| glucose 1-dehydrogenase (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.119 | ||||||||
| CAS no. | 37250-50-3 | ||||||||
| 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, a glucose 1-dehydrogenase (NADP+) ( EC 1.1.1.119) is an enzyme that catalyzes the chemical reaction
- D-glucose + NADP+ D-glucono-1,5-lactone + NADPH + H+
Thus, the two substrates of this enzyme are D-glucose and NADP+, whereas its 3 products are D-glucono-1,5-lactone, NADPH, 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:NADP+ 1-oxidoreductase. Other names in common use include nicotinamide adenine dinucleotide phosphate-linked aldohexose, dehydrogenase, NADP+-linked aldohexose dehydrogenase, NADP+-dependent glucose dehydrogenase, and glucose 1-dehydrogenase (NADP+).
References
- Adachi O; Ameyama M (1982). "D-Glucose dehydrogenase from Gluconobacter su☐ydans". Carbohydrate Metabolism - Part D. Methods in Enzymology. Vol. 89. pp. 159–163. doi: 10.1016/S0076-6879(82)89028-9. ISBN 978-0-12-181989-7.
- Avigad G, Alroy Y, Englard S (1968). "Purification and properties of a nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogeanse from Gluconobacter cerinus". J. Biol. Chem. 243 (8): 1936–41. doi: 10.1016/S0021-9258(18)93531-3. PMID 4384672.
