Biology:UDP-3-O-acyl-N-acetylglucosamine deacetylase
From HandWiki
| UDP-3-O-acyl-N-acetylglucosamine deacetylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.1.108 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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UDP-3-O-acyl-N-acetylglucosamine deacetylase (EC 3.5.1.108, LpxC protein, LpxC enzyme, LpxC deacetylase, deacetylase LpxC, UDP-3-O-acyl-GlcNAc deacetylase, UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase, UDP-(3-O-acyl)-N-acetylglucosamine deacetylase, UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase, UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase) is an enzyme with systematic name UDP-3-O-((3R)-3-hydroxymyristoyl)-N-acetylglucosamine amidohydrolase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine + H2O [math]\displaystyle{ \rightleftharpoons }[/math] UDP-3-O-[(3R)-3-hydroxymyristoyl]-D-glucosamine + acetate
This zinc protein participates in biosynthesis of lipid A.
References
- ↑ "UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism". The Journal of Biological Chemistry 280 (17): 16969–78. April 2005. doi:10.1074/jbc.M413560200. PMID 15705580.
- ↑ "UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme". Biochemistry 38 (6): 1902–11. February 1999. doi:10.1021/bi982339s. PMID 10026271.
- ↑ "Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway". Journal of Bacteriology 179 (6): 2029–37. March 1997. doi:10.1128/jb.179.6.2029-2037.1997. PMID 9068651.
- ↑ "A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase". Analytical Biochemistry 290 (2): 338–46. March 2001. doi:10.1006/abio.2000.4973. PMID 11237337.
- ↑ "Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis". Proceedings of the National Academy of Sciences of the United States of America 100 (14): 8146–50. July 2003. doi:10.1073/pnas.1432990100. PMID 12819349. Bibcode: 2003PNAS..100.8146W.
- ↑ "Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor". Protein Science 17 (3): 450–7. March 2008. doi:10.1110/ps.073324108. PMID 18287278.
External links
- UDP-3-O-acyl-N-acetylglucosamine+deacetylase at the US National Library of Medicine Medical Subject Headings (MeSH)
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