Gluconate 5-dehydrogenase

Last updated
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, gluconate 5-dehydrogenase (EC 1.1.1.69) is an enzyme that catalyzes the chemical reaction

+ NAD+
 
 
 
H+
Gluconate 5-dehydrogenase
 
H+
 
+ NADH
 

The two substrates of this enzyme are D-gluconic acid and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are 5-oxo-D-gluconic acid, reduced NADH, and a proton. The enzyme can use nicotinamide adenine dinucleotide phosphate as an alternative cofactor. [1] [2] [3] [4]

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

  1. Enzyme 1.1.1.69 at KEGG Pathway Database.
  2. 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.
  3. 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.
  4. 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.