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J Biol Chem, Vol. 273, Issue 14, 8112-8118, April 3, 1998
From the Department of Pharmacokinetics and Metabolism, Genentech,
Inc., South San Francisco, California 94080
A GDP-fucose:polypeptide fucosyltransferase was
purified 5000-fold to homogeneity from Chinese hamster ovary cell
extracts in the absence of detergent. The purification procedure
included two affinity chromatographic steps using the acceptor
substrate, a recombinant factor VII EGF-1 domain, and the donor
substrate analog, GDP-hexanolamine, as ligands. The purified enzyme
migrates as a single band of 44,000 daltons on SDS-polyacrylamide gel
electrophoresis and is itself a glycoprotein with more than one high
mannose type oligosaccharide chain with a total molecular weight of
4000. The Km values for factor VII EGF-1 domain and
GDP-fucose are 15 and 6 µM, respectively. The
Vmax is 2.5 µmol·min
1·mg1. The presence of 50 mM Mn2+ increased the enzyme activity 17-fold,
but Mn2+ was not absolutely required, since the enzyme
exhibited some activity even in the presence of EDTA. The acceptor
substrate specificity was studied using site-directed mutagenesis of
human factor IX EGF domain. Only one of several differently folded
species could serve as acceptor substrate, although they all had the
same molecular weight as determined by liquid chromatography on-line with mass spectrometry. This indicates that the enzyme requires proper
folding of the epidermal growth factor domain for its activity.
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