Cyanocobalamin reductase (cyanide-eliminating) | |||||||||
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Identifiers | |||||||||
EC no. | 1.16.1.6 | ||||||||
CAS no. | 131145-00-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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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
- 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.
Other oxidoreductases (EC 1.15–1.21) | |
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1.15: Acting on superoxide as acceptor | |
1.16: Oxidizing metal ions | |
1.17: Acting on CH or CH2 groups | |
1.18: Acting on iron–sulfur proteins as donors | |
1.19: Acting on reduced flavodoxin as donor | |
1.20: Acting on phosphorus or arsenic in donors | |
1.21: Acting on X-H and Y-H to form an X-Y bond |
Enzymes | |
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