Structures and mechanisms of glycosyltransferases

被引:519
作者
Breton, C
Snajdrová, L
Jeanneau, C
Koca, J
Imberty, A
机构
[1] Univ Grenoble 1, CNRS, CERMAV, F-38041 Grenoble 9, France
[2] Masaryk Univ, NCBR, CZ-61137 Brno, Czech Republic
关键词
fold recognition; glycosyltransferase; mechanism; superfamily; three-dimensional structure;
D O I
10.1093/glycob/cwj016
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Glycosyltransferases (GTs) catalyze the transfer of a sugar moiety from an activated donor sugar onto saccharide and nonsaccharide acceptors. A sequence-based classification spreads GTs in many families thus reflecting the variety of molecules that can be used as acceptors. In contrast, this enzyme family is characterized by a more conserved three-dimensional architecture. Until recently, only two different folds (GT-A and GT-B) have been identified for solved crystal structures. The recent report of a structure for a bacterial sialyltransferase allows the definition of a new fold family. Progress in the elucidation of the structures and mechanisms of GTs are discussed in this review. To accommodate the growing number of crystal structures, we created the 3D-Glycosyltransferase database to gather structural information concerning this class of enzymes.
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收藏
页码:29R / 37R
页数:9
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