An Evolving Hierarchical Family Classification for Glycosyltransferases

Glycosyltransferases are a ubiquitous group of enzymes that catalyse the transfer of a sugar moiety from an activated sugar donor onto saccharide or non-saccharide acceptors. Although many glycosyltransferases catalyse chemically similar reactions, presumably through transition states with substanti...

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Bibliographic Details
Published in:Journal of molecular biology 2003-04, Vol.328 (2), p.307-317
Main Authors: Coutinho, Pedro M., Deleury, Emeline, Davies, Gideon J., Henrissat, Bernard
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Animals
classification
Conserved Sequence
genomic annotations
Genomics
glycosyltransferases
Glycosyltransferases - chemistry
Glycosyltransferases - classification
Glycosyltransferases - genetics
Glycosyltransferases - metabolism
Humans
Models, Molecular
modular structure
protein families
Protein Folding
Sequence Homology, Amino Acid
Substrate Specificity
Terminology as Topic
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Summary:Glycosyltransferases are a ubiquitous group of enzymes that catalyse the transfer of a sugar moiety from an activated sugar donor onto saccharide or non-saccharide acceptors. Although many glycosyltransferases catalyse chemically similar reactions, presumably through transition states with substantial oxocarbenium ion character, they display remarkable diversity in their donor, acceptor and product specificity and thereby generate a potentially infinite number of glycoconjugates, oligo- and polysaccharides. We have performed a comprehensive survey of glycosyltransferase-related sequences (over 7200 to date) and present here a classification of these enzymes akin to that proposed previously for glycoside hydrolases, into a hierarchical system of families, clans, and folds. This evolving classification rationalises structural and mechanistic investigation, harnesses information from a wide variety of related enzymes to inform cell biology and overcomes recurrent problems in the functional prediction of glycosyltransferase-related open-reading frames.
ISSN:0022-2836
1089-8638
DOI:10.1016/S0022-2836(03)00307-3