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Volume 272, Number 50, Issue of December 12, 1997
pp. 31340-31347
(Received for publication, August 1, 1997, and in revised form, September 29, 1997)
From the The enzyme that transfers
D-xylose from UDP-xylose to the
Purification and Specificity of
1,2-Xylosyltransferase, an
Enzyme That Contributes to the Allergenicity of Some Plant
Proteins
,
,
and
Department of Biochemistry and Molecular
Biology, University of Arkansas for Medical Sciences, Little Rock,
Arkansas 72205 and the § Department of Medicinal Chemistry,
University of Michigan, College of Pharmacy,
Ann Arbor, Michigan 48109-1065
-linked mannose of
plant N-linked oligosaccharides was purified about
51,000-fold to apparent homogeneity from soybean microsomes. On SDS
gels, two proteins of 56 and 59 kDa were detected and both were labeled
to the same extent by the photoaffinity label,
5-N3-UDP-[32P]xylose. Labeling of both
proteins was inhibited by cold UDP-xylose, but not by UDP-glucose. The
amount of 5-N3-UDP-[32P]xylose that bound to
the two protein bands was greatly increased in the presence of
oligosaccharide acceptors. The best acceptor for xylose transfer and
for stimulation of UDP-xylose binding was
GlcNAc2Man3GlcNAc2-T, but
GlcNAc1Man3GlcNAc2, with the
GlcNAc on the 3-branch, was also a good acceptor and a good stimulator. A number of other N-linked oligosaccharides were poor
acceptors, especially those with galactose units at the nonreducing
termini. Many of the properties of this enzyme have been described, and the product of the reaction of UDP-xylose and
GlcNAc2Man3(GlcNAc)2 was
characterized as GlcNAc1,
2Man
1,6(GlcNAc1,2Man1,3)(Xyl1,2)Man1,4GlcNA c2-T
by chemical and NMR methods.
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