Target type: molecularfunction
Catalysis of the reaction: D-glucose + NAD+ = D-glucono-1,5-lactone + NADH. [EC:1.1.1.118, MetaCyc:GLUCOSE-1-DEHYDROGENASE-NAD+-RXN]
Glucose 1-dehydrogenase (NAD+) catalyzes the oxidation of glucose to gluconolactone, with the concomitant reduction of NAD+ to NADH. This reaction involves the transfer of two electrons and one proton from the C1 hydroxyl group of glucose to NAD+. The enzyme is a flavoprotein that utilizes flavin adenine dinucleotide (FAD) as a cofactor. FAD accepts the electrons from glucose and is then reduced to FADH2. The reduced FADH2 then transfers the electrons to NAD+, which is reduced to NADH. The gluconolactone product is a cyclic ester that can be hydrolyzed to gluconate by the enzyme gluconolactonase. The overall reaction catalyzed by glucose 1-dehydrogenase (NAD+) is therefore:
Glucose + NAD+ + H2O → Gluconate + NADH + H+
This enzyme plays an important role in the metabolism of glucose, particularly in bacteria and fungi. It is involved in the oxidation of glucose to produce energy and reducing equivalents for biosynthesis. The enzyme is also involved in the detoxification of glucose analogs, such as glucose 6-phosphate, which can inhibit cellular metabolism. Furthermore, glucose 1-dehydrogenase (NAD+) activity has been implicated in the pathogenesis of various diseases, including diabetes and cancer.'
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Protein | Definition | Taxonomy |
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GDH/6PGL endoplasmic bifunctional protein | A GDH/6PGL endoplasmic bifunctional protein that is encoded in the genome of human. [PRO:DNx, UniProtKB:O95479] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
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rucaparib | AG14447: Poly(ADP-ribose) polymerase inhibitor; structure in first source | azepinoindole; caprolactams; organofluorine compound; secondary amino compound | antineoplastic agent; EC 2.4.2.30 (NAD(+) ADP-ribosyltransferase) inhibitor |