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(Received for publication, May 6, 1996, and in revised form, July 15, 1996)
From the Institute of Biochemistry, University of Genova, and
Advanced Biotechnology Center, Viale Benedetto XV, 1, 16132 Genova, Italy
FX is a homodimeric NADP(H)-binding protein of 68 kDa, first identified in human erythrocytes, from which it was purified
to homogeneity. Its function has been unrecognized despite partial
structural and genetic characterization. Recently, on the basis of
partial amino acid sequence, it proved to be the human homolog of the
murine protein P35B, a tumor rejection antigen. In order to address the
biochemical role of FX, its primary structure was completed by cDNA
sequencing. This sequence revealed a significant homology with many
proteins from different organisms. Specifically, FX showed a remarkable
similarity with a putative Escherichia coli protein, named
Yefb, whose gene maps in a region of E. coli chromosome
coding for enzymes involved in synthesis and utilization of
GDP-D-mannose. Accordingly, a possible role of FX in this
metabolism was investigated. The data obtained indicate FX as the
enzyme responsible for the last step of the major metabolic pathway
resulting in GDP-L-fucose synthesis from
GDP-D-mannose in procaryotic and eucaryotic cells.
Specifically, purified FX apparently catalyzes a combined epimerase and
NADPH-dependent reductase reaction, converting
GDP-4-keto-6-D-deoxymannose to GDP-L-fucose.
This is the substrate of several fucosyltranferases involved in the
correct expression of many glyconjugates, including blood groups and
developmental antigens.
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27274-27279
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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