Manganese peroxidase

Function

Manganese peroxidase (MnP) catalyzes the conversion of Mn+2 to Mn+3 using hydrogen peroxide. MnP contains a heme group and needs calcium ion for activity. MnP is involved in lignin degradation. MnP is produced by wood-rotting fungi^[1]. Ceriporiopsis subvermispora expresses 3 genes of MnP: a short, long and extralong.

Relevance

Mn+3 in a chelated form is a powerful oxidizing agent which is able to mineralize lignin to CO2.

Structural highlights

The . Water molecules are shown as red spheres. The ^[2].

Heme-containing glycosylated manganese peroxidase complex with glycerol, Mn+2 (purple) and Ca+2 (green) ions 3m5q

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3D structures of manganese peroxidase3D structures of manganese peroxidase

Updated on 09-July-2019

ReferencesReferences

↑ Youngs HL, Sundaramoorthy M, Gold MH. Effects of cadmium on manganese peroxidase competitive inhibition of MnII oxidation and thermal stabilization of the enzyme. Eur J Biochem. 2000 Mar;267(6):1761-9. PMID:10712608
↑ Sundaramoorthy M, Gold MH, Poulos TL. Ultrahigh (0.93A) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: implications for the catalytic mechanism. J Inorg Biochem. 2010 Jun;104(6):683-90. Epub 2010 Mar 6. PMID:20356630 doi:10.1016/j.jinorgbio.2010.02.011

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

[1] Youngs HL, Sundaramoorthy M, Gold MH. Effects of cadmium on manganese peroxidase competitive inhibition of MnII oxidation and thermal stabilization of the enzyme. Eur J Biochem. 2000 Mar;267(6):1761-9. PMID:10712608

[2] Sundaramoorthy M, Gold MH, Poulos TL. Ultrahigh (0.93A) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: implications for the catalytic mechanism. J Inorg Biochem. 2010 Jun;104(6):683-90. Epub 2010 Mar 6. PMID:20356630 doi:10.1016/j.jinorgbio.2010.02.011

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