UDP-3-O-acyl-N-acetylglucosamine deacetylase

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 UDP-3-O-[(3R)-3-hydroxymyristoyl]-D-glucosamine + acetate
UDP-3-O-acyl-N-acetylglucosamine deacetylase
Identifiers
EC number3.5.1.108
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

This zinc protein participates in biosynthesis of lipid A.

References
  1. Hernick M, Gennadios HA, Whittington DA, Rusche KM, Christianson DW, Fierke CA (April 2005). "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. doi:10.1074/jbc.M413560200. PMID 15705580.
  2. Jackman JE, Raetz CR, Fierke CA (February 1999). "UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme". Biochemistry. 38 (6): 1902–11. doi:10.1021/bi982339s. PMID 10026271.
  3. Hyland SA, Eveland SS, Anderson MS (March 1997). "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. doi:10.1128/jb.179.6.2029-2037.1997. PMC 178929. PMID 9068651.
  4. Wang W, Maniar M, Jain R, Jacobs J, Trias J, Yuan Z (March 2001). "A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase". Analytical Biochemistry. 290 (2): 338–46. doi:10.1006/abio.2000.4973. PMID 11237337.
  5. Whittington DA, Rusche KM, Shin H, Fierke CA, Christianson DW (July 2003). "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. doi:10.1073/pnas.1432990100. PMC 166197. PMID 12819349.
  6. Mochalkin I, Knafels JD, Lightle S (March 2008). "Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor". Protein Science. 17 (3): 450–7. doi:10.1110/ps.073324108. PMC 2248309. PMID 18287278.
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