• Title of article

    Moraxella catarrhalis Lgt2, a galactosyltransferase with broad acceptor substrate specificity Original Research Article

  • Author/Authors

    Isabelle Faglin، نويسنده , , Jennifer C. Wilson، نويسنده , , Joe Tiralongo، نويسنده , , Ian R. Peak، نويسنده ,

  • Issue Information
    دوهفته نامه با شماره پیاپی سال 2010
  • Pages
    6
  • From page
    2151
  • To page
    2156
  • 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 Lgt2B/C. The lgt2B/C gene was amplified from M. catarrhalis, expressed in Escherichia coli, and Lgt2B/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 Lgt2B/C is a galactosyltransferase with relatively broad acceptor specificity with optimal activity in the presence of exogenous Mg2+.
  • Keywords
    Glycosyltransferase , Lipopolysaccharide , Moraxella catarrhalis , Galactosyltransferase , Biosynthesis
  • Journal title
    Carbohydrate Research
  • Serial Year
    2010
  • Journal title
    Carbohydrate Research
  • Record number

    966728