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J. Biol. Chem., Vol. 277, Issue 48, 45719-45728, November 29, 2002
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-Galactoside
2,6-Sialyltransferase (ST6Gal II), Which Sialylates Gal
1,4GlcNAc
Structures on Oligosaccharides Preferentially
§,
From the A novel member of the human
Laboratory of Cellular Biochemistry, RIKEN
(The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako,
Saitama 351-0198 and ¶ Department of Chemistry, Faculty of
Science, Ochanomizu University, Otsuka, Bunkyo-ku, Tokyo 112-8610, Japan
-galactoside
2,6-sialyltransferase (ST6Gal) family, designated
ST6Gal II, was identified by BLAST analysis of expressed sequence tags
and genomic sequences. The sequence of ST6Gal II encoded a protein of
529 amino acids, and it showed 48.9% amino acid sequence identity with
human ST6Gal I. Recombinant ST6Gal II exhibited
2,6-sialyltransferase activity toward oligosaccharides that
have the Gal
1,4GlcNAc sequence at the nonreducing end of their
carbohydrate groups, but it exhibited relatively low and no activities
toward some glycoproteins and glycolipids, respectively. It is
concluded that ST6Gal II is an oligosaccharide-specific enzyme compared
with ST6Gal I, which exhibits broad substrate specificities, and is
mainly involved in the synthesis of sialyloligosaccharides. The
expression of the ST6Gal II gene was significantly detected by reverse
transcription PCR in small intestine, colon, and fetal brain,
whereas the ST6Gal I gene was ubiquitously expressed, and its
expression levels were much higher than those of the ST6Gal II gene.
The ST6Gal I gene was also expressed in all tumors examined, but no
expression was observed for the ST6Gal II gene in these tumors. The
ST6Gal II gene is located on chromosome 2 (2q11.2-q12.1), and it spans
over 85 kb of human genomic DNA consisting of at least eight exons and
shares a similar genomic structure with the ST6Gal I gene. In this
paper, we have shown that ST6Gal I, which has been known as the sole
member of the ST6Gal family, also has the counterpart enzyme (ST6Gal
II) like other sialyltransferases.
The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession number(s) AB059555.
§ Special postdoctoral researcher from RIKEN (The Institute of Physical and Chemical Research).
To whom correspondence should be addressed. Tel.:
81-48-467-9370; Fax: 81-48-462-4670; E-mail:
tsujimot@postman.riken.go.jp.
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