Aquacobalamin reductase
aquacobalamin reductase | |||||||||
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Identifiers | |||||||||
EC number | 1.16.1.3 | ||||||||
CAS number | 37256-39-6 | ||||||||
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 / EGO | ||||||||
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Aquacobalamin reductase (EC 1.16.1.3) is an enzyme that catalyzes the chemical reaction
- 2 cob(II)alamin + NAD+ 2 aquacob(III)alamin + NADH + H+
Thus, the two substrates of this enzyme are cob(II)alamin and nicotinamide adenine dinucleotide ion, whereas its 3 products are aquacob(III)alamin, nicotinamide adenine dinucleotide, and hydrogen ion.
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(II)alamin:NAD+ oxidoreductase. Other names in common use include aquocobalamin reductase, vitamin B12a reductase, NADH-linked aquacobalamin reductase, B12a reductase, and NADH2:cob(III)alamin oxidoreductase. This enzyme participates in porphyrin and chlorophyll metabolism. It employs one cofactor, FAD.
References
- 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.