CATH Domain 3u1yA01

Superfamily	lpxc deacetylase, domain 1
Functional Family	UDP-3-O-acyl-N-acetylglucosamine deacetylase

3.5.1.108

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

based on mapping to UniProt P47205

UDP-3-O-((3R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine + H(2)O = UDP-3-O-((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + acetate.

-!- The enzyme catalyzes a committed step in the biosynthesis of lipid A. -!- Formerly EC 3.5.1.n1.

LPXC_PSEAE

Pseudomonas aeruginosa PAO1

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

PDB	3U1Y
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Potent inhibitors of LpxC for the treatment of Gram-negative infections. Brown, M.F., Reilly, U., Abramite, J.A., Arcari, J.T., Oliver, R., Barham, R.A., Che, Y., Chen, J.M., Collantes, E.M., Chung, S.W., Desbonnet, C., Doty, J., Doroski, M., Engtrakul, J.J., Harris, T.M., Huband, M., Knafels, J.D., Leach, K.L., Liu, S., Marfat, A., Marra, A., McElroy, E., Melnick, M., Menard, C.A., Montgomery, J.I., Mullins, L., Noe, M.C., O'Donnell, J., Penzien, J., Plummer, M.S., Price, L.M., Shanmugasundaram, V., Thoma, C., Uccello, D.P., Warmus, J.S., Wishka, D.G. J.Med.Chem.