L-threonate 3-dehydrogenase
| L-threonate 3-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.129 | ||||||||
| CAS no. | 37250-59-2 | ||||||||
| 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, L-threonate 3-dehydrogenase (EC 1.1.1.129) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are threonic acid and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are 3-dehydro-L-threonic acid, reduced NADH, and a proton.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-threonate:NAD+ 3-oxidoreductase. Other names in common use include threonate dehydrogenase, and L-threonic acid dehydrogenase. This enzyme participates in ascorbate and aldarate metabolism.
References
- ^ Enzyme 1.1.1.129 at KEGG Pathway Database.
- ^ Aspen AJ, Jakoby WB (1964). "L-threonic Acid Dehydrogenase: Purification and Properties". J. Biol. Chem. 239 (3): 710–3. doi:10.1016/S0021-9258(18)51644-6. PMID 14154441.