K. Uchimura et al., Diversity of N-acetylglucosamine-6-O-sulfotransferases: Molecular cloning of a novel enzyme with different distribution and specificities, BIOC BIOP R, 274(2), 2000, pp. 291-296
Citations number
27
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
N-Acetylglucosamine-6-O-sulfotransferase (GlcNAc6ST) transfers sulfate to t
he C-6 position of non-reducing N-acetylglucosamine (GlcNAc) residues. We c
loned human and mouse cDNAs encoding a novel GlcNAc6ST, designated as GlcNA
c6ST-4, which showed sequence identities of 26 to 41% to other GlcNAc6STs.
Human organs with strong expression of the enzyme mRNA were the heart, sple
en, and ovary, while in the mouse strong expression was detected in the kid
ney. The enzyme expressed in CHO cells preferentially acted on mannose-link
ed GlcNAc, while a core 2 mucin-type oligosaccharide and an N-acetyllactosa
mine oligomer also served as accepters, The distribution and the specificit
y of GlcNAc6ST are different from those of GlcNAc6STs identified previously
. (C) 2000 Academic Press.