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Moraxella catarrhalis Lgt2, a galactosyltransferase with broad acceptor substrate specificity

机译:卡他莫拉氏菌Lgt2,具有广泛的受体底物特异性的半乳糖基转移酶

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摘要

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+).
机译:卡他莫拉氏菌细菌的脂寡糖(LOS)生物合成的遗传基础已经阐明,并建议了每种糖基转移酶的功能。在这项研究中,我们已经表达并鉴定了其中一种酶,即假定的半乳糖基转移酶Lgt2_(B / C)。从粘膜炎莫拉氏菌中扩增出lgt2_(B / C)基因,在大肠杆菌中表达,并纯化了Lgt2_(B / C)。分析其糖基转移酶的催化活性确定了最适的pH和温度。检查了供体特异性和受体特异性,结果表明Lgt2_(B / C)是一种半乳糖基转移酶,在外源Mg〜(2+)存在下具有相对较宽的受体特异性和最佳活性。

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