EC 184.108.40.206 - Manganese peroxidase
IntEnz Enzyme Nomenclature
22776 [IUBMB]2H+H(+)Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)H2O2H2O2Name origin: UniProt - CHECKED (C)Formula: H2O2
Charge: 0ChEBI compound status: CHECKED (C)2Mn2+Mn(2+)Name origin: UniProt - CHECKED (C)Formula: Mn
Charge: 2ChEBI compound status: CHECKED (C)=2H2OH2OName origin: UniProt - CHECKED (C)Formula: H2O
Charge: 0ChEBI compound status: CHECKED (C)2
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.
Links to other databases
Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium.Arch. Biochem. Biophys. 251: 688-696 (1986).
Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium.Arch. Biochem. Biophys. 244: 750-765 (1986). [PMID: 3080953]
Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle.Biochemistry 27: 5365-5370 (1988).
Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation.Proc. Natl. Acad. Sci. U.S.A. 90: 1242-1246 (1993). [PMID: 8433984]
[EC 220.127.116.11 created 1992]