| 2,5-dioxovalerate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.26 | ||||||||
| CAS no. | 37250-92-3 | ||||||||
| 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 | ||||||||
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In enzymology, a 2,5-dioxovalerate dehydrogenase (EC 1.2.1.26) is an enzyme that catalyzes the chemical reaction
- 2,5-dioxopentanoate + NADP + H2O 2-oxoglutarate + NADPH + 2 H
2-oxoglutarate + NADPH + 2 HThe 3 substrates of this enzyme are 2,5-dioxopentanoate, NADP, and H2O, whereas its 3 products are 2-oxoglutarate, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2,5-dioxopentanoate:NADP+ 5-oxidoreductase. Other names in common use include 2-oxoglutarate semialdehyde dehydrogenase, and alpha-ketoglutaric semialdehyde dehydrogenase. This enzyme participates in ascorbate and aldarate metabolism.
References
- Adams E, Rosso G (April 1967). "Alpha-ketoglutaric semialdehyde dehydrogenase of Pseudomonas. Properties of the purified enzyme induced by hydroxyproline and of the glucarate-induced and constitutive enzymes". The Journal of Biological Chemistry. 242 (8): 1802–14. PMID 6024771.
| Aldehyde/oxo oxidoreductases (EC 1.2) | |
|---|---|
| 1.2.1: NAD or NADP | |
| 1.2.2: cytochrome | |
| 1.2.3: oxygen | |
| 1.2.4: disulfide | |
| 1.2.7: iron–sulfur protein | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
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