| N-acetylhexosamine 1-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.240 | ||||||||
| CAS no. | 122785-18-6 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a N-acetylhexosamine 1-dehydrogenase (EC 1.1.1.240) is an enzyme that catalyzes the chemical reaction
- N-acetyl-D-glucosamine + NAD+ N-acetyl-D-glucosaminate + NADH + H+
Thus, the two substrates of this enzyme are N-acetyl-D-glucosamine and NAD+, whereas its 3 products are N-acetyl-D-glucosaminate, 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 N-acetyl-D-hexosamine:NAD+ 1-oxidoreductase. Other names in common use include N-acetylhexosamine dehydrogenase, and N-acetyl-D-hexosamine dehydrogenase.
References
- Horiuchi T, Kurokawa T (1989). "Purification and characterization of N-acetyl-D-hexosamine dehydrogenase from Pseudomonas sp no 53". Agric. Biol. Chem. 53 (7): 1919–1925. doi:10.1271/bbb1961.53.1919.
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