Literature DB >> 12943234

Thiamine triphosphate and thiamine triphosphatase activities: from bacteria to mammals.

A F Makarchikov1, B Lakaye, I E Gulyai, J Czerniecki, B Coumans, P Wins, T Grisar, L Bettendorff.   

Abstract

In most organisms, the main form of thiamine is the coenzyme thiamine diphosphate. Thiamine triphosphate (ThTP) is also found in low amounts in most vertebrate tissues and can phosphorylate certain proteins. Here we show that ThTP exists not only in vertebrates but is present in bacteria, fungi, plants and invertebrates. Unexpectedly, we found that in Escherichia coli as well as in Arabidopsis thaliana, ThTP was synthesized only under particular circumstances such as hypoxia (E. coli) or withering (A. thaliana). In mammalian tissues, ThTP concentrations are regulated by a specific thiamine triphosphatase that we have recently characterized. This enzyme was found only in mammals. In other organisms, ThTP can be hydrolyzed by unspecific phosphohydrolases. The occurrence of ThTP from prokaryotes to mammals suggests that it may have a basic role in cell metabolism or cell signaling. A decreased content may contribute to the symptoms observed during thiamine deficiency.

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Year:  2003        PMID: 12943234     DOI: 10.1007/s00018-003-3098-4

Source DB:  PubMed          Journal:  Cell Mol Life Sci        ISSN: 1420-682X            Impact factor:   9.261


  25 in total

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5.  Thiamine triphosphate synthesis in rat brain occurs in mitochondria and is coupled to the respiratory chain.

Authors:  Marjorie Gangolf; Pierre Wins; Marc Thiry; Benaïssa El Moualij; Lucien Bettendorff
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6.  Adenosine thiamine triphosphate accumulates in Escherichia coli cells in response to specific conditions of metabolic stress.

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7.  Thiamine status in humans and content of phosphorylated thiamine derivatives in biopsies and cultured cells.

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Review 9.  Thiamine triphosphate: a ubiquitous molecule in search of a physiological role.

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Journal:  Metab Brain Dis       Date:  2014-03-04       Impact factor: 3.584

10.  High inorganic triphosphatase activities in bacteria and mammalian cells: identification of the enzymes involved.

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Journal:  PLoS One       Date:  2012-09-12       Impact factor: 3.240

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