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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2010-5-31
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pubmed:abstractText |
Xyloglucan xyloglucosyl transferases (EC 2.4.1.207), known as xyloglucan endotransglycosylases (XETs) use a disproportionation reaction mechanism and modulate molecular masses of xyloglucans. However, it is not known precisely how these size modulations and transfer reactions occur with polymeric acceptor substrates.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:copyrightInfo |
Crown Copyright 2010. Published by Elsevier B.V. All rights reserved.
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pubmed:issnType |
Print
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pubmed:volume |
1800
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
674-84
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pubmed:meshHeading |
pubmed-meshheading:20388532-Binding Sites,
pubmed-meshheading:20388532-Cloning, Molecular,
pubmed-meshheading:20388532-Enzyme Stability,
pubmed-meshheading:20388532-Glucans,
pubmed-meshheading:20388532-Glucosyltransferases,
pubmed-meshheading:20388532-Hordeum,
pubmed-meshheading:20388532-Kinetics,
pubmed-meshheading:20388532-Molecular Weight,
pubmed-meshheading:20388532-Oligosaccharides,
pubmed-meshheading:20388532-Protein Binding,
pubmed-meshheading:20388532-Solvents,
pubmed-meshheading:20388532-Xylans
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pubmed:year |
2010
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pubmed:articleTitle |
Xyloglucan xyloglucosyl transferases from barley (Hordeum vulgare L.) bind oligomeric and polymeric xyloglucan molecules in their acceptor binding sites.
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pubmed:affiliation |
Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, 1432 As, Norway.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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