| First Author | Sakaguchi H | Year | 2000 |
| Journal | Biochim Biophys Acta | Volume | 1523 |
| Issue | 2-3 | Pages | 269-76 |
| PubMed ID | 11042394 | Mgi Jnum | J:65460 |
| Mgi Id | MGI:1926617 | Doi | 10.1016/s0304-4165(00)00136-7 |
| Citation | Sakaguchi H, et al. (2000) Functional expression and genomic structure of human N-acetylglucosamine-6-O-sulfotransferase that transfers sulfate to beta-N-acetylglucosamine at the nonreducing end of an N-acetyllactosamine sequence(1). Biochim Biophys Acta 1523(2-3):269-76 |
| abstractText | The cDNA and gene encoding human N-acetylglucosamine-6-O-sulfotransferase (Gn6ST) have been cloned. Comparative analysis of this cDNA with the mouse Gn6ST sequence indicates 96% amino acid identity between the two sequences. The expression of a soluble recombinant form of the protein in COS-1 cells produced an active sulfotransferase, which transferred sulfate to the terminal GlcNAc in GlcNAcbeta1-O-CH(3), GlcNAcbeta1-3Galbeta1-O-CH(3) and GlcNAcbeta1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4GlcNAc but not in GlcNAcalpha1-4GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser. In addition, neither Galbeta1-4GlcNAcbeta1-O-naphthalenemethanol nor GalNAcbeta1-4GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser were utilized as acceptors. These findings indicate that a terminal beta-linked GlcNAc residue is necessary for acceptor substrates of Gn6ST. The human Gn6ST gene spans about 7 kb, consists of two exons and exhibits an intron-less coding region. |
