Source:http://linkedlifedata.com/resource/pubmed/id/18491328
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2008-6-26
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pubmed:abstractText |
Helicobacter pylori is a highly persistent and common pathogen in humans. It is the causative agent of chronic gastritis and its further stages. HP0826 is the beta-1,4-galactosyltransferase involved in the biosynthesis of the LPS O-chain backbone of H. pylori. 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 H. pylori 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-beta-S-1,4-GlcNAc-pNP as well as Gal-beta-1,4-Man-pNP. We further show that Neisseria meningitidis beta-1,4-galactosyltransferases 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-beta-1,4-Man linkage is found in the Leishmania species LPG backbone disaccharide repeats and cap, which have been associated with vector binding in Leishmaniasis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Disaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetyllactosamine Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Thioglycosides
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1439-7633
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
2
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1632-40
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pubmed:meshHeading |
pubmed-meshheading:18491328-Bacterial Proteins,
pubmed-meshheading:18491328-Catalysis,
pubmed-meshheading:18491328-Disaccharides,
pubmed-meshheading:18491328-Escherichia coli,
pubmed-meshheading:18491328-Escherichia coli Proteins,
pubmed-meshheading:18491328-Helicobacter pylori,
pubmed-meshheading:18491328-Hydrogen-Ion Concentration,
pubmed-meshheading:18491328-Kinetics,
pubmed-meshheading:18491328-Models, Molecular,
pubmed-meshheading:18491328-N-Acetyllactosamine Synthase,
pubmed-meshheading:18491328-Thioglycosides
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pubmed:year |
2008
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pubmed:articleTitle |
A beta-1,4-galactosyltransferase from Helicobacter pylori is an efficient and versatile biocatalyst displaying a novel activity for thioglycoside synthesis.
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pubmed:affiliation |
Institute for Biological Sciences, National Research Council Canada, 100 Sussex Drive, Ottawa, ON K1A0R6, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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