Comparative aspects of glycosyltransferases.
Glycosyltransferases, the enzymes that build oligosaccharides and glycoconjugates, have received much interest in recent years owing to their biological functions and their potential uses in biotechnology. Despite the fact that many glycosyltransferases recognize similar donor or acceptor substrates, there is surprisingly limited sequence identity between different classes. On the one hand, the glycosyltransferases are found in a large number of families, by sequence-based classification. On the other hand, only two structural folds have been identified among the fewer than one dozen glycosyltransferases that have been crystallized at present. Detection of conserved motifs that have a direct role in the functional aspects of glycosyltransferases is one approach for identifying remote similarity. With the availability of more crystal structures, the use of the fold-recognition approach is also very promising.
Breton
Christelle
C
Centre de Recherches sur les Macromolécules Végétales, Centre National de la Recherche Scientifique, BP 53, 38041 Grenoble, France.
Heissigerová
Helena
H
Jeanneau
Charlotte
C
Moravcová
Jitka
J
Imberty
Anne
A
D020816:Amino Acid Motifs; D016695:Glycosyltransferases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding
D016695:Glycosyltransferases