fructose 5-dehydrogenase (NADP) | |||||||||
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Identifiers | |||||||||
EC no. | 1.1.1.124 | ||||||||
CAS no. | 37250-53-6 | ||||||||
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 fructose 5-dehydrogenase (NADP) (EC 1.1.1.124) is an enzyme that catalyzes the chemical reaction
- D-fructose + NADP 5-dehydro-D-fructose + NADPH + H
Thus, the two substrates of this enzyme are D-fructose and NADP, whereas its 3 products are 5-dehydro-D-fructose, 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-fructose:NADP 5-oxidoreductase. Other names in common use include 5-ketofructose reductase (NADP), 5-keto-D-fructose reductase (NADP), fructose 5-(nicotinamide adenine dinucleotide phosphate), dehydrogenase, D-(-)fructose:(NADP) 5-oxidoreductase, and fructose 5-dehydrogenase (NADP).
References
- Ameyama M, Matsushita K, Shinagawa E, Adachi O (1981). "5-keto-D-Fructose reductase of Gluconobacter industrius Purification, crystallization and properties". Agric. Biol. Chem. 45 (4): 863–869. doi:10.1271/bbb1961.45.863.
- Avigad G, Englard S, Pifko S (1966). "5-Keto-D-fructose. IV. A specific reduced nicotinamide adenine dinucleotide phosphate-linked reductase from Gluconobacter cerinus". J. Biol. Chem. 241 (2): 373–8. PMID 4379259.
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