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Glycobiology vol 2 no 4 pp. 271-277, 1992
© 1992
review-article |
Mammalian glycosyltransferases: genomic organization and protein structure
Department of Medical Chemistry, Vrije Universiteit Van der Boechorststraat 7, NL-1081 BT Amsterdam, The Netherlands
Received on April 14, 1992; accepted on May 8, 1992
In recent years, several glycosyltransferase genes and cDNAs have been cloned and characterized. Although the glycosyltransferases seem to share the same general architecture, there is only little sequence similarity between the various enzymes. Moreover, a comparison of the organization of the genes shows that there is no common pattern of intron-exon structure. In addition, there seems to be little or no correlation between glycosyltransferase exons and protein domains. Taken together, these observations suggest that many of the glycosyltransferase genes evolved independently. So far, only two glycosyltransferase gene families have been described. These families may have evolved by exon-shuffling, or by gene duplication and subsequent divergence. For specific glycosyltransferases, mechanisms such as alternative splicing and alternative promoter usage play a role in the production of multiple protein isoforms from a single gene. These isoenzymes may differ In their enzymatic properties or cellular localization.
genomic organization glycosyltransferases mammals protein structure
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