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- Title
The action of N-acetylglucosaminyltransferase-V is prevented by the bisecting GlcNAc residue at the catalytic step
- Authors
Sasai, Ken; Ikeda, Yoshitaka; Eguchi, Hironobu; Tsuda, Takeo; Honke, Koichi; Taniguchi, Naoyuki
- Abstract
Using a purified protein and bisected acceptor oligosaccharides, we demonstrate that N-acetylglucosaminyltransferase (GnT)-V transfers a N-acetylglucosamine residue via a β1,6-linkage to the bisected oligosaccharides. We also kinetically characterized the substrate specificity of GnT-V with respect to the bisected oligosaccharide. Although the Km values for the bisected acceptors were comparable to that for a non-bisected acceptor, the Vmax values for the bisected acceptors were much lower than that for the non-bisected acceptor. These findings suggest that the acceptor specificity of GnT-V is determined by the catalytic process rather than by its binding to the substrate. It was also found that the presence of the 2-N-acetyl group in the bisecting monosaccharide moiety plays a critical role in determining the catalytic efficiency of the enzyme.
- Subjects
OLIGOSACCHARIDES; HIGH performance liquid chromatography
- Publication
FEBS Letters, 2002, Vol 522, Issue 1-3, p151
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(02)02916-2