JBC Transcription and Nuclear Factor Monoclonals

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J Biol Chem, Vol. 273, Issue 14, 8193-8202, April 3, 1998

Molecular Cloning of Human GDP-mannose 4,6-Dehydratase and Reconstitution of GDP-fucose Biosynthesis in Vitro

Francis X. Sullivan, Ravindra Kumar, Ronald Kriz, Mark Stahl, Guang-Yi Xu, Jason Rouse, Xiao-jia Chang, Amechand Boodhoo§, Barry Potvin, and Dale A. Cumming

From Small Molecule Drug Discovery, Genetics Institute, Inc., § On-Site Biochromatography Inc., 424 Wilkinway, Edmonton, Alberta T6M 2H8, Canada, and the  Department of Biology, Yeshiva University, New York, New York 10033

We have cloned the cDNA encoding human GDP-mannose 4,6-dehydratase, the first enzyme in the pathway converting GDP-mannose to GDP-fucose. The message is expressed in all tissues and cell lines examined, and the cDNA complements Lec13, a Chinese Hamster Ovary cell line deficient in GDP-mannose 4,6-dehydratase activity. The human GDP-mannose 4,6-dehydratase polypeptide shares 61% identity with the enzyme from Escherichia coli, suggesting broad evolutionary conservation. Purified recombinant enzyme utilizes NADP+ as a cofactor and, like its E. coli counterpart, is inhibited by GDP-fucose, suggesting that this aspect of regulation is also conserved. We have isolated the product of the dehydratase reaction, GDP-4-keto-6-deoxymannose, and confirmed its structure by electrospray ionization-mass spectrometry and high field NMR. Using purified recombinant human GDP-mannose 4,6-dehydratase and FX protein (GDP-keto-6-deoxymannose 3,5-epimerase, 4-reductase), we show that the two proteins alone are sufficient to convert GDP-mannose to GDP-fucose in vitro. This unequivocally demonstrates that the epimerase and reductase activities are on a single polypeptide. Finally, we show that the two homologous enzymes from E. coli are sufficient to carry out the same enzymatic pathway in bacteria.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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