Gluconate 5-dehydrogenase
| gluconate 5-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.69 | ||||||||
| CAS no. | 9028-70-0 | ||||||||
| 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 gluconate 5-dehydrogenase (EC 1.1.1.69) is an enzyme that catalyzes the chemical reaction
- D-gluconate + NAD(P)+ 5-dehydro-D-gluconate + NAD(P)H + H+
The 3 substrates of this enzyme are D-gluconate, NAD+, and NADP+, whereas its 4 products are 5-dehydro-D-gluconate, NADH, NADPH, and H+.
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 D-gluconate:NAD(P)+ 5-oxidoreductase. Other names in common use include 5-keto-D-gluconate 5-reductase, 5-keto-D-gluconate 5-reductase, 5-ketogluconate 5-reductase, 5-ketogluconate reductase, and 5-keto-D-gluconate reductase.
Structural studies
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1VL8.
References
[edit]- Ameyama M; Adachi O (1982). "5-Keto-d-gluconate reductase from Gluconobacter su☐ydans". Carbohydrate Metabolism - Part D. Methods in Enzymology. Vol. 89. pp. 198–202. doi:10.1016/S0076-6879(82)89035-6. ISBN 978-0-12-181989-7.
- Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM (2006). "A proteomic analysis of arsenical drug resistance in Trypanosoma brucei". Proteomics. 6 (9): 2726–32. doi:10.1002/pmic.200500419. PMID 16526094. S2CID 24074942.
- Okamoto K (1963). "Enzymic studies on the formation of 5-ketogluconic acid by Acetobacter suboxydans. II. 5-Ketogluconate reductase". J. Biochem. 53 (6). Tokyo: 448–52. doi:10.1093/oxfordjournals.jbchem.a127721. PMID 13939777.
