| N-acylmannosamine 1-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.233 | ||||||||
| CAS no. | 117698-08-5 | ||||||||
| 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-acylmannosamine 1-dehydrogenase (EC 1.1.1.233) is an enzyme that catalyzes the chemical reaction
- N-acyl-D-mannosamine + NAD+ N-acyl-D-mannosaminolactone + NADH + H+
Thus, the two substrates of this enzyme are N-acyl-D-mannosamine and NAD+, whereas its 3 products are N-acyl-D-mannosaminolactone, 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-acyl-D-mannosamine:NAD+ 1-oxidoreductase. Other names in common use include N-acylmannosamine dehydrogenase, N-acetyl-D-mannosamine dehydrogenase, N-acyl-D-mannosamine dehydrogenase, and N-acylmannosamine dehydrogenase.
References
- Horiuchi T, Kurokawa T (September 1988). "Purification and properties of N-acyl-D-mannosamine dehydrogenase from Flavobacterium sp. 141-8". J. Biochem. Tokyo. 104 (3): 466–71. PMID 3240988.
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