rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
8
|
pubmed:dateCreated |
2008-8-11
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pubmed:abstractText |
Site-directed mutagenesis of the glucansucrase gtf180 gene from Lactobacillus reuteri strain 180 was used to transform the active site region. The alpha-D-glucan ( mEPS-PNNS) produced by the triple mutant V1027P:S1137N:A1139S differed in structure from that of the wild-type alpha-D-glucan ( EPS180). Besides (alpha1-->3) and (alpha1-->6) linkages, as present in EPS180, mEPS-PNNS also contained (alpha1-->4) linkages. Linkage analysis, periodate oxidation, and 1D/2D (1)H NMR spectroscopy of the intact mEPS-PNNS, as well as MS and NMR analysis of oligosaccharides obtained by partial acid hydrolysis of mEPS-PNNS afforded a composite model, which includes all identified structural features.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Aug
|
pubmed:issn |
1526-4602
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pubmed:author |
|
pubmed:issnType |
Electronic
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pubmed:volume |
9
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2251-8
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pubmed:meshHeading |
pubmed-meshheading:18616317-Anions,
pubmed-meshheading:18616317-Chromatography, Ion Exchange,
pubmed-meshheading:18616317-Glucans,
pubmed-meshheading:18616317-Glycosyltransferases,
pubmed-meshheading:18616317-Hydrogen-Ion Concentration,
pubmed-meshheading:18616317-Hydrolysis,
pubmed-meshheading:18616317-Lactic Acid,
pubmed-meshheading:18616317-Lactobacillus reuteri,
pubmed-meshheading:18616317-Magnetic Resonance Spectroscopy,
pubmed-meshheading:18616317-Mass Spectrometry,
pubmed-meshheading:18616317-Mutagenesis, Site-Directed,
pubmed-meshheading:18616317-Mutation,
pubmed-meshheading:18616317-Oxygen,
pubmed-meshheading:18616317-Periodic Acid,
pubmed-meshheading:18616317-Protein Engineering
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pubmed:year |
2008
|
pubmed:articleTitle |
Structural analysis of bioengineered alpha-D-glucan produced by a triple mutant of the Glucansucrase GTF180 enzyme from Lactobacillus reuteri strain 180: generation of (alpha1-->4) linkages in a native (1-->3)(1-->6)-alpha-D-glucan.
|
pubmed:affiliation |
Department of Bio-Organic Chemistry, Bijvoet Center, Utrecht University, 3584 CH Utrecht, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|