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Papers In Press, published online ahead of print February 4, 2002
Center for Cellular and Molecular Neurobiology, University of Liege, Liege 4020
Corresponding Author: L.Bettendorff{at}ulg.ac.be
Thiamine triphosphate (ThTP) is found at low concentrations in most animal tissues and recent data suggest that it may act as a phosphate donor for the phosphorylation of some proteins. In the mammalian brain, ThTP synthesis is rapid, but its steady-state concentration remains low, presumably because of rapid hydrolysis. In this report we purified a soluble thiamine triphosphatase (ThTPase, EC 3.6.1.28) from calf brain. The bovine ThTPase is a 24-kDa monomer, hydrolyzing ThTP with virtually absolute specificity. Partial sequence data obtained from the purified bovine enzyme by tandem mass spectrometry were used to search the GenBank database. A significant identity was found with only one human sequence, the hypothetical 230 amino acid protein MGC2652. The coding regions from human and bovine brain mRNA were amplified by RT-PCR, cloned in E. coli and sequenced. The human open reading frame was expressed in E. coli as a GST-fusion protein. Transformed bacteria had a high IPTG-inducible ThTPase activity. The recombinant ThTPase had properties similar to those of human brain ThTPase and it was specific for ThTP. The mRNA was expressed in most human tissues, but at relatively low levels. This is the first report of a molecular characterization of a specific ThTPase.
J. Biol. Chem, 10.1074/jbc.M111241200
Submitted on November 26, 2001
Revised on January 22, 2002
Accepted on February 4, 2002
Molecular characterization of a specific thiamine triphosphatase widely expressed in mammalian tissues
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