In enzymology, a cob(II)alamin reductase (EC 1.16.1.4) is an enzyme that catalyzes the chemical reaction
| cob(II)alamin reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.16.1.4 | ||||||||
| CAS no. | 37256-40-9 | ||||||||
| 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 | ||||||||
| |||||||||
- 2 cob(I)alamin + NAD+ 2 cob(II)alamin + NADH + H+
Thus, the two substrates of this enzyme are cob(I)alamin and NAD+, whereas its 3 products are cob(II)alamin, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those oxidizing metal ion with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cob(I)alamin:NAD+ oxidoreductase. Other names in common use include vitamin B12r reductase, B12r reductase, and NADH2:cob(II)alamin oxidoreductase. This enzyme participates in porphyrin and chlorophyll metabolism. It employs one cofactor, FAD.
References
edit- Walker GA, Murphy S, Huennekens FM (1969). "Enzymatic conversion of vitamin B 12a to adenosyl-B 12: evidence for the existence of two separate reducing systems". Arch. Biochem. Biophys. 134 (1): 95–102. doi:10.1016/0003-9861(69)90255-0. PMID 4390543.
