In enzymology, a precorrin-6A reductase (EC 1.3.1.54) is an enzyme that catalyzes the chemical reaction
| precorrin-6A reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.1.54 | ||||||||
| CAS no. | 137672-84-5 | ||||||||
| 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 | ||||||||
| |||||||||
- precorrin-6A + NADPH + H+ precorrin-6B + NADP+
The three substrates of this enzyme are precorrin 6A, NADPH and a proton; its two products are precorrin 6B and NADP+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH=CH group of an acceptor with NAD or NADPH as donor. The systematic name of this enzyme class is precorrin-6B:NADP+ oxidoreductase. Other names in common use include precorrin-6X reductase, precorrin-6Y:NADP+ oxidoreductase and CobK. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
See also
editReferences
edit- Blanche F, Thibaut D, Famechon A, Debussche L, Cameron B, Crouzet J (1992). "Precorrin-6x reductase from Pseudomonas denitrificans: purification and characterization of the enzyme and identification of the structural gene". J. Bacteriol. 174 (3): 1036–42. PMC 206185. PMID 1732193.
- 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.
