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J Biol Chem, Vol. 274, Issue 17, 11479-11486, April 23, 1999
2,3-Sialyltransferase (ST3Gal VI)
That Sialylates Type II Lactosamine Structures on Glycoproteins and
Glycolipids
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From the A novel member of the human
CMP-NeuAc: Department of Biochemistry,
-galactoside 
2,3-sialyltransferase (ST) subfamily,
designated ST3Gal VI, was identified based on BLAST analysis of
expressed sequence tags, and a cDNA clone was isolated from a human
melanoma line library. The sequence of ST3Gal VI encoded a type II
membrane protein with 2 amino acids of cytoplasmic domain, 32 amino
acids of transmembrane region, and a large catalytic domain with 297 amino acids; and showed homology to previously cloned ST3Gal III,
ST3Gal IV, and ST3Gal V at 34, 38, and 33%, respectively. Extracts
from L cells transfected with ST3Gal VI cDNA in a expression vector
and a fusion protein with protein A showed an enzyme activity of
2,3-sialyltransferase toward Gal1,4GlcNAc structure on
glycoproteins and glycolipids. In contrast to ST3Gal III and
ST3Gal IV, this enzyme exhibited restricted substrate specificity,
i.e. it utilized Gal1,4GlcNAc on glycoproteins, and
neolactotetraosylceramide and neolactohexaosylceramide, but not
lactotetraosylceramide, lactosylceramide, or asialo-GM1. Consequently, these data indicated that this enzyme is
involved in the synthesis of sialyl-paragloboside, a precursor of
sialyl-Lewis X determinant.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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