EC 3.5.1.108 - UDP-3-O-acyl-N-acetylglucosamine deacetylase

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IntEnz Enzyme Nomenclature
EC 3.5.1.108

Names

Accepted name:
UDP-3-O-acyl-N-acetylglucosamine deacetylase
Other names:
UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase
UDP-3-O-acyl-GlcNAc deacetylase
LpxC
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
LpxC 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
LpxC enzyme
deacetylase LpxC
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine amidohydrolase
Systematic name:
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-α-D-glucosamine amidohydrolase

Reaction

Cofactor

Comments:

A zinc protein. The enzyme catalyses a committed step in the biosynthesis of lipid A.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008759 , GO:0103117
UniProtKB/Swiss-Prot: (324) [show] [UniProt]

References

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

[EC 3.5.1.108 created 2010]