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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Faglin I,Tiralongo J,Wilson JC,Collins PM,Peak IR

doi

10.1016/j.bbrc.2010.02.028

subject

Has Abstract

pub_date

2010-03-19 00:00:00

pages

609-13

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(10)00239-1

journal_volume

393

pub_type

杂志文章

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