cob(II)yrinic acid a,c-diamide reductase | |||||||||
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Identifiers | |||||||||
EC no. | 1.16.8.1 | ||||||||
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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In enzymology, a cob(II)yrinic acid a,c-diamide reductase (EC 1.16.8.1) is an enzyme that catalyzes the chemical reaction
2 cob(I)yrinic acid a,c-diamide + FMN + 3 H 2 cob(II)yrinic acid a,c-diamide + FMNH2The three substrates of this enzyme are cob(I)yrinic acid a,c-diamide, flavin mononucleotide, and H; its two products are cob(II)yrinic acid a,c-diamide and FMNH2.
Classification
This enzyme belongs to the family of oxidoreductases, specifically those oxidizing metal ion with a flavin as acceptor.
Nomenclature
The systematic name of this enzyme class is cob(I)yrinic acid-a,c-diamide:FMN oxidoreductase. This enzyme is also called CobR and cob(II)yrinic acid-a,c-diamide:FMN oxidoreductase (incorrect).
Biological role
This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria.
See also
References
- Blanche F, Maton L, Debussche L, Thibaut D (1992). "Purification and characterization of Cob(II)yrinic acid a,c-diamide reductase from Pseudomonas denitrificans". J. Bacteriol. 174 (22): 7452–4. PMC 207442. PMID 1429467.
- Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Nat. Prod. Rep. 19 (4): 390–412. doi:10.1039/b108967f. PMID 12195810.
Other oxidoreductases (EC 1.15–1.21) | |
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1.15: Acting on superoxide as acceptor | |
1.16: Oxidizing metal ions | |
1.17: Acting on CH or CH2 groups | |
1.18: Acting on iron–sulfur proteins as donors | |
1.19: Acting on reduced flavodoxin as donor | |
1.20: Acting on phosphorus or arsenic in donors | |
1.21: Acting on X-H and Y-H to form an X-Y bond |
Enzymes | |
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Activity | |
Regulation | |
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