Biochemical analysis of Lgt3, a glycosyltransferase of the bacterium Moraxella catarrhalis

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Title Biochemical analysis of Lgt3, a glycosyltransferase of the bacterium Moraxella catarrhalis
Author Faglin, Isabelle; Tiralongo, Joe; Wilson, Jenny; Collins, Patrick; Peak, Ian
Journal Name Biochemical and Biophysical Research Communications
Year Published 2010
Place of publication United States
Publisher Elsevier
Abstract The lipooligosaccharide (LOS) of Moraxella catarrhalis is unusual in that it lacks heptose. The sugar linking oligosaccharide to Lipid A is a trisubstituted glucose. A single enzyme, Lgt3, is suggested to trisubstitute this core sugar. The lgt3 gene encodes two distinct domains with high similarity to glucosyltransferases of the GT-A superfamily, thus encoding a bidomain, multifunctional glucosyltransferase. To characterise Lgt3, the gene was amplified from M. catarrhalis, expressed in Escherichia coli, and purified. Analysis of its glycosyltransferase catalytic activity ascertained the pH and temperature optima for Lgt3. The donor specificity and acceptor specificity were examined. This study confirms that Lgt3 is a glucosyltransferase which catalyses addition of glucose to its cognate receptor, a terminal glucose presented as the core region of LOS.
Peer Reviewed Yes
Published Yes
Alternative URI http://dx.doi.org/10.1016/j.bbrc.2010.02.028
Volume 393
Issue Number 4
Page from 609
Page to 613
ISSN 0006-291X
Date Accessioned 2010-06-02
Date Available 2012-02-10T02:05:17Z
Language en_US
Research Centre Institute for Glycomics
Faculty Faculty of Science, Environment, Engineering and Technology
Subject Enzymes
URI http://hdl.handle.net/10072/33169
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1

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