Function
UDP-N-acetylglucosamine acyltransferase or
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (LpxA) initiates lipid A biosynthesis. It catalyzes the transfer of 3-hydroxymyristic acid from acyl carrier protein to the 3'-hydroxyl group of UDP-GlcNAc[1].
Structural highlights
The of LpxA interacts with the substrate UDP moiety and the Glc-NAc moiety. It contains a where the His acts as a general base and Asp helps to orient the His for participation in the catalysis[2].
3D structures of UDP-N-acetylglucosamine acyltransferase
UDP-N-acetylglucosamine acyltransferase 3D structures
References
- ↑ Wyckoff TJ, Raetz CR. The active site of Escherichia coli UDP-N-acetylglucosamine acyltransferase. Chemical modification and site-directed mutagenesis. J Biol Chem. 1999 Sep 17;274(38):27047-55. PMID:10480918
- ↑ Ulaganathan V, Buetow L, Hunter WN. Nucleotide substrate recognition by UDP-N-acetylglucosamine acyltransferase (LpxA) in the first step of lipid A biosynthesis. J Mol Biol. 2007 Jun 1;369(2):305-12. Epub 2007 Mar 21. PMID:17434525 doi:10.1016/j.jmb.2007.03.039
