In enzymology, a L-gulonate 3-dehydrogenase (EC 1.1.1.45) is an enzyme that catalyzes the chemical reaction
| 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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- 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
editAs 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.
