My watch list
my.chemeurope.com  
Login  

Sialyltransferase




Sialyltransferases are enzymes that transfer sialic acid to nascent oligosaccharides. Each sialyltransferase is specific for a particular sugar substrate. Sialyltransferases add sialic acid to the terminal portions of the sialylated glycolipids (gangliosides) or to the N- or O-linked sugar chains of glycoproteins.

There are about twenty different sialyltransferases which can be distinguished on the basis of the acceptor structure on which they act and on the type of sugar linkage they form. For example, a group of sialyltransferases adds sialic acid with an alpha2,3 linkage to galactose, while other sialyltransferases add sialic acid with an alpha2,6 linkage to galactose or N-acetylgalactosamine. A peculiar type of sialyltransferases add sialic acid to other sialic acid units with an alpha 2,8 linkage, forming structures referred to as polysialic acid. As occurs for other glycosyltransferases, the expression of sialyltransferases undergoes profound modifications during cell differentiation and neoplastic transformation; in some cases such changes induce phenotypic alterations.[1]

References

  1. ^ Dall'Olio and Chiricolo, Glycoconjugate J. 18 841-850, 2001
 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Sialyltransferase". A list of authors is available in Wikipedia.
Your browser is not current. Microsoft Internet Explorer 6.0 does not support some functions on Chemie.DE