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 | ||||||||
|
In enzymology, a cob(II)alamin reductase (EC 1.16.1.4) is an enzyme that catalyzes the chemical reaction
- 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
- 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.
Other oxidoreductases (EC 1.15–1.21) | |
---|---|
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 | |
---|---|
Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
|
This EC 1.16 enzyme-related article is a stub. You can help Misplaced Pages by expanding it. |