Acyl-acyl carrier protein specificity of UDP-GlcNAc acyltransferases from gram-negative bacteria: relationship to lipid A structure

Author:

Williamson J M1,Anderson M S1,Raetz C R1

Affiliation:

1. Department of Biochemistry, Merck Sharp & Dohme Research Laboratories, Rahway, New Jersey 07065.

Abstract

Lipid A, the component of lipopolysaccharide that provides the membrane anchor of the core and O-antigen sugars, is known to contain characteristic R-3-hydroxy fatty acids bound to the 2,2' (N-linked) and 3,3' (O-linked) positions of the glucosamine disaccharide in different gram-negative bacteria. The studies reported here show that it is the acyl-acyl carrier protein specificities of the enzymes UDP-GlcNAc-O-acyltransferase and UDP-3-O-[(R)-3-hydroxyacyl]-GlcN-N-acyltransferase that determine the nature of these fatty acids.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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