title: Moraxella catarrhalis Lgt2, a galactosyltransferase with broad acceptor substrate specificity.
abstract: The genetic basis of lipo-oligosaccharide (LOS) biosynthesis for the bacterium Moraxella catarrhalis has been elucidated and functions suggested for each of the glycosyltransferases. In this study we have expressed and characterised one of these enzymes, the putative galactosyltransferase Lgt2(B/C). The lgt2(B/C) gene was amplified from M. catarrhalis, expressed in Escherichia coli, and Lgt2(B/C) was purified. Analysis of its glycosyltransferase catalytic activity ascertained the pH and temperature optima. The donor specificity and acceptor specificity were examined and they showed that Lgt2(B/C) is a galactosyltransferase with relatively broad acceptor specificity with optimal activity in the presence of exogenous Mg(2+).
authors.affiliation: Institute for Glycomics, Griffith University, Gold Coast Campus, Southport, QLD 4222, Australia.
authors.forename: Isabelle
authors.initials: I
authors.lastname: Faglin
authors.forename: Jennifer C
authors.initials: JC
authors.lastname: Wilson
authors.forename: Joe
authors.initials: J
authors.lastname: Tiralongo
authors.forename: Ian R
authors.initials: IR
authors.lastname: Peak
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D005700:Galactosyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D001936:Moraxella catarrhalis / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D005700:Galactosyltransferases