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- W2039446688 endingPage "53" @default.
- W2039446688 startingPage "35" @default.
- W2039446688 abstract "Enzymatic glycosylation of proteins and lipids is an abundant and important biological process. A great diversity of oligosaccharide structures and types of glycoconjugates is found in nature, and these are synthesized by a large number of glycosyltransferases. Glycosyltransferases have high donor and acceptor substrate specificities and are in general limited to catalysis of one unique glycosidic linkage. Emerging evidence indicates that formation of many glycosidic linkages is covered by large homologous glycosyltransferase gene families, and that the existence of multiple enzyme isoforms provides a degree of redundancy as well as a higher level of regulation of the glycoforms synthesized. Here, we discuss recent cloning strategies enabling the identification of these large glycosyltransferase gene families and exemplify the implication this has for our understanding of regulation of glycosylation by discussing two galactosyltransferase gene families." @default.
- W2039446688 created "2016-06-24" @default.
- W2039446688 creator A5016034491 @default.
- W2039446688 creator A5020795650 @default.
- W2039446688 creator A5058714848 @default.
- W2039446688 creator A5079197829 @default.
- W2039446688 date "1999-12-01" @default.
- W2039446688 modified "2023-10-10" @default.
- W2039446688 title "Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions" @default.
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