| glucose 1-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Glucose dehydrogenase tetramer, Caenorhabditis Elegans | |||||||||
| Identifiers | |||||||||
| EC no. | 1.1.1.47 | ||||||||
| CAS no. | 9028-53-9 | ||||||||
| 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, glucose 1-dehydrogenase (EC 1.1.1.47) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are β-D-glucose and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are D-glucono-1,5-lactone, reduced NADH, and a proton. The enzyme can alternatively use nicotinamide adenine dinucleotide phosphate (NADP+) for oxidation and in that case produces NADPH. [1]
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 beta-D-glucose:NAD(P)+ 1-oxidoreductase. Another name in common use is D-glucose dehydrogenase (NAD(P)+).
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1G6K, 1GCO, 1GEE, 1RWB, 1SPX, 2B5V, 2B5W, 2CD9, and 2CDA.