UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining)
| UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.2.1.135 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining) (EC 4.2.1.135, PglF) is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine hydro-lyase (configuration-retaining; UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose-forming).[1][2] This enzyme catalyses the following chemical reaction
- UDP-N-acetyl-alpha-D-glucosamine UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + H2O
This enzyme contains NAD+ as a cofactor.
References
- ↑ Schoenhofen, I.C.; McNally, D.J.; Vinogradov, E.; Whitfield, D.; Young, N.M.; Dick, S.; Wakarchuk, W.W.; Brisson, J.R.; Logan, S.M. (2006). "Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways". J. Biol. Chem. 281: 723–732. doi:10.1074/jbc.m511021200. PMID 16286454.
- ↑ Olivier, N.B.; Chen, M.M.; Behr, J.R.; Imperiali, B. (2006). "In vitro biosynthesis of UDP-N,N′-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system". Biochemistry. 45: 13659–13669. doi:10.1021/bi061456h. PMC 2542654. PMID 17087520.
External links
- UDP-N-acetylglucosamine+4,6-dehydratase+(configuration-retaining) at the US National Library of Medicine Medical Subject Headings (MeSH)
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