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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a gluconate 5-dehydrogenase (EC 1.1.1.69) is an enzyme that catalyzes the chemical reaction

D-gluconate + NAD(P)⁺${\displaystyle \rightleftharpoons }$ 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

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 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.