L-idonate 5-dehydrogenase
| L-idonate 5-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.264 | ||||||||
| 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, L-idonate 5-dehydrogenase (EC 1.1.1.264) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-idonic acid and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are 5-oxo-D-gluconic acid, reduced NADH, and a proton. The enzyme can also use the alternative cofactor, nicotinamide adenine dinucleotide phosphate.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-idonate:NAD(P)+ oxidoreductase.
References
- ^ Enzyme 1.1.1.264 at KEGG Pathway Database.
- ^ Bausch C, Peekhaus N, Utz C, Blais T, Murray E, Lowary T, Conway T (1998). "Sequence analysis of the GntII (subsidiary) system for gluconate metabolism reveals a novel pathway for L-idonic acid catabolism in Escherichia coli". J. Bacteriol. 180 (14): 3704–10. doi:10.1128/JB.180.14.3704-3710.1998. PMC 107343. PMID 9658018.