Biology:Precorrin-6A reductase
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Short description: Class of enzymes
| precorrin-6A reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.3.1.54 | ||||||||
| CAS number | 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 | ||||||||
| |||||||||
In enzymology, precorrin-6A reductase (EC 1.3.1.54) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are precorrin-6A, reduced nicotinamide adenine dinucleotide phosphate (NADPH) and a proton. Its products are precorrin-6B and oxidised NADP+.[1][2][3]
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.[4]
See also
References
- ↑ Enzyme 1.3.1.54 at KEGG Pathway Database.
- ↑ "Precorrin-6x reductase from Pseudomonas denitrificans: purification and characterization of the enzyme and identification of the structural gene". J. Bacteriol. 174 (3): 1036–42. 1992. doi:10.1128/jb.174.3.1036-1042.1992. PMID 1732193.
- ↑ "The biosynthesis of adenosylcobalamin (vitamin B12)". Nat. Prod. Rep. 19 (4): 390–412. 2002. doi:10.1039/b108967f. PMID 12195810.
- ↑ Fang, H; Kang, J; Zhang, D (30 January 2017). "Microbial production of vitamin B12: a review and future perspectives.". Microbial Cell Factories 16 (1): 15. doi:10.1186/s12934-017-0631-y. PMID 28137297.
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