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

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

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 \rightleftharpoons UDP-3-O-[(3R)-3-hydroxymyristoyl]-D-glucosamine + acetate

This zinc protein participates in biosynthesis of lipid A.

References

  1. Hernick, M., Gennadios, H.A., Whittington, D.A., Rusche, K.M., Christianson, D.W. and Fierke, C.A. (2005). "UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism". J. Biol. Chem. 280 (17): 16969–16978. doi:10.1074/jbc.M413560200. PMID 15705580.
  2. Jackman, J.E., Raetz, C.R. and Fierke, C.A. (1999). "UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme". Biochemistry 38 (6): 1902–1911. doi:10.1021/bi982339s. PMID 10026271.
  3. Hyland, S.A., Eveland, S.S. and Anderson, M.S. (1997). "Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway". J. Bacteriol. 179 (6): 2029–2037. PMID 9068651.
  4. Wang, W., Maniar, M., Jain, R., Jacobs, J., Trias, J. and Yuan, Z. (2001). "A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase". Anal. Biochem. 290 (2): 338–346. doi:10.1006/abio.2000.4973. PMID 11237337.
  5. Whittington, D.A., Rusche, K.M., Shin, H., Fierke, C.A. and Christianson, D.W. (2003). "Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis". Proc. Natl. Acad. Sci. USA 100: 8146–8150. doi:10.1073/pnas.1432990100. PMC 166197. PMID 12819349.
  6. Mochalkin, I., Knafels, J.D. and Lightle, S. (2008). "Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor". Protein Sci. 17 (3): 450–457. doi:10.1110/ps.073324108. PMID 18287278.

External links

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