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Gene Review

THTPA  -  thiamine triphosphatase

Homo sapiens

Synonyms: THTP, THTPASE, ThTPase, Thiamine-triphosphatase
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Disease relevance of THTPA

  • For this purpose, we expressed the untagged recombinant human ThTPase (hThTPase) in E. coli, produced the protein on a large scale and purified it to homogeneity [1].

High impact information on THTPA


Biological context of THTPA


Anatomical context of THTPA

  • The protein was rather uniformly located in the perikarya and dendrites, suggesting that ThTP and ThTPase may play a general role in neuronal metabolism rather than a specific role in excitability [7].
  • Some interneurons were also labeled and many ThTPase mRNA-positive and immunoreactive cells were distributed throughout cerebral cortical gray matter and the thalamus [7].
  • Thiamine triphosphatase (TTPase) from membranes isolated from the main electric organ of E. electricus is activated about 8 fold by NO3-, I- and SCN- while SO42- is inhibitory [8].

Associations of THTPA with chemical compounds

  • CONCLUSIONS: HAS rats have the genetically mediated thiamine diphosphate deficiency and increased thiamine triphosphate levels, probably due to reduced activity of thiamine triphosphatase in the liver and brain, compared with LAS rats [9].
  • A 6.4-fold increase in specific activity is obtained by successive treatment of crude membranes with octanoyl-N-methylglucamide, which solubilized other proteins, and Lubrol-PX with releases 60% of the thiamine triphosphatase (TTPase) activity [10].

Analytical, diagnostic and therapeutic context of THTPA


  1. Human recombinant thiamine triphosphatase: purification, secondary structure and catalytic properties. Lakaye, B., Makarchikov, A.F., Wins, P., Margineanu, I., Roland, S., Lins, L., Aichour, R., Lebeau, L., El Moualij, B., Zorzi, W., Coumans, B., Grisar, T., Bettendorff, L. Int. J. Biochem. Cell Biol. (2004) [Pubmed]
  2. Thiamine triphosphate and thiamine triphosphatase activities: from bacteria to mammals. Makarchikov, A.F., Lakaye, B., Gulyai, I.E., Czerniecki, J., Coumans, B., Wins, P., Grisar, T., Bettendorff, L. Cell. Mol. Life Sci. (2003) [Pubmed]
  3. Thiamine triphosphatase in the membranes of the main electric organ of Electrophorus electricus: substrate-enzyme interactions. Bettendorff, L., Grandfils, C., Wins, P., Schoffeniels, E. J. Neurochem. (1989) [Pubmed]
  4. Thiamine triphosphate and membrane-associated thiamine phosphatases in the electric organ of Electrophorus electricus. Bettendorff, L., Michel-Cahay, C., Grandfils, C., De Rycker, C., Schoffeniels, E. J. Neurochem. (1987) [Pubmed]
  5. Nonaromatic amidine derivatives as acylation catalysts. Birman, V.B., Li, X., Han, Z. Org. Lett. (2007) [Pubmed]
  6. The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates. Iyer, L.M., Aravind, L. BMC Genomics (2002) [Pubmed]
  7. Neuronal localization of the 25-kDa specific thiamine triphosphatase in rodent brain. Czerniecki, J., Chanas, G., Verlaet, M., Bettendorff, L., Makarchikov, A.F., Leprince, P., Wins, P., Grisar, T., Lakaye, B. Neuroscience (2004) [Pubmed]
  8. Thiamine triphosphatase from Electrophorus electric organ is anion-dependent and irreversibly inhibited by 4,4'-diisothiocyanostilbene-2,2'disulfonic acid. Bettendorff, L., Wins, P., Schoffeniels, E. Biochem. Biophys. Res. Commun. (1988) [Pubmed]
  9. Thiamine status in liver and brain of rats genetically selected for different sensitivity to hypnotic effect of alcohol. Zimatkina, T.I., Chernikevich, I.P., Zimatkin, S.M., Deitrich, R.A. Alcohol. Clin. Exp. Res. (2000) [Pubmed]
  10. Solubilization of thiamine triphosphatase from the electric organ of Electrophorus electricus. Bettendorff, L., Longrée, I., Wins, P., Schoffeniels, E. Biochim. Biophys. Acta (1991) [Pubmed]
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