Document Detail


Identification of new acceptor specificities of glycosyltransferase R with the aid of substrate microarrays.
MedLine Citation:
PMID:  16416490     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Finding opportunities to construct sugar motifs and to transfer them to targets of biological relevance and rapid identification of glycosylation events are important goals for glycobiology and a field of increasing interest. Here we have applied an enzyme microarray screening system for the identification of new acceptor specificities of the glycosyltransferase R (GTFR) from Streptococcus oralis (E.C. 2.4.1.5), which was able to effect the synthesis of sugar motifs in short times and with low amounts of substrate. These observations resulted in the development of a convenient alpha-glycosylation by the non-Leloir glycosyltransferase GTFR, with sucrose as substrate and with different alcohols and amino acid derivatives as acceptors, for the synthesis of glycoethers and glycosylated amino acids not observed with the use of familiar GTFs with high sequence homology.
Authors:
Jürgen Seibel; Hendrik Hellmuth; Bernd Hofer; Anna-Maria Kicinska; Bodo Schmalbruch
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Chembiochem : a European journal of chemical biology     Volume:  7     ISSN:  1439-4227     ISO Abbreviation:  Chembiochem     Publication Date:  2006 Feb 
Date Detail:
Created Date:  2006-02-07     Completed Date:  2006-05-25     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  100937360     Medline TA:  Chembiochem     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  310-20     Citation Subset:  IM    
Affiliation:
Technical Chemistry, Department for Carbohydrate Technology, Technical University Braunschweig, Langer Kamp 5, 38106 Braunschweig, Germany. jseibel@tu-bs.de
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MeSH Terms
Descriptor/Qualifier:
Alcohols / chemistry,  metabolism
Amino Acid Sequence
Amino Acids / chemistry,  metabolism
Bacterial Proteins / chemistry,  metabolism*
Carbohydrate Conformation
Carbohydrate Sequence
Glycosylation
Glycosyltransferases / chemistry,  genetics,  metabolism*
Methylglucosides / biosynthesis
Microarray Analysis / methods*
Molecular Sequence Data
Molecular Structure
Oligosaccharides* / chemistry,  metabolism
Sequence Alignment
Streptococcus oralis / enzymology
Substrate Specificity
Chemical
Reg. No./Substance:
0/Alcohols; 0/Amino Acids; 0/Bacterial Proteins; 0/Methylglucosides; 0/Oligosaccharides; 25360-07-0/methylglucoside; EC 2.4.-/Glycosyltransferases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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