Abstract:
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 β1-4, β1-3, α1-3 and α1-4 linkages. The present review focuses on the description of these mammalian galactosyltransferases.
Keywords: Key words: Glycosylation; galactose; enzyme; Golgi; cell biology; gene family.
Footnotes
Received 17 December 2001; received after revision 15 January 2002; accepted 17 January 2002