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Chemical Compound Review

Berolase     [2-[3-[(4-amino-2-methyl- pyrimidin-5...

Synonyms: Bivitasi, Cocarvit, Coxylase, Pyrolase, Biosyth, ...
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Disease relevance of thiamine diphosphate


High impact information on thiamine diphosphate

  • It contains thiamine pyrophosphate (TPP) and at least two ferredoxin-type [4Fe-4S] clusters per molecule, as determined by iron analysis and EPR spectroscopy [5].
  • Each catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and CO2 near the optimal growth temperature of the organism and are virtually inactive at 25 degrees C. Both PORs contain a thiamine pyrophosphate (TPP) cofactor and at least two [4Fe-4S] ferredoxin-type clusters [6].
  • Bromopyruvate also inactivates the intact pyruvate dehydrogenase complex in a TPP-dependent process, but the inhibition is more rapid and is mechanistically different [7].
  • Phosphorylation also substantially inhibited the transfer of [14C]acetyl groups from enzyme-bound [14C]acetylhydrolipoate to TPP in the presence of NADH [8].
  • Circular dichroism spectra were used to monitor the effect of phosphorylation on the following stages of the process: holoform formation from apo-E1 and thiamine pyrophosphate (TPP), substrate binding and active site deacetylation [9].

Biological context of thiamine diphosphate

  • Cocarboxylase inhibited deterioration in metabolic function as reflected by improved pH and base excess as well as maintenance of normal oxygen consumption [1].
  • Our analysis helps to further define the THI regulon and hence the spectrum of genes/proteins involved in the ThDP homeostasis [10].

Anatomical context of thiamine diphosphate

  • METHODS: Measurement of erythrocyte transketolase activity (ETK) and thiaminpyrophosphate (TPP) effect in 55 consecutive HIV-positive patients of a specialized outpatient clinic were grouped into five groups according to their CD4 counts [11].
  • In conclusion, this experiment suggests that cocarboxylase may be beneficial to ischemic canine myocardium by virtue of its favorable systemic hemodynamic effects [2].
  • During the reanimation the addition of ATP to the blood stimulated the restoration of RNA biosynthesis in the spinal cord to a considerable extent; the addition of cocarboxylase to the blood promoted cardiac RNA biosynthesis as well as cardiac and pancreatic DNA biosynthesis during recovery [12].
  • In particular, we identify novel proteins putatively involved in thiamine and/or ThDP transport across the plasma and the mitochondrial membrane [10].
  • Cocarboxylase, a radioprotector, improved these changes regarding the structures of the small intestine and also the GP of sublingual glands, stomach, small intestine and colon, demonstrating there its efficiency [13].

Associations of thiamine diphosphate with other chemical compounds


Gene context of thiamine diphosphate

  • The increase in the liver transketolase activity by the in vitro addition of cocarboxylase (TPP effect) was higher in group 3 than in group 4 although original transketolase activity was lower in group 4 [15].
  • The change in the energy barriers for the heterogeneous reduction of pyruvate decarboxylase (PDC) relative to its coenzyme, thiamin pyrophosphate (ThPP), was determined experimentally using square wave voltammetry (SWV) to be 5.3 kcal/mol [16].

Analytical, diagnostic and therapeutic context of thiamine diphosphate

  • Cysteine-cystine and IVX but not cocarboxylase supplementation allowed H. somnus to grow in Eagle minimal medium, a completely synthetic medium, but attempts at serial passage were unsuccessful [17].
  • In one group (Group II), cocarboxylase (150 mgm/kg) was given systematically via a central line 15 minutes and 45 minutes after ligation, while in Group I an equal amount of D5W was given [2].


