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J Biol Chem, Vol. 274, Issue 17, 11958-11967, April 23, 1999
2,3Gal
1,3GalNAc GalNAc2,6-Sialyltransferase Family,
ST6GalNAc III and IV
,,,,,,
From Two cDNA clones encoding
NeuAc Molecular Glycobiology, Frontier Research
Program, Institute of Physical and Chemical Research (RIKEN), Wako,
Saitama 351-0198, Japan and the ¶ Department of Immunology,
Institute of Medical Microbiology and Hygiene, University of Freiburg,
Hermann-Herder-Strasse 11, D-79104 Freiburg, Germany
2,3Gal
1,3GalNAc GalNAc2,6-sialyltransferase have been
isolated from mouse brain cDNA libraries. One of the cDNA
clones is a homologue of previously reported rat ST6GalNAc III
according to the amino acid sequence identity (94.4%) and the
substrate specificity of the expressed recombinant enzyme, while the
other cDNA clone includes an open reading frame coding for 302 amino acids. The deduced amino acid sequence is not identical to those
of other cloned mouse sialyltransferases, although it shows the highest
sequence similarity with mouse ST6GalNAc III (43.0%). The expressed
soluble recombinant enzyme exhibited activity toward
NeuAc2, 3Gal1,3GalNAc, fetuin, and GM1b, while no significant activity was detected toward Gal1,3GalNAc or asialofetuin, or the
other glycoprotein substrates tested. The sialidase sensitivity of the
14C-sialylated residue of fetuin, which was
sialylated by this enzyme with CMP-[14C]NeuAc, was the
same as that of ST6GalNAc III. These results indicate that the
expressed enzyme is a new type of GalNAc2,6-sialyltransferase, which
requires sialic acid residues linked to Gal1,3GalNAc residues for
its activity; therefore, we designated it mouse ST6GalNAc IV. Although
the substrate specificity of this enzyme is similar to that of
ST6GalNAc III, ST6GalNAc IV prefers O-glycans to
glycolipids. Glycolipids, however, are better substrates for ST6GalNAc III.
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