L-gulonate 3-dehydrogenase
| L-gulonate 3-dehydrogenase | |||||||||
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| Identifiers | |||||||||
| EC no. | 1.1.1.45 | ||||||||
| CAS no. | 9028-51-7 | ||||||||
| 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 L-gulonate 3-dehydrogenase (EC 1.1.1.45) is an enzyme that catalyzes the chemical reaction
- L-gulonate + NAD+ 3-dehydro-L-gulonate + NADH + H+
Thus, the two substrates of this enzyme are L-gulonate and NAD+, whereas its 3 products are 3-dehydro-L-gulonate, NADH, 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 L-gulonate:NAD+ 3-oxidoreductase. Other names in common use include L-3-aldonate dehydrogenase, L-3-aldonic dehydrogenase, L-gulonic acid dehydrogenase, L-beta-hydroxyacid dehydrogenase, L-beta-hydroxy-acid-NAD+-oxidoreductase, and L-3-hydroxyacid dehydrogenase. This enzyme participates in pentose and glucuronate interconversions.
Structural studies
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2DPO.
References
[edit]- Dworsky P, Hoffmann-Ostenhof O (1964). "L-3-Aldonic acid dehydrogenase from Schwanniomyces occidentalis". Acta Biochim. Pol. 11: 269–277.
- Smiley JD, Ashwell G (1961). "Purification and properties of beta-L-hydroxy acid dehydrogenase II. Isolation of beta-keto-L-gluconic acid, an intermediate in L-xylulose biosynthesis". J. Biol. Chem. 236: 357–364. doi:10.1016/S0021-9258(18)64367-4.
