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Literature summary for 1.11.1.13 extracted from

  • 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 (1991), J. Biol. Chem., 266, 8751-8758.
    View publication on PubMed
Search for more literature for 1.11.1.13

Activating Compound

Activating Compound Comment Organism Structure
alpha-hydroxy acid stimulates by stabilizing Mn3+ Phanerodontia chrysosporium
H2O2 H2O2-dependent Phanerodontia chrysosporium

Inhibitors

Inhibitors Comment Organism Structure
Co2+ at concentrations below 4 mM in presence of H2O2 competitive inhibitor to Mn2+, slightly stimulates NaN3 or alkylhydrazine inactivation Phanerodontia chrysosporium
Cu2+
-
 Phanerodontia chrysosporium
diphosphate
-
 Phanerodontia chrysosporium
ethylhydrazine time-dependent inactivation via delta-meso-ethylheme adduct at pH 7.0, slightly stimulated by Co2+ Phanerodontia chrysosporium
Fe3+
-
 Phanerodontia chrysosporium
methylhydrazine slow inactivation in presence of H2O2, concentration- and time-dependent, slightly stimulated by Co2+ Phanerodontia chrysosporium
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+ Phanerodontia chrysosporium
phenyldiazene concentration-dependent inactivation Phanerodontia chrysosporium
phenylhydrazine rapid inactivation, concentration-dependent, no heme adducts detectable, inactivation is slightly stimulated by Co2+ Phanerodontia chrysosporium

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Phanerodontia chrysosporium
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
-
 Phanerodontia chrysosporium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Mn2+ + H+ + H2O2 Phanerodontia chrysosporium acts together with lignin peroxidase in lignin-degradation of white rot fungi Mn3+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium
-
-
-
Phanerodontia chrysosporium
-
 white rot basidomycete
-
Phanerodontia chrysosporium OGC101
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Phanerodontia chrysosporium

Purification (Commentary)

Purification (Comment) Organism
isoenzyme 1 Phanerodontia chrysosporium

Reaction

Reaction Comment Organism Reaction ID
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O mechanism Phanerodontia chrysosporium
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Mn2+ + H+ + H2O2 completion of MnP catalytic cycle requires Mn2+ Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes guaiacol ?
Mn2+ + H+ + H2O2 Mn2+ binds to a common site close to the delta-meso-carbon without blocking the approach of small molecules to the heme edge Phanerodontia chrysosporium Mn3+ + H2O Mn3+ oxidizes guaiacol ?
Mn2+ + H+ + H2O2 acts together with lignin peroxidase in lignin-degradation of white rot fungi Phanerodontia chrysosporium Mn3+ + H2O
-
 ?
Mn2+ + H+ + H2O2 completion of MnP catalytic cycle requires Mn2+ Phanerodontia chrysosporium OGC101 Mn3+ + H2O Mn3+ oxidizes guaiacol ?
Mn2+ + H+ + H2O2 Mn2+ binds to a common site close to the delta-meso-carbon without blocking the approach of small molecules to the heme edge Phanerodontia chrysosporium OGC101 Mn3+ + H2O Mn3+ oxidizes guaiacol ?
additional information enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate Phanerodontia chrysosporium ?
-
 ?
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 Phanerodontia chrysosporium ?
-
 ?
additional information enzyme oxidizes ferrocyanide Phanerodontia chrysosporium ?
-
 ?
additional information enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate Phanerodontia chrysosporium OGC101 ?
-
 ?
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 Phanerodontia chrysosporium OGC101 ?
-
 ?
additional information enzyme oxidizes ferrocyanide Phanerodontia chrysosporium OGC101 ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 pI: 4.9 Phanerodontia chrysosporium

Cofactor

Cofactor Comment Organism Structure
heme enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme Phanerodontia chrysosporium

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.402
-
 methylhydrazine
-
 Phanerodontia chrysosporium
1
-
 Co2+
-
 Phanerodontia chrysosporium