  1. Effect of cocarboxylase in dogs subjected to experimental septic shock. Lindenbaum, G.A., Larrieu, A.J., Carroll, S.F., Kapusnick, R.A. Crit. Care Med. (1989) [Pubmed]
  2. Beneficial effects of cocarboxylase in the treatment of experimental myocardial infarction in dogs. Larrieu, A.J., Yazdanfar, S., Redovan, E., Eftychiadis, A., Kao, R., Silver, J., Ghosh, S.C. The American surgeon. (1987) [Pubmed]
  3. The influence of hepatic insufficiency due to alcoholic cirrhosis on the erythrocyte transketolase activity (ETKA). Graudal, N., Torp-Pedersen, K., Bonde, J., Hanel, H.K., Kristensen, M., Milman, N., Thomsen, A.C. Liver (1987) [Pubmed]
  4. Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens. Mosbacher, T.G., Mueller, M., Schulz, G.E. FEBS J. (2005) [Pubmed]
  5. Characterization of an ancestral type of pyruvate ferredoxin oxidoreductase from the hyperthermophilic bacterium, Thermotoga maritima. Blamey, J.M., Adams, M.W. Biochemistry (1994) [Pubmed]
  6. Pyruvate ferredoxin oxidoreductases of the hyperthermophilic archaeon, Pyrococcus furiosus, and the hyperthermophilic bacterium, Thermotoga maritima, have different catalytic mechanisms. Smith, E.T., Blamey, J.M., Adams, M.W. Biochemistry (1994) [Pubmed]
  7. Bromopyruvate as an active-site-directed inhibitor of the pyruvate dehydrogenase multienzyme complex from Escherichia coli. Lowe, P.N., Perham, R.N. Biochemistry (1984) [Pubmed]
  8. The elementary reactions of the pig heart pyruvate dehydrogenase complex. A study of the inhibition by phosphorylation. Walsh, D.A., Cooper, R.H., Denton, R.M., Bridges, B.J., Randle, P.J. Biochem. J. (1976) [Pubmed]
  9. The effect of phosphorylation on pyruvate dehydrogenase. Korotchkina, L.G., Khailova, L.S., Severin, S.E. FEBS Lett. (1995) [Pubmed]
  10. Pdc2 coordinates expression of the THI regulon in the yeast Saccharomyces cerevisiae. Mojzita, D., Hohmann, S. Mol. Genet. Genomics (2006) [Pubmed]
  11. Thiamin deficiency in HIV-positive patients: evaluation by erythrocyte transketolase activity and thiamin pyrophosphate effect. Müri, R.M., Von Overbeck, J., Furrer, J., Ballmer, P.E. Clinical nutrition (Edinburgh, Scotland) (1999) [Pubmed]
  12. Restoration of nucleic acid biosynthesis after clinical death and factors stimulating the process in vivo. Konikova, A.S., Petukhova, L.M., Pogossova, A.V., Vinarskaya, A.A., Nikulin, V.I. Resuscitation. (1975) [Pubmed]
  13. Histochemical changes in the digestive tract in irradiated rats. Groza, P., Boca, A., Gheorghe, N. Physiologie. (1987) [Pubmed]
  14. Cerebrospinal fluid levels of thiamine in patients with Parkinson's disease. Jiménez-Jiménez, F.J., Molina, J.A., Hernánz, A., Fernández-Vivancos, E., de Bustos, F., Barcenilla, B., Gómez-Escalonilla, C., Zurdo, M., Berbel, A., Villanueva, C. Neurosci. Lett. (1999) [Pubmed]
  15. Effect of ethanol administration on thiamine metabolism and transketolase activity in rats. Abe, T., Itokawa, Y. International journal for vitamin and nutrition research. Internationale Zeitschrift für Vitamin- und Ernährungsforschung. Journal international de vitaminologie et de nutrition. (1977) [Pubmed]
  16. The electrochemical investigation of the catalytic power of pyruvate decarboxylase and its coenzyme. Bell, P., Hoyt, K., Shabangi, M. Bioelectrochemistry (Amsterdam, Netherlands) (2006) [Pubmed]
  17. Growth requirements of Haemophilus somnus. Merino, M., Biberstein, E.L. J. Clin. Microbiol. (1982) [Pubmed]
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