| EC |
1.11.1.13 |
| Accepted name: |
manganese peroxidase |
| Reaction: |
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O |
| Other name(s): |
peroxidase-M2; Mn-dependent (NADH-oxidizing) peroxidase |
| Systematic name: |
Mn(II):hydrogen-peroxide oxidoreductase |
| 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+ [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. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 114995-15-2 |
| References: |
| 1. |
Glenn, J.K., Akileswaran, L. and Gold, M.H. Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium. Arch. Biochem. Biophys. 251 (1986) 688–696. [DOI] [PMID: 3800395] |
| 2. |
Paszczynski, A., Huynh, V.-B. and Crawford, R. Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium. Arch. Biochem. Biophys. 244 (1986) 750–765. [DOI] [PMID: 3080953] |
| 3. |
Wariishi, H., Akileswaran, L. and Gold, M.H. Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle. Biochemistry 27 (1988) 5365–5370. [PMID: 3167051] |
| 4. |
Kuan, I.C. and Tien, M. Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation. Proc. Natl. Acad. Sci. USA 90 (1993) 1242–1246. [DOI] [PMID: 8433984] |
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| [EC 1.11.1.13 created 1992] |
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