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Cyanocobalamin reductase (cyanide-eliminating)

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Cyanocobalamin reductase (cyanide-eliminating)
Identifiers
EC no.1.16.1.6
CAS no.131145-00-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
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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+ 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

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  • 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.