Biology:Glucose 1-dehydrogenase (NAD+)
From HandWiki
glucose 1-dehydrogenase (NAD+) | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 1.1.1.118 | ||||||||
CAS number | 37250-49-0 | ||||||||
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 (NAD+) (EC 1.1.1.118) is an enzyme that catalyzes the chemical reaction
- D-glucose + NAD+ [math]\displaystyle{ \rightleftharpoons }[/math] D-glucono-1,5-lactone + NADH + H+
Thus, the two substrates of this enzyme are D-glucose and NAD+, whereas its 3 products are D-glucono-1,5-lactone, NADH, 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:NAD+ 1-oxidoreductase. Other names in common use include D-glucose:NAD+ oxidoreductase, D-aldohexose dehydrogenase, and glucose 1-dehydrogenase (NAD+).
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2DTD, 2DTE, and 2DTX.
References
- "The regulation of some sugar dehydrogenases in a pseudomonad". Biochimica et Biophysica Acta (BBA) - General Subjects 93 (2): 237–45. November 1964. doi:10.1016/0304-4165(64)90371-x. PMID 14251301.
Original source: https://en.wikipedia.org/wiki/Glucose 1-dehydrogenase (NAD+).
Read more |