The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Chemical Compound Review

thiamine diphosphate     [2-[3-[(4-amino-2-methyl- pyrimidin-5...

Synonyms: ThDP, ThPP, thiamin-PPi, thiamine-PPi, SLV-319, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of thiamine diphosphate

  • Thiamine pyrophosphate (TPP) is synthesized de novo in Salmonella typhimurium and is a required cofactor for many enzymes in the cell [1].
  • Pediococcus sp. pyruvate oxidase, when introduced in the reaction mixture along with thiamine pyrophosphate (TPP) and flavin adenine dinucleotide (FAD), catalyzed the generation of acetyl phosphate from pyruvate and inorganic phosphate [2].
  • CONCLUSION: These findings justify the therapeutic application of BTMP in ESRD, because a high intracellular concentration of TDP may protect against numerous adverse effects of uremia in the long run [3].
  • Because of the essential role of TPP as a co-factor in intermediary metabolism, it is concluded that high doses of thiamine should be included in the routine nutritional management of patients with severe chronic liver disease [4].
  • We propose that paracatalytic reactions with O(2) catalyzed by PLP-dependent decarboxylases and by ThDP-dependent enzymes within the alpha-keto acid dehydrogenase complexes may contribute to normal cellular signaling and to cellular damage in neurodegenerative diseases [5].
 

Psychiatry related information on thiamine diphosphate

  • We found that the above-mentioned patient and one of the diabetic kindreds with no history of Wernicke's encephalopathy had abnormal transketolase as determined by its Km for TPP [6].
  • Activities of TPP-dependent enzymes appear to be deficient in the brain and perhaps in some peripheral tissues in patients with Alzheimer's disease [7].
  • Because of clinical and neuropathological overlap between the characteristics of dementia of the Alzheimer type (DAT) and of a human thiamin deficiency syndrome (Wernicke-Korsakoff syndrome), thiamin pyrophosphate (TPP) dependent processes have been studied in DAT brain and other tissues [8].
 

High impact information on thiamine diphosphate

  • Our results suggest that: 1) His291-alpha plays a structural rather than a catalytic role in the binding of cofactor ThDP and the lipoyl-bearing domain to E1b, and 2) His146-beta' is an essential catalytic residue, probably functioning as a proton donor in the reductive acylation of lipoamide on the lipoyl-bearing domain [9].
  • This decreased level of TPP, synthesized intracellularly from imported thiamin, resulted from RFC1-mediated efflux of TPP [10].
  • The rate of binding of thiamin-PPi to the enzyme and the subsequent enzyme activation are not limited by a reaction at C-2 of the thiazolium ring of thiamin-PPi since no kinetic isotope effect is observed when 2-D-thiamin-PPi is substituted for the protonated cofactor [11].
  • As we learn more about ThDP-dependent enzymes, we find an ever-expanding range of reactions that they are able to catalyze and see increased amino acid sequence heterogeneity [12].
  • Thiamine deficiency was confirmed by a decrease in blood thiamine concentration, a decrease in erythrocyte transketolase activity and an increase in thiamine pyrophosphate (TPP) effect [13].
 

Biological context of thiamine diphosphate

  • We report here that alterations of either His291-alpha or His146-beta' in the active site of human branched-chain alpha-ketoacid dehydrogenase (E1b) impede both the decarboxylation and the reductive acylation reactions catalyzed by E1b as well as the binding of cofactor thiamin diphosphate (ThDP) [9].
  • Only the subjects with persistently low TPP concentrations showed subjective benefits from treatment with improvements in quality of life (measured on a visual analogue scale; P = 0.02) and decreases in systolic blood pressure (P = 0.05) and weight (P < 0.01) when compared with subjects given placebo [14].
  • The DNA sequence had no significant homologue in the databases searched, whereas the derived amino acid sequence indicated an oxo-acid lyase, revealed a TPP-binding site and gave a derived molecular mass of 63.8 kDa [15].
  • One of these regions (157-182) includes a possible thiamin pyrophosphate (TPP) binding domain, and another (410-433) may contain the catalytic domain [16].
  • We measured the activity of the alpha-ketoglutarate dehydrogenase complex (alpha-KGDHC), a rate-limiting Krebs cycle enzyme, in postmortem brain samples from 38 controls and 30 neuropathologically confirmed Alzheimer's disease (AD) cases, in both the presence and absence of thiamine pyrophosphate (TPP), the enzyme's cofactor [17].
 

