Biological Specificity of Sialyltransferases

  • Subhash Basu
  • Manju Basu
  • Shib Sankar Basu

Abstract

Sialyltransferases (abbreviated as SATs or STs) are a family of glycosyltransferases involved in the biosynthesis of complex sialoglycoproteins (SGPs) and sialoglycosphingolipids (SGSLs). A separate sialyltransferase (SAT or ST) catalyzes the transfer of sialic acid to a specific oligosaccharide with concomitant formation of a defined anomeric as well as positional linkage (Schachter and Roseman, 1980; Sadler et al., 1982; S. Basu and Basu, 1982). If one accepts the “one linkage, one enzyme” hypothesis (Schachter and Roseman, 1980), then based on the various different sialyl linkages present in cell surface oligosaccharides, genes for many different SATs (M. Basu et al., 1987; S. C. Basu, 1991; Paulson and Colley, 1989) occur in animal cells. The substrate specificity profiles serve as the basis for a general classification of Golgi-bound animal SATs into three major classes: glycoprotein:sialyltransferases, glycolipid:sialyltransferases, and mucin:sialyltransferases. Comparison of their primary structures (as defined by amino acid sequence derived from the cDNAs), as well as three-dimensional structures, will be an important approach for further studies.

Keywords

Sialic Acid Human Placenta Bovine Colostrum Polysialic Acid Biological Specificity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Subhash Basu
    • 1
  • Manju Basu
    • 1
  • Shib Sankar Basu
    • 1
  1. 1.Department of Chemistry and BiochemistryUniversity of Notre DameNotre DameUSA

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