UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase

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spinqualitylabelsall models E. coli UDP-N-acetylglucosamine acyltransferase complex with UDP-Glc-NAC (PDB code 6uec) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (LpxD) is involved in the biosynthesis of lipid A which is a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Thus, LpxD is essential to survival of Gram-negative bacteria. It catalyzes the N-acylation of UDP-3-O-(3-hydroxytetradeanoyl)glucosamine[1]. Relevance LpxD inhibitors are antimicrobials[2]. 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[3].

3D structures of UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase

Updated on 28-January-2021

References

1. ↑ Bainbridge BW, Karimi-Naser L, Reife R, Blethen F, Ernst RK, Darveau RP. Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis. J Bacteriol. 2008 Jul;190(13):4549-58. doi: 10.1128/JB.00234-08. Epub 2008 May 2. PMID:18456814 doi:http://dx.doi.org/10.1128/JB.00234-08
2. ↑ Jenkins RJ, Dotson GD. Dual targeting antibacterial peptide inhibitor of early lipid A biosynthesis. ACS Chem Biol. 2012 Jul 20;7(7):1170-7. doi: 10.1021/cb300094a. Epub 2012 Apr 27. PMID:22530734 doi:http://dx.doi.org/10.1021/cb300094a
3. ↑ 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