Linked Life Data

19549605

Source:http://linkedlifedata.com/resource/pubmed/id/19549605

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2009-6-24
pubmed:databankReference
pubmed:abstractText
Glycodiversification, an invaluable tool for generating biochemical diversity, can be catalyzed by glycosyltransferases, which attach activated sugar "donors" onto "acceptor" molecules. However, many glycosyltransferases can tolerate only minor modifications to their native substrates, thus making them unsuitable tools for current glycodiversification strategies. Here we report the production of functional chimeric glycosyltransferases by mixing and matching the N- and C-terminal domains of glycopeptide glycosyltransferases. Using this method we have generated hybrid glycopeptides and have demonstrated that domain swapping can result in a predictable switch of substrate specificity, illustrating that N- and C-terminal domains predominantly dictate acceptor and donor specificity, respectively. The determination of the structure of a chimera in complex with a sugar donor analog shows that almost all sugar-glycosyltransferase binding interactions occur in the C-terminal domain.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1879-1301
pubmed:author
pubmed:issnType
Electronic
pubmed:day
26
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
676-85
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Chimeric glycosyltransferases for the generation of hybrid glycopeptides.
pubmed:affiliation
University Chemical Laboratory, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, England, UK. awt26@cam.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't