Galβ1-4GlcNAc α2-6-sialyltransferase (EC catalyzes the incorporation of sialic acids at the terminal positions of glycoconjugates with NeuAc α2-6-Gal linkage. cDNA sequences from mouse, rat, human, and chicken, along with the human genomic DNA sequence and-tissue specific alternative splicing in rat have been described. Also, the domains responsible for localization to the Golgi apparatus and the acceptor substrate specificity, with synthetic acceptors, have been reported. Cloned sialyltrans- ferases have been expressed in cultured eukaryotic cells and in E. coli. Like other sialyltransferases, ST6Gal-I exhibits type II membrane protein topology and has characteristic motifs for sialyltransferases called sialylmotifs L, S, and VS. ST3Gal-II also has a Kurosawa motif (Cys-Xaa75-82-Cys-Xaa-Cys-Ala-Xaa-Vα1-Xaa150–160-Cys; Xaa denotes any amino acid residue) as seen in the ST3Gal family and two members of the ST6GalNAc family (Kurosawa et al. 1996; Tsuji 1999). Currently, ST6Gal-I is the sole member of the ST6Gal subfamily that can also synthesize the ganglioside terminal NeuAc α2-6-Gal glycoconjugates.


Sialic Acid Acceptor Substrate Bovine Colostrum Membrane Protein Topology Synthetic Acceptor 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Fast DG, Jamieson JC, McCaffrey G (1993) The role of the carbohydrate chains of Gal β-1,4-GlcNAc a 2,6-sialyltransferase for enzyme activity. Biochim Biophys Acta 1202:325–330PubMedCrossRefGoogle Scholar
  2. Grundnann V, Nerlich C, Rein T, Zettlmeissl G (1990) Complete cDNA sequence encoding human β-galactoside α2,6-sialyltransferase Nucleic Acids Res 18:667Google Scholar
  3. Hamamoto T, Lee Y-C, Kurosawa N, Nakaoka T, Kojima N, Tsuji S (1994) Expression of mouse Gal β 1,4GlcNAc a 2,6-sialyltransferase in an insoluble form in Escherichia coli and partial renaturation. Bioorg Med Chem 2:79–84PubMedCrossRefGoogle Scholar
  4. Hamamoto T, Kurosawa N, Lee Y-C, Tsuji S (1995) Donor substrate specificities of Galβ1,4GlcNAc α2,6-sialyltransferase and Galβ1,3GalNAc α2,3-sialyltransferase: comparison of N-acetyl and N-grycolylneuraminic acids. Biochim Biophys Acta 1244:223–228PubMedCrossRefGoogle Scholar
  5. Hennet T, Chui D, Paulson JC, Marth JD (1998) Immune regulation by the ST6Gal sialyltransferase. Proc Natl Acad Sci USA 95:4504–4509PubMedCrossRefGoogle Scholar
  6. Joziasse DH, Schiphorst WECM, Van den Eijnden DH, Van Kuik JA, Van Halbeek H, Vliegenthart JFG (1985) Branch specificity of bovine colostrum CMP-sialic acid: N-acetyllactosaminide α 2-6-sialyltransferase. Interaction with biantennary oligosaccharides and glycopeptides of N-glycosylproteins. J Biol Chem 260:714–719PubMedGoogle Scholar
  7. Kurosawa N, Hamamoto T, Lee YC, Nakaoka T, Kojima N, Tsuji S (1994) Molecular cloning and expression of GalNAc α2,6-sialyltransferase. J Biol Chem 269:1402–1409PubMedGoogle Scholar
  8. Kurosawa N, Kojima N, Inoue M, Hamamoto T, Tsuji S (1994) Cloning and expression of Gal β 1,3GalNAc-specific GalNAc a 2,6-sialyltransferase. J Biol Chem 269:19048–19053PubMedGoogle Scholar
  9. Kurosawa N, Inoue M, Yoshida Y, Tsuji S (1996) Molecular cloning and genomic analysis of mouse Galβ1,3GalNAc-specific GalNAc α2,6-sialyltransferase. J Biol Chem 271:15109–15116PubMedCrossRefGoogle Scholar
  10. Svensson EC, Soreghan B, Paulson JC (1990) Organization of the β-galactoside α-2,6-sialyltransferase gene. Evidence for the transcriptional regulation of terminal glycosylation. J Biol Chem 265:20863–20868PubMedGoogle Scholar
  11. Svensson EC, Conley PB, Paulson JC (1992) Regulated expression of a 2,6-sialyltransferase by the liver-enriched transcription factors HNF-1, DBP, and LAP. J Biol Chem 267:466–472Google Scholar
  12. Tsuji S (1999) Molecular cloning and characterization of sialyltransferases. In: Inoue Y, Lee YC, Troy FA (eds) Sialobiology and other novel forms of glycosylation. Gakushin, Osaka, pp 145–154Google Scholar
  13. Tsuji S, Datta AK, Paulson JC (1996) Systematic nomenclature for sialyltransferases. Glycobiology 6(7):v–viiPubMedCrossRefGoogle Scholar
  14. Van den Eijnden DH, Joziasse DH, Dorland L, Van Halbeek H, Vliegenthart JFG, Schmid K (1980) Specificity in the enzymic transfer of sialic acid to the oligosaccharide branches of bi-and triantennary glycopeptides of α1-acid glycoprotein. Biochem Biophys Res Commun 92:839–845PubMedCrossRefGoogle Scholar
  15. Weinstein J, de Souza-e-Silva U, Paulson JC (1982a) Purification of a Gal β 1 to 4GlcNAc α 2 to 6 sialyltransferase and a Gal β 1 to 3(4) GlcNAc α 2 to 3 sialyltransferase to homogeneity from rat liver. J Biol Chem 257:13835–13844PubMedGoogle Scholar
  16. Weinstein J, de Souza-e-Silva U, Paulson JC (1982b) Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal β 1 to 3(4)GlcNAc α 2 to 3 sialyltransferase and a Gal β 1 to 4GlcNAc α 2 to 6 sialyltransferase from rat liver. J Biol Chem 257:13845–13853PubMedGoogle Scholar
  17. Weinstein J, Lee EU, McEntee K, Lai PH, Paulson JC (1987) Primary structure of β-galactoside α 2,6-sialyltransferase. Conversion of membrane-bound enzyme to soluble forms by cleavage of the NH2-terminal signal anchor. J Biol Chem 262:17735–17743PubMedGoogle Scholar
  18. Wen DX, Svensson EC, Paulson JC (1992) Tissue-specific alternative splicing of the β-galactoside a 2,6-sialyltransferase gene. J Biol Chem 267:2512–2518PubMedGoogle Scholar
  19. Wuensch SA, Huang RY, Ewing J, Liang X-L, Lau JTY (2000) Murine B cell differentiation is accompanied by programmed expression of multiple novel β-galactoside α2,6-sialyltransferase mRNA forms. Glycobiology 10:67–75PubMedCrossRefGoogle Scholar

Copyright information

© Springer Japan 2002

Authors and Affiliations

  • Toshiro Hamamoto
    • 1
  • Shuichi Tsuji
    • 2
  1. 1.Department of BiochemistryJichi Medical School, MinamikawachiTochigiJapan
  2. 2.Department of Chemistry, Faculty of ScienceOchanomizu University, Otsuka, Bunkyo-kuTokyoJapan

Personalised recommendations