glucose 1-dehydrogenase (NADP) | |||||||||
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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 | ||||||||
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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.
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