title: Comparative aspects of glycosyltransferases.
abstract: 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.
authors.affiliation: Centre de Recherches sur les Macromolécules Végétales, Centre National de la Recherche Scientifique, BP 53, 38041 Grenoble, France.
authors.forename: Christelle
authors.initials: C
authors.lastname: Breton
authors.forename: Helena
authors.initials: H
authors.lastname: Heissigerová
authors.forename: Charlotte
authors.initials: C
authors.lastname: Jeanneau
authors.forename: Jitka
authors.initials: J
authors.lastname: Moravcová
authors.forename: Anne
authors.initials: A
authors.lastname: Imberty
mesh_terms: D020816:Amino Acid Motifs; D016695:Glycosyltransferases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D016695:Glycosyltransferases