Anatomical context of thiamine diphosphate

  • In the absence of exogenously administered TPP, mean alpha-KGDHC activity was reduced to a slightly greater extent in all seven AD brain areas (-39 to -83%), with the reductions now reaching statistical significance in the four cerebral cortical areas and hippocampus [17].
  • As compared with the controls, mean alpha-KGDHC activity, with added TPP, was significantly (p < 0.005) reduced in AD brain in frontal (-56%), temporal (-60%), and parietal (-68%) cortices, with the reductions (-25 to -53%) in the occipital cortex, hippocampus, amygdala, and caudate failing to reach statistical significance [17].
  • Ovaries of immature and adult hamsters were incubated in medium containing thiamine pyrophosphate (TPP) to determine the age at which TPPase-reactive cytoplasmic structures first appear in the germ cells, and at what age the structures cease to be present [18].
  • At 1 and 4 weeks, the decrease in tissue TPP was significant in the liver (65% and 89%, respectively), gut (52% and 94%, respectively), spleen (40% and 60%, respectively), and skeletal muscle (37% and 76%, respectively), with the brain (7% and 84%, respectively) showing the slowest initial rate of depletion [19].
  • In particular, Tk derived from fibroblasts has been found to have an increased Km app for its cofactor thiamine pyrophosphate [TPP] and/or exist in different isoelectric forms in alcoholic patients with WKS as compared with unaffected individuals [20].
 

Associations of thiamine diphosphate with other chemical compounds

 

Gene context of thiamine diphosphate

 

Analytical, diagnostic and therapeutic context of thiamine diphosphate

  • The methods of erythrocyte transketolase activity and HPLC determination of thiamin pyrophosphate (TPP) for thiamin and erythrocyte glutathione reductase and HPLC determination of flavin adenine dinucleotide (FAD) for riboflavin were used [29].
  • In order to follow up the morphological changes of the rat liver as a reaction to the tumour graft, three groups of Guérin tumour-grafted animals were used: a first control group, a second one treated with leucotrophine (LT) and a third one treated with LT and thiamine diphosphate (TDP) [30].

References

  1. Identification and characterization of an operon in Salmonella typhimurium involved in thiamine biosynthesis. Petersen, L.A., Downs, D.M. J. Bacteriol. (1997) [Pubmed]
  2. Prolonging cell-free protein synthesis with a novel ATP regeneration system. Kim, D.M., Swartz, J.R. Biotechnol. Bioeng. (1999) [Pubmed]
  3. Alteration of thiamine pharmacokinetics by end-stage renal disease (ESRD). Frank, T., Bitsch, R., Maiwald, J., Stein, G. International journal of clinical pharmacology and therapeutics. (1999) [Pubmed]
  4. Red blood cell transketolase activity and the effect of thiamine supplementation in patients with chronic liver disease. Rossouw, J.E., Labadarios, D., Krasner, N., Davis, M., Williams, R. Scand. J. Gastroenterol. (1978) [Pubmed]
  5. Enzyme-Catalyzed Side Reactions with Molecular Oxygen may Contribute to Cell Signaling and Neurodegenerative Diseases. Bunik, V.I., Schloss, J.V., Pinto, J.T., Gibson, G.E., Cooper, A.J. Neurochem. Res. (2007) [Pubmed]
  6. Transketolase abnormality in tolazamide-induced Wernicke's encephalopathy. Mukherjee, A.B., Ghazanfari, A., Svoronos, S., Staton, R.C., Nakada, T., Kwee, I.L. Neurology (1986) [Pubmed]
  7. Reduced activities of thiamine-dependent enzymes in the brains and peripheral tissues of patients with Alzheimer's disease. Gibson, G.E., Sheu, K.F., Blass, J.P., Baker, A., Carlson, K.C., Harding, B., Perrino, P. Arch. Neurol. (1988) [Pubmed]
  8. Thiamin and Alzheimer's disease. Blass, J.P., Sheu, K.F., Cooper, A.J., Jung, E.H., Gibson, G.E. J. Nutr. Sci. Vitaminol. (1992) [Pubmed]
  9. Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase: refined phosphorylation loop structure in the active site. Wynn, R.M., Machius, M., Chuang, J.L., Li, J., Tomchick, D.R., Chuang, D.T. J. Biol. Chem. (2003) [Pubmed]
  10. Impact of the reduced folate carrier on the accumulation of active thiamin metabolites in murine leukemia cells. Zhao, R., Gao, F., Wang, Y., Diaz, G.A., Gelb, B.D., Goldman, I.D. J. Biol. Chem. (2001) [Pubmed]
  11. Regulation of the 2-oxoglutarate dehydrogenase lipoate succinyltransferase complex from cauliflower by nucleotide. Pre-steady state kinetics and physical studies. Craig, D.W., Wedding, R.T. J. Biol. Chem. (1980) [Pubmed]
  12. A new perspective on thiamine catalysis. Pohl, M., Sprenger, G.A., Müller, M. Curr. Opin. Biotechnol. (2004) [Pubmed]
  13. Reappearance of beriberi heart disease in Japan. A study of 23 cases. Kawai, C., Wakabayashi, A., Matsumura, T., Yui, Y. Am. J. Med. (1980) [Pubmed]
  14. The response to treatment of subclinical thiamine deficiency in the elderly. Wilkinson, T.J., Hanger, H.C., Elmslie, J., George, P.M., Sainsbury, R. Am. J. Clin. Nutr. (1997) [Pubmed]
  15. Sulphoacetaldehyde sulpho-lyase (EC 4.4.1.12) from Desulfonispora thiosulfatigenes: purification, properties and primary sequence. Denger, K., Ruff, J., Rein, U., Cook, A.M. Biochem. J. (2001) [Pubmed]
  16. DNA sequence of the yeast transketolase gene. Fletcher, T.S., Kwee, I.L., Nakada, T., Largman, C., Martin, B.M. Biochemistry (1992) [Pubmed]
  17. Brain alpha-ketoglutarate dehydrogenase complex activity in Alzheimer's disease. Mastrogiacomo, F., Bergeron, C., Kish, S.J. J. Neurochem. (1993) [Pubmed]
  18. Enzyme studies on TPPase-reactive cytoplasmic structures observed in early meiotic prophase I of the hamster oocyte. Weakley, B.S., Bowker, S.J., James, J.L. Cell Tissue Res. (1984) [Pubmed]
  19. Nutritional and metabolic characterization of a thiamine-deficient rat model. Molina, P.E., Myers, N., Smith, R.M., Lang, C.H., Yousef, K.A., Tepper, P.G., Abumrad, N.N. JPEN. Journal of parenteral and enteral nutrition. (1994) [Pubmed]
  20. Molecular genetics of transketolase in the pathogenesis of the Wernicke-Korsakoff syndrome. Martin, P.R., McCool, B.A., Singleton, C.K. Metabolic brain disease. (1995) [Pubmed]
  21. The biosynthesis of the thiazole phosphate moiety of thiamin: the sulfur transfer mediated by the sulfur carrier protein ThiS. Dorrestein, P.C., Zhai, H., McLafferty, F.W., Begley, T.P. Chem. Biol. (2004) [Pubmed]
  22. Effect of some monoamine oxidase inhibitors on the thiamin status of rabbits. Ali, B.H. Br. J. Pharmacol. (1985) [Pubmed]
  23. His103 in yeast transketolase is required for substrate recognition and catalysis. Wikner, C., Meshalkina, L., Nilsson, U., Bäckström, S., Lindqvist, Y., Schneider, G. Eur. J. Biochem. (1995) [Pubmed]
  24. Phosphatase localization in the endomembrane system of the dinoflagellate Crypthecodinium cohnii. Barlow, S.B., Triemer, R.E. J. Histochem. Cytochem. (1986) [Pubmed]
  25. Adenylate kinase 1 knockout mice have normal thiamine triphosphate levels. Makarchikov, A.F., Wins, P., Janssen, E., Wieringa, B., Grisar, T., Bettendorff, L. Biochim. Biophys. Acta (2002) [Pubmed]
  26. Thiamine homeostasis in neuroblastoma cells. Bettendorff, L. Neurochem. Int. (1995) [Pubmed]
  27. The relationship between plasma and red cell B-vitamin concentrations in critically-ill patients. Quasim, T., McMillan, D.C., Talwar, D., Vasilaki, A., St J O'Reilly, D., Kinsella, J. Clinical nutrition (Edinburgh, Scotland) (2005) [Pubmed]
  28. Evidence for in vivo synthesis of thiamin triphosphate by cytosolic adenylate kinase in chicken skeletal muscle. Miyoshi, K., Egi, Y., Shioda, T., Kawasaki, T. J. Biochem. (1990) [Pubmed]
  29. Comparison of methods for thiamin and riboflavin nutriture in man. Fidanza, F., Simonetti, M.S., Floridi, A., Codini, M., Fidanza, R. International journal for vitamin and nutrition research. Internationale Zeitschrift für Vitamin- und Ernährungsforschung. Journal international de vitaminologie et de nutrition. (1989) [Pubmed]
  30. Histochemical and histoenzymatic liver changes in Guérin tumour-grafted rats. Bădescu, A., Cotuţiu, C., Mârza, D. Morphologie et embryologie. (1981