Cloning and characterization of the Escherichia coli Heptosyltransferase III: Exploring substrate specificity in lipopolysaccharide core biosynthesis
- PMID: 25957775
- DOI: 10.1016/j.febslet.2015.04.051
Cloning and characterization of the Escherichia coli Heptosyltransferase III: Exploring substrate specificity in lipopolysaccharide core biosynthesis
Abstract
Bacterial lipopolysaccharide (LPS) molecules are an important cell surface component that enables adhesion to surfaces and cell motility, amongst other functions. In Escherichia coli, there are multiple Heptosyltransferase enzymes involved in the biosynthesis of the core region of LPS. Here we describe the first ever cloning, expression, purification and characterization of Heptosyltransferase III (HepIII) from E. coli, which catalyzes the addition of an L-glycero-D-manno-heptose (Hep) residue to the growing LPS core via an α(1→7) bond. Inspired by results from our lab on the E. coli HepI, we assessed the catalytic efficiency with phospho-Hep2-Kdo2-Lipid A (PH2K2LA) and two deacylated analogues.
Keywords: Bacterial biofilms; Core oligosaccharide; Glycosyltransferase; Heptosyltransferase; Lipopolysaccharide biosynthesis.
Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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