Linked Life Data

17678897

Source:http://linkedlifedata.com/resource/pubmed/id/17678897

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2007-8-13
pubmed:abstractText
Segments that may crucially influence the catalytic behaviour of glucosyltransferases of the glucansucrase type were selected for modification. This was done by sequence alignments, followed by structural modelling of the putative catalytic domain, based on a permuted form of the glucosyltransferase R (GtfR) of Streptococcus oralis. Five selected regions, located in the C-terminal half of the potential catalytic domain, were replaced by segments found at equivalent positions in other glucosyltransferases. The exchanges of four of these regions significantly affected catalysis by GtfR. This identified C-terminal determinants for substrate binding and turnover and supports the so-called permutation hypothesis with respect to enzymes of the glucansucrase type. Based on the model, roles are proposed for specific residues. Major effects appear to involve a re-positioning of the C-terminal Tyr965 that very likely serves as a hydrophobic platform for the substrate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
581
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4036-42
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Identification of structural determinants for substrate binding and turnover by glucosyltransferase R supports the permutation hypothesis.
pubmed:affiliation
Division of Microbiology, Helmholtz Centre for Infection Research, Braunschweig, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't