mg, the degradation rate reaches the highest
environmental protection
paper production
synthesis
-
expression of active manganese peroxidase in an Escherichia coli cell-free protein synthesis system, and optimization of reaction conditions such as the concentrations of hemin, calcium ions, and disulfide bond isomerase. Cell-free synthesized manganese peroxidase purified using the hemagglutinin tag shows higher specific activity than the commercial wild-type enzyme
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
environmental protection
mediated system of degradation is potentially valuable for degradation of synthetic polymers and of environmental pollutants
environmental protection
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
thiol-mediated degradation of dimeric model compounds and of polymeric lignin by MnP has potential applications in the degradation of industrial lignins
environmental protection
-
mediated system of degradation is potentially valuable for degradation of synthetic polymers and of environmental pollutants
environmental protection
-
degradation of recalcitrant pollutants
environmental protection
-
the enzyme can degrade sulfamethoxazole (SMX), a broad-spectrum antibiotic (one non-phenolic compound) that has been widely used as a growth promoter in the breeding industry. SMX has been widely detected in effluents, soils, and surface waters in China. SMX is a persistent and polar organic compound in effluent with a half-life time of 17.8 days. More seriously, the SMX in aquatic environments may accelerate the spread of sul genes (antibiotic resistance genes (ARGs)) in microbial populations, and this would have detrimental effects on the ecosystem balance
paper production
-
mediated system of degradation is potentially valuable for pulp and paper industries
paper production
-
applications of recombinant enzyme in the pulp and paper industry and in the processing of lignocellulosic materials for ethanol and biofuels production
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
Gold, M.H.; Glenn, J.K.
Manganese peroxidase from Phanerochaete chrysosporium
Methods Enzymol.
161
258-264
1988
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
-
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
-
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
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)
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
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
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
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
-
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
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
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
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)
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
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
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
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
-
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
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
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
-
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
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
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)
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
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
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
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
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
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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