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Glycobiology Advance Access published online on December 11, 2005
Glycobiology, doi:10.1093/glycob/cwj068
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received October 12, 2005
Revised December 1, 2005
Accepted December 7, 2005

Article

Reaction Mechanism and Substrate Specificity for Nucleotide-Sugar of Mammalian {alpha}1,6-Fucosyltransferase

Hideyuki Ihara 1, Yoshitaka Ikeda 2, and Naoyuki Taniguchi 1 *

1 Department of Biochemistry, Osaka University Graduate School of Medicine, B1, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan
2 Division of Molecular Biology, Department of Biomolecular Sciences, Saga University Faculty of Medicine, 5-1-1 Nabeshima, Saga 849-8501, Japan; CREST, JST

* To whom correspondence should be addressed.
Naoyuki Taniguchi, E-mail: proftani{at}biochem.med.osaka-u.ac.jp


  Abstract

FUT8, mammalian {alpha}1,6-fucosyltransferase, catalyzes the transfer of a fucose residue from the donor substrate, GDP-{beta}-L-fucose, to the reduced terminal GlcNAc of the core structure of asparagine-linked oligosaccharide via an {alpha}1,6-linkage. FUT8 is a typical type II membrane protein ,which is localized in the Golgi apparatus. We have previously shown that two neighboring arginine residues that are conserved among the {alpha}1,2-, {alpha}1,6- and protein O-fucosyltransferases play an important role in donor substrate binding. However, details of the catalytic and reaction mechanisms and the ternary structure of FUT8 are not understood except for the substrate specificity of the acceptor. In order to develop a better understanding of FUT8, we established a large-scale production system for recombinant human FUT8, in which the enzyme is produced in soluble form by baculovirus-infected insect cells. Kinetic analyses and inhibition studies using derivatives of GDP-{beta}-L-fucose revealed that FUT8 catalyzes the reaction which depends on a rapid equilibrium random mechanism and strongly recognizes the base portion and diphosphoryl group of GDP-{beta}-L-fucose. These results may be also applicable to other fucosyltransferases and glycosyltransferases.

Keywords: fucosyltransferase/FUT8/kinetic analysis/reaction mechanism/baculovirus/insect cell expression system.
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