In enzymology, a glucose 1-dehydrogenase (NAD+) (EC 1.1.1.118) is an enzyme that catalyzes the chemical reaction
| glucose 1-dehydrogenase (NAD+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.118 | ||||||||
| CAS no. | 37250-49-0 | ||||||||
| 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 | ||||||||
| |||||||||
- D-glucose + NAD+ D-glucono-1,5-lactone + NADH + H+
Thus, the two substrates of this enzyme are D-glucose and NAD+, whereas its 3 products are D-glucono-1,5-lactone, 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 D-glucose:NAD+ 1-oxidoreductase. Other names in common use include D-glucose:NAD+ oxidoreductase, D-aldohexose dehydrogenase, and glucose 1-dehydrogenase (NAD+).
Structural studies edit
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2DTD, 2DTE, and 2DTX.
References edit
- Hu AS, Cline AL (November 1964). "The regulation of some sugar dehydrogenases in a pseudomonad". Biochimica et Biophysica Acta (BBA) - General Subjects. 93 (2): 237–45. doi:10.1016/0304-4165(64)90371-x. PMID 14251301.
