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HP0826 is the \u03b2\u20101,4\u2010galactosyltransferase involved in the biosynthesis of the LPS O\u2010chain backbone of <jats:italic>H. pylori<\/jats:italic>. Though it was first cloned nearly a decade ago, there are surprisingly limited data about the characteristics of HP0826, especially given its prominent role in <jats:italic>H. pylori<\/jats:italic> pathogenicity. We here demonstrate that HP0826 is a highly efficient and promiscuous biocatalyst. We have exploited two novel enzymatic activities for the quantitative synthesis of the thiodisaccharide Gal\u2010\u03b2\u2010<jats:italic>S<\/jats:italic>\u20101,4\u2010GlcNAc\u2010<jats:italic>p<\/jats:italic>NP as well as Gal\u2010\u03b2\u20101,4\u2010Man\u2010<jats:italic>p<\/jats:italic>NP. We further show that <jats:italic>Neisseria meningitidis<\/jats:italic> \u03b2\u20101,4\u2010galactosyltransferases LgtB can be used as an equally efficient catalyst in the latter reaction. Thiodisaccharides have been extensively used in structural biology but can also have therapeutic uses. The Gal\u2010\u03b2\u20101,4\u2010Man linkage is found in the <jats:italic>Leishmania<\/jats:italic> species LPG backbone disaccharide repeats and cap, which have been associated with vector binding in Leishmaniasis.<\/jats:p>","DOI":"10.1002\/cbic.200700775","type":"journal-article","created":{"date-parts":[[2008,5,19]],"date-time":"2008-05-19T11:19:40Z","timestamp":1211195980000},"page":"1632-1640","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":41,"title":["A \u03b2\u20101,4\u2010Galactosyltransferase from <i>Helicobacter pylori<\/i> is an Efficient and Versatile Biocatalyst Displaying a Novel Activity for Thioglycoside 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