Manganese peroxidase
From Proteopedia
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== Function == | == 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<ref>PMID:10712608</ref>. | + | '''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<ref>PMID:10712608</ref>. ''Ceriporiopsis subvermispora'' expresses 3 genes of MnP: a short, long and '''extralong'''. |
== Relevance == | == Relevance == | ||
Revision as of 10:57, 17 April 2016
Contents |
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 Mn binding site of MnP contains the heme group which coordinates with the ion. The heme group is coordinated mostly by aromatic side chains[2].
3D structures of manganese peroxidase
Updated on 17-April-2016
References
- ↑ 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
