precorrin-6A reductase | |||||||||
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Identifiers | |||||||||
EC no. | 1.3.1.54 | ||||||||
CAS no. | 137672-84-5 | ||||||||
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 | ||||||||
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In enzymology, a precorrin-6A reductase (EC 1.3.1.54) is an enzyme that catalyzes the chemical reaction
- precorrin-6A + NADPH + H precorrin-6B + NADP
The three substrates of this enzyme are precorrin 6A, NADPH and a proton; its two products are precorrin 6B and NADP.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH=CH group of an acceptor with NAD or NADPH as donor. The systematic name of this enzyme class is precorrin-6B:NADP+ oxidoreductase. Other names in common use include precorrin-6X reductase, precorrin-6Y:NADP+ oxidoreductase and CobK. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
See also
References
- Blanche F, Thibaut D, Famechon A, Debussche L, Cameron B, Crouzet J (1992). "Precorrin-6x reductase from Pseudomonas denitrificans: purification and characterization of the enzyme and identification of the structural gene". J. Bacteriol. 174 (3): 1036–42. PMC 206185. PMID 1732193.
- Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Nat. Prod. Rep. 19 (4): 390–412. doi:10.1039/b108967f. PMID 12195810.
Oxidoreductases: CH–CH oxidoreductases (EC 1.3) | |
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1.3.1: NAD/NADP acceptor | |
1.3.3: Oxygen acceptor | |
1.3.5: Quinone | |
1.3.99: Other acceptors |
Enzymes | |
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Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
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