Biology:2,5-didehydrogluconate reductase
| 2,5-didehydrogluconate reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.1.274 | ||||||||
| CAS number | 95725-95-4 | ||||||||
| 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, 2,5-didehydrogluconate reductase (EC 1.1.1.274) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The two substrates of this enzyme are 2-dehydro-D-gluconic acid and oxidised nicotinamide adenine dinucleotide phosphate (NADP+). Its products are 2,5-didehydro-D-gluconic acid, reduced NADPH, and a proton.[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 2-dehydro-D-gluconate:NADP+ 2-oxidoreductase. Other names in common use include 2,5-diketo-D-gluconate reductase, and YqhE reductase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1VP5.
References
- ↑ Enzyme 1.1.1.274 at KEGG Pathway Database.
- ↑ "Identification of the yqhE and yafB genes encoding two 2, 5-diketo-D-gluconate reductases in Escherichia coli". Appl. Environ. Microbiol. 65 (8): 3341–6. 1999. doi:10.1128/AEM.65.8.3341-3346.1999. PMID 10427017. Bibcode: 1999ApEnM..65.3341Y.
- ↑ "The yiaE gene, located at 80.1 minutes on the Escherichia coli chromosome, encodes a 2-ketoaldonate reductase". J. Bacteriol. 180 (22): 5984–8. 1998. doi:10.1128/JB.180.22.5984-5988.1998. PMID 9811658.
- ↑ "Purification and identification of an Escherichia coli beta-keto ester reductase as 2,5-diketo-D-gluconate reductase YqhE". Biotechnol. Prog. 18 (2): 257–61. 2002. doi:10.1021/bp0101841. PMID 11934293.
 |  |
