Thiamine triphosphate and thiamine triphosphatase activities: from bacteria to mammals

  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},
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… 

Thiamine triphosphate: a ubiquitous molecule in search of a physiological role

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.

Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes

Members of this protein family are found in nearly all living organisms, where they bind organic and inorganic triphosphates, ThTPase activity seems to be restricted to animals and in mammals, THTPA is ubiquitously expressed with probable post-transcriptional regulation.

On the nature of thiamine triphosphate in Arabidopsis

It is proposed that TTP may signify TDP sufficiency, particularly in the organellar powerhouses, and discussed the findings in relation to its role.

Thiamin diphosphate in biological chemistry: new aspects of thiamin metabolism, especially triphosphate derivatives acting other than as cofactors

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.

Adenylate kinase-independent thiamine triphosphate accumulation under severe energy stress in Escherichia coli

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.

Adenosine thiamine triphosphate and adenosine thiamine triphosphate hydrolase activity in animal tissues

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.

Adenosine thiamine triphosphate accumulates in Escherichia coli cells in response to specific conditions of metabolic stress

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.

Thiamine Triphosphate, a New Signal Required for Optimal Growth of Escherichia coli during Amino Acid Starvation*

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.

Thiamine diphosphate adenylyl transferase from E. coli: functional characterization of the enzyme synthesizing adenosine thiamine triphosphate

This is the first demonstration of an enzyme activity transferring a nucleotidyl group on thiamine diphosphate to produce AThTP, and the existence of a mechanism for the enzymatic synthesis of this compound is in agreement with the hypothesis of a non-cofactor role forThiamine derivatives in living cells.

Thiamine triphosphatase and the CYTH superfamily of proteins

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.



Molecular Characterization of a Specific Thiamine Triphosphatase Widely Expressed in Mammalian Tissues*

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.

Hydrolysis and synthesis of thiamin triphosphate in bacteria.

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.

Thiamine Triphosphate in Bakers' Yeast

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.

Thiamine Triphosphate and Membrane‐Associated Thiamine Phosphatases in the Electric Organ of Electrophorus electricus

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.

Metabolism of Thiamine Triphosphate in Rat Brain: Correlation with Chloride Permeability

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.

Content of thiamin phosphate esters in mammalian tissues--an extremely high concentration of thiamin triphosphate in pig skeletal muscle.

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.

The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates

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.