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Originally published In Press as doi:10.1074/jbc.M111241200 on February 4, 2002

J. Biol. Chem., Vol. 277, Issue 16, 13771-13777, April 19, 2002
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Molecular Characterization of a Specific Thiamine Triphosphatase Widely Expressed in Mammalian Tissues*

Bernard LakayeDagger , Alexander F. MakarchikovDagger §, Adelio Fernandes Antunes, Willy Zorzi||, Bernard CoumansDagger , Edwin De Pauw, Pierre WinsDagger **, Thierry GrisarDagger , and Lucien BettendorffDagger **Dagger Dagger

From the Dagger  Center for Cellular and Molecular Neurobiology and the || Department of Human Histology, University of Liège, 4020 Liège, Belgium, the  Department of Physical Chemistry, University of Liège, 4000 Liège Sart Tilman, Belgium, and the § Laboratory of Enzymology, Institute of Biochemistry, National Academy of Sciences of Belarus, 230009 Grodno, Belarus

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 GenBankTM data base. 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 reverse transcription-PCR, cloned in Escherichia coli, and sequenced. The human open reading frame was expressed in E. coli as a GST fusion protein. Transformed bacteria had a high isopropyl-beta -D-thiogalactopyranoside-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.

* This work was supported by Fonds de la Recherche Fondamentale Collective Grant 2.4541.99 (to L. B. and B. L.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF432862 (human) and AF432863 (bovine).

** Research Associate at the Fonds National de la Recherche Scientifique.

Dagger Dagger To whom correspondence should be addressed: Center for Cellular and Molecular Neurobiology, University of Liège, 17 Place Delcour, B-4020 Liège, Belgium. Tel.: 32-4-366-59-67; Fax: 32-4-366-59-53; E-mail: L.Bettendorff@ulg.ac.be.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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