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Literature summary extracted from

  • 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 (2000), Eur. J. Biochem., 267, 7038-7045.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.11.1.13 malonate
-
 Phanerodontia chrysosporium
1.11.1.13 oxalate activates by chelating and stabilizing Mn3+ Phanerodontia chrysosporium

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.13 cDNA sequences of several MnP-encoding genes, including mnp1, mnp2 and mnp3 Phanerodontia chrysosporium

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.1.13
-
 Phanerodontia chrysosporium

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.13 E35Q engineered mutant Phanerodontia chrysosporium
1.11.1.13 R177A mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35 Phanerodontia chrysosporium
1.11.1.13 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+ Phanerodontia chrysosporium
1.11.1.13 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+ Phanerodontia chrysosporium
1.11.1.13 R177K mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35 Phanerodontia chrysosporium
1.11.1.13 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+ Phanerodontia chrysosporium
1.11.1.13 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+ Phanerodontia chrysosporium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.13 0.0057
-
 H2O2 mutant R177E Phanerodontia chrysosporium
1.11.1.13 0.0078
-
 H2O2 mutant R177Q Phanerodontia chrysosporium
1.11.1.13 0.0121
-
 H2O2 mutant R177N Phanerodontia chrysosporium
1.11.1.13 0.0126
-
 H2O2 mutant R177D Phanerodontia chrysosporium
1.11.1.13 0.039
-
 H2O2 mutant R177A Phanerodontia chrysosporium
1.11.1.13 0.044
-
 H2O2 mutant R177K Phanerodontia chrysosporium
1.11.1.13 0.055
-
 H2O2 wild-type MnP Phanerodontia chrysosporium
1.11.1.13 0.09
-
 Mn2+ wild-type MnP Phanerodontia chrysosporium
1.11.1.13 1.64
-
 Mn2+ mutant R177A Phanerodontia chrysosporium
1.11.1.13 2.15
-
 Mn2+ mutant R177D Phanerodontia chrysosporium
1.11.1.13 2.32
-
 Mn2+ mutant R177K Phanerodontia chrysosporium
1.11.1.13 2.91
-
 Mn2+ mutant R177Q Phanerodontia chrysosporium
1.11.1.13 3.61
-
 Mn2+ mutant R177N Phanerodontia chrysosporium
1.11.1.13 3.9
-
 Mn2+ mutant R177E Phanerodontia chrysosporium
1.11.1.13 4.4
-
 Mn2+ mutant E35Q Phanerodontia chrysosporium

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.11.1.13 extracellular
-
 Phanerodontia chrysosporium
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.11.1.13 46000
-
 x * 46000, wild-type and mutants R177D, R177E, R177N and R177Q, SDS-PAGE Phanerodontia chrysosporium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.11.1.13 Mn2+ + H+ + H2O2 Phanerodontia chrysosporium important component of lignin degradation system Mn3+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.13 Phanerodontia chrysosporium
-
-
-
1.11.1.13 Phanerodontia chrysosporium
-
 white rot basidomycete
-
1.11.1.13 Phanerodontia chrysosporium
-
 MnP1
-
1.11.1.13 Phanerodontia chrysosporium
-
 auxotrophic strain OGC107-1
-
1.11.1.13 Phanerodontia chrysosporium OGC101
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.13 purification of the mutant enzymes R177D, R177E, R177N and R177Q Phanerodontia chrysosporium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.13 Mn2+ + H+ + H2O2 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 Phanerodontia chrysosporium Mn3+ + H2O freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates ?
1.11.1.13 Mn2+ + H+ + H2O2 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 Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes lignin ?
1.11.1.13 Mn2+ + H+ + H2O2 role for Arg-177 in promoting efficient Mn2+ binding and oxidation by MnP Phanerodontia chrysosporium Mn3+ + H2O freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates ?
1.11.1.13 Mn2+ + H+ + H2O2 role for Arg-177 in promoting efficient Mn2+ binding and oxidation by MnP Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes lignin ?
1.11.1.13 Mn2+ + H+ + H2O2 important component of lignin degradation system Phanerodontia chrysosporium Mn3+ + H2O
-
 ?
1.11.1.13 Mn2+ + H+ + H2O2 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 Phanerodontia chrysosporium OGC101 Mn3+ + H2O freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates ?
1.11.1.13 additional information structural properties Phanerodontia chrysosporium ?
-
 ?
1.11.1.13 additional information catalytic cycle with oxidized intermediates MnP compound I and II Phanerodontia chrysosporium ?
-
 ?
1.11.1.13 additional information enzyme oxidizes ferrocyanide Phanerodontia chrysosporium ?
-
 ?
1.11.1.13 additional information enzyme oxidizes bromide Phanerodontia chrysosporium ?
-
 ?
1.11.1.13 additional information structural properties Phanerodontia chrysosporium OGC101 ?
-
 ?
1.11.1.13 additional information catalytic cycle with oxidized intermediates MnP compound I and II Phanerodontia chrysosporium OGC101 ?
-
 ?
1.11.1.13 additional information enzyme oxidizes ferrocyanide Phanerodontia chrysosporium OGC101 ?
-
 ?
1.11.1.13 additional information enzyme oxidizes bromide Phanerodontia chrysosporium OGC101 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.11.1.13 ? x * 46000, wild-type and mutants R177D, R177E, R177N and R177Q, SDS-PAGE Phanerodontia chrysosporium

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.11.1.13 0.77
-
 Mn2+ mutant E35Q Phanerodontia chrysosporium
1.11.1.13 17.3
-
 H2O2 mutant R177E Phanerodontia chrysosporium
1.11.1.13 23.2
-
 H2O2 mutant R177Q Phanerodontia chrysosporium
1.11.1.13 25
-
 Mn2+ mutant R177Q Phanerodontia chrysosporium
1.11.1.13 25.5
-
 Mn2+ mutant R177E Phanerodontia chrysosporium
1.11.1.13 28.8
-
 H2O2 mutant R177D Phanerodontia chrysosporium
1.11.1.13 30.2
-
 Mn2+ mutant R177D Phanerodontia chrysosporium
1.11.1.13 34.6
-
 Mn2+ mutant R177N Phanerodontia chrysosporium
1.11.1.13 35.8
-
 H2O2 mutant R177N Phanerodontia chrysosporium
1.11.1.13 184
-
 Mn2+ mutant R177A Phanerodontia chrysosporium
1.11.1.13 190
-
 H2O2 mutant R177A Phanerodontia chrysosporium
1.11.1.13 252
-
 H2O2 wild-type MnP Phanerodontia chrysosporium
1.11.1.13 256
-
 Mn2+ wild-type MnP Phanerodontia chrysosporium
1.11.1.13 262
-
 Mn2+ mutant R177K Phanerodontia chrysosporium
1.11.1.13 273
-
 H2O2 mutant R177K Phanerodontia chrysosporium

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.13 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 Phanerodontia chrysosporium