Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxidases

Mn(II):hydrogen-peroxide oxidoreductase

2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O [RN:R00011]

R00011

Mn(II) [CPD:C19610];
H+ [CPD:C00080];
H2O2 [CPD:C00027]

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.

EC 1.11.1.13 created 1992

1  [PMID:3800395]

Glenn JK, Akileswaran L, Gold MH.

Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium.

Arch. Biochem. Biophys. 251 (1986) 688-96.

2  [PMID:3080953]

Paszczynski A, Huynh VB, Crawford R.

Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium.

Arch. Biochem. Biophys. 244 (1986) 750-65.

3  [PMID:3167051]

Wariishi H, Akileswaran L, Gold MH.

Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle.

Biochemistry. 27 (1988) 5365-70.

4  [PMID:8433984]

Kuan IC, Tien M

Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation.

Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 1242-6.