- Source: Cyanocobalamin reductase (cyanide-eliminating)
In enzymology, a cyanocobalamin reductase (cyanide-eliminating) (EC 1.16.1.6) is an enzyme that catalyzes the chemical reaction
cob(I)alamin + cyanide + NADP+
⇌
{\displaystyle \rightleftharpoons }
cyanocob(III)alamin + NADPH + H+
The 3 substrates of this enzyme are cob(I)alamin, cyanide, and NADP+, whereas its 3 products are cyanocob(III)alamin, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those that oxidize metal ions and use NAD+ or NADP+ as an electron acceptor (for that oxidization reaction). The systematic name of this enzyme class is cob(I)alamin, cyanide:NADP+ oxidoreductase. Other names in common use include cyanocobalamin reductase, cyanocobalamin reductase (NADPH, cyanide-eliminating), cyanocobalamin reductase (NADPH, CN-eliminating), and NADPH:cyanocob(III)alamin oxidoreductase (cyanide-eliminating). This enzyme participates in porphyrin and chlorophyll metabolism. It uses one cofactor, FAD.
References
Watanabe F, Oki Y, Nakano Y, Kitaoka S (February 1988). "Occurrence and characterization of cyanocobalamin reductase (NADPH CN-eliminating) involved in decyanation of cyanocobalamin in Euglena gracilis". J. Nutr. Sci. Vitaminol. 34 (1). Tokyo: 1–10. doi:10.3177/jnsv.34.1. PMID 3134526.
