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.
YouTube Encyclopedic
-
1/1Views:5 729
-
Kristala L. J. Prather (MIT) Part 2: Teaching an Old Bacterium New Tricks
Transcription
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1VL8.
References
- Ameyama M; Adachi O (1982). "5-Keto-D-gluconate reductase from Gluconobacter suboxydans". Methods Enzymol. Methods in Enzymology. 89: 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. Tokyo. 53 (6): 448–52. doi:10.1093/oxfordjournals.jbchem.a127721. PMID 13939777.