The galactosyltransferase family.
Galactose is transferred via several linkages to acceptor structures by galactosyltransferase enzymes. In prokaryotes, galactose is mainly found on lipopolysaccharides and capsular polysaccharides. In eukaryotes, galactosyltransferases, which are localized in the Golgi apparatus, are involved in the formation of several classes of glycoconjugates and in lactose biosynthesis. Although they sometimes catalyze identical reactions, prokaryotic and eukaryotic galactosyltransferases share only little structural similarities. In mammals, 19 distinct galactosyltransferase enzymes have been characterized to date. These enzymes catalyze the transfer of galactose via beta1-4, beta1-3, alpha1-3 and alpha1-4 linkages. The present review focuses on the description of these mammalian galactosyltransferases.
Hennet
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Institute of Physiology, University of Zürich, Switzerland. thennet@access.unizh.ch
D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000201:enzymology; D002240:Carbohydrate Sequence; D005700:Galactosyltransferases / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D006001:Glycoconjugates / Q000096:biosynthesis / Q000737:chemistry; D008969:Molecular Sequence Data; D010802:Phylogeny; D016415:Sequence Alignment; D013379:Substrate Specificity
D006001:Glycoconjugates; D005700:Galactosyltransferases