Manganese peroxidase
| manganese peroxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.11.1.13 | ||||||||
| CAS number | 114995-15-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| Search | |
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| PMC | articles |
| PubMed | articles |
| NCBI | proteins |
In enzymology, a manganese peroxidase (EC 1.11.1.13) is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are Mn(II), H+, and H2O2, whereas its two products are Mn(III) and H2O.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on a peroxide as acceptor (peroxidases). The systematic name of this enzyme class is Mn(II):hydrogen-peroxide oxidoreductase. Other names in common use include peroxidase-M2, and Mn-dependent (NADH-oxidizing) peroxidase. It employs one cofactor, heme. This enzyme needs Ca2+ for activity.
White rot fungi secrete this enzyme to aid lignin degradation.
Manganese peroxidase (commonly referred to as MnP) was discovered in 1985 simultaneously by the research groups of Michael H. Gold and Ronald Crawford in the fungus Phanerochaete chrysosporium. The protein was genetically sequenced in P. chrysoporium in 1989. The enzyme is thought to be unique to Basidiomycota as no bacterium, yeast, or mold species has yet been found which naturally produces it.
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