Thiamine triphosphate and thiamine triphosphatase activities: from bacteria to mammals

@article{Makarchikov2003ThiamineTA,
  title={Thiamine triphosphate and thiamine triphosphatase
activities: from bacteria to mammals},
  author={Alexander F Makarchikov and Bernard Lakaye and I. E. Gulyai and Jan Czerniecki and Bernard Coumans and Pierre Wins and Thierry Grisar and Lucien Bettendorff},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={2003},
  volume={60},
  pages={1477-1488}
}
AbstractIn 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… Expand
Thiamine triphosphate: a ubiquitous molecule in search of a physiological role
TLDR
In some tissues where adenylate kinase activity is high and ThTPase is absent, ThTP accumulates, reaching ≥ 70 % of total thiamine, with no obvious physiological consequences, raising the possibility that ThTP is part of a still uncharacterized cellular signaling pathway. Expand
On the nature of thiamine triphosphate in Arabidopsis
TLDR
It is proposed that TTP may signify TDP sufficiency, particularly in the organellar powerhouses, and discussed the findings in relation to its role. Expand
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TLDR
In animal cells, ThTP can phosphorylate some proteins, but the physiological significance of this mechanism remains unknown, and among the proteins involved in thiamin metabolism, thiam in transporters, Thiamin pyrophosphokinase and a soluble 25‐kDaThiamin triphosphatase have been characterized at the molecular level, in contrast to thiamIn mono‐ and diphosphatases whose specificities remain to be proven. Expand
Adenylate kinase-independent thiamine triphosphate accumulation under severe energy stress in Escherichia coli
TLDR
It is shown that bacterial, as vertebrate adenylate kinases are able to catalyze ThTP synthesis, but at a rate more than 106-fold lower than ATP synthesis, which is too low to explain the high rate of ThTP accumulation observed in E. coli during amino acid starvation. Expand
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TLDR
The hydrolysis of AThTP has been found to occur in all samples examined from rat, chicken and bovine tissues, with liver and kidney being the most abundant in enzyme activity. Expand
Adenosine thiamine triphosphate accumulates in Escherichia coli cells in response to specific conditions of metabolic stress
TLDR
It is concluded that a low energy charge is not sufficient to trigger AThTP accumulation and the latter can only accumulate under conditions where no ThTP is synthesized. Expand
Thiamine Triphosphate, a New Signal Required for Optimal Growth of Escherichia coli during Amino Acid Starvation*
TLDR
The results suggest that the early accumulation of ThTP initiates a reaction cascade involved in the adaptation of bacteria to stringent conditions such as amino acid starvation. Expand
Thiamine diphosphate adenylyl transferase from E. coli: functional characterization of the enzyme synthesizing adenosine thiamine triphosphate
TLDR
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Thiamine triphosphatase and the CYTH superfamily of proteins
TLDR
It is proposed that inorganic tripolyphosphate, the simplest triph phosphate compound, is the primitive substrate of CYTH proteins, other enzyme activities, such as adenylate cyclase, mRNA triphosphatase, and ThTPase, being secondary acquisitions. Expand
Thiamine Triphosphate Synthesis in Rat Brain Occurs in Mitochondria and Is Coupled to the Respiratory Chain*
TLDR
The results show for the first time that a high energy triphosphate compound other than ATP can be produced by a chemiosmotic type of mechanism, and might shed a new light on the understanding of the mechanisms of thiamine deficiency-induced brain lesions. Expand
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References

SHOWING 1-10 OF 47 REFERENCES
Adenylate kinase 1 knockout mice have normal thiamine triphosphate levels.
TLDR
It is predicted that the high ThTP content of particular tissues is more tightly correlated with high ThDP kinase activity or low soluble ThTPase activity than with non-stringent substrate specificity and high activity of adenylate kinase. Expand
Molecular Characterization of a Specific Thiamine Triphosphatase Widely Expressed in Mammalian Tissues*
TLDR
The recombinant ThTP enzyme had properties similar to those of human brain ThTPase, and it was specific for ThTP, and the mRNA was expressed in most human tissues but at relatively low levels. Expand
Hydrolysis and synthesis of thiamin triphosphate in bacteria.
TLDR
Cellular ThTP was found to be controlled in the course of the long term to maintain its ratio to the amount of cellular ThDP and two phosphatases specific for ThTP (ThTPase) among thiamin phosphates were detected in E. coli. Expand
Thiamine Triphosphate in Bakers' Yeast
TLDR
This compound gave, like thiamine diphosphate, a blue fluorescence in ultra-violet light after having been oxidized with potassium ferricyanide in alkaline solution and had biological activity when tested in a Warburg apparatus with washed yeast. Expand
Thiamine Triphosphate and Membrane‐Associated Thiamine Phosphatases in the Electric Organ of Electrophorus electricus
TLDR
The main electric organ of Electrophorus electricus is particularly rich in thiamine triphosphate, which represents 87% of the totalThiamine content in this tissue is very low in the eel electric organ and skeletal muscle as compared with other eel or rat tissues. Expand
Metabolism of Thiamine Triphosphate in Rat Brain: Correlation with Chloride Permeability
TLDR
The results suggest that TTP synthesis is catalyzed by an ATP:TDP transphosphorylase rather than by the cytoplasmic adenylate kinase that may be present in the vesicles and a regulatory role of TTP on chloride permeability, but the target remains to be characterized. Expand
Content of thiamin phosphate esters in mammalian tissues--an extremely high concentration of thiamin triphosphate in pig skeletal muscle.
TLDR
An extremely high concentration of thiamin triphosphate (TTP) was detected in adult pig skeletal muscles and may give a clue as to the physiological functions of TTP. Expand
Nucleoside-triphosphatase and hydrolysis of thiamin triphosphate in Escherichia coli.
A membrane-bound nonspecific triphosphatase of E. coli was solubilized and purified to a homogeneous SDS-acrylamide gel electrophoresis band. It was found to be a single polypeptide of 16 kDaExpand
A membrane-associated thiamine triphosphatase from rat brain. Properties of the enzyme.
TLDR
A specific inhibitor of the enzyme, the β-γ-methylene phosphonate analog of thiamine triphosphate, has been synthesized, and its inhibitory characteristics are described. Expand
The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates
TLDR
The phyletic distribution of the CYTH domain suggests that it is an ancient enzymatic domain that was present in the Last Universal Common Ancestor and was involved in nucleotide or organic phosphate metabolism. Expand
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