2,5-didehydrogluconate reductase
| 2,5-didehydrogluconate reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.274 | ||||||||
| CAS no. | 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, a 2,5-didehydrogluconate reductase (EC 1.1.1.274) is an enzyme that catalyzes the chemical reaction
- 2-dehydro-D-gluconate + NADP+ 2,5-didehydro-D-gluconate + NADPH + H+
Thus, the two substrates of this enzyme are 2-dehydro-D-gluconate and NADP+, whereas its 3 products are 2,5-didehydro-D-gluconate, 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 2-dehydro-D-gluconate:NADP+ 2-oxidoreductase. Other names in common use include 2,5-diketo-D-gluconate reductase, and YqhE reductase.
Structural studies
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1VP5.
References
[edit]- Yum DY, Lee BY, Pan JG (1999). "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. Bibcode:1999ApEnM..65.3341Y. doi:10.1128/AEM.65.8.3341-3346.1999. PMC 91502. PMID 10427017.
- Yum DY, Lee BY, Hahm DH, Pan JG (1998). "The yiaE gene, located at 80.1 minutes on the Escherichia coli chromosome, encodes a 2-ketoaldonate reductase". J. Bacteriol. 180 (22): 5984–8. doi:10.1128/JB.180.22.5984-5988.1998. PMC 107674. PMID 9811658.
- Habrych M, Rodriguez S, Stewart JD (2002). "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. doi:10.1021/bp0101841. PMID 11934293. S2CID 23141855.
