In enzymology, a glucose 1-dehydrogenase (FAD, quinone) (EC 1.1.5.9) is an enzyme that catalyzes the chemical reaction
glucose 1-dehydrogenase (FAD, quinone) | |||||||||
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Identifiers | |||||||||
EC no. | 1.1.5.9 | ||||||||
CAS no. | 37250-84-3 | ||||||||
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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- D-glucose + a quinone D-glucono-1,5-lactone + a quinol
Thus, the two substrates of this enzyme are D-glucose and a quinone, whereas its two products are D-glucono-1,5-lactone and a quinol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is D-glucose:acceptor 1-oxidoreductase. Other names in common use include glucose dehydrogenase (Aspergillus), glucose dehydrogenase (decarboxylating), and D-glucose:(acceptor) 1-oxidoreductase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, FAD.
References
edit- Bak TG (July 1967). "Studies on glucose dehydrogenase of Aspergillus oryzae. II. Purification and physical and chemical properties". Biochimica et Biophysica Acta (BBA) - Enzymology. 139 (2): 277–93. doi:10.1016/0005-2744(67)90032-0. PMID 6034674.