Biology:UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining)
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Short description: Class of enzymes
| 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-α-Dglucosamine hydro-lyase (configuration-retaining; UDP-2-acetamido-2,6-dideoxy-α-Dxylo-hex-4-ulose-forming).[1][2] This enzyme catalyses the following chemical reaction
- UDP-N-acetyl-α-D-glucosamine [math]\displaystyle{ \rightleftharpoons }[/math] UDP-2-acetamido-2,6-dideoxy-α-D-xylo-hex-4-ulose + H2O
This enzyme contains NAD+ as a cofactor.
References
- ↑ "Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways". The Journal of Biological Chemistry 281 (2): 723–32. January 2006. doi:10.1074/jbc.m511021200. PMID 16286454.
- ↑ "In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system". Biochemistry 45 (45): 13659–69. November 2006. doi:10.1021/bi061456h. 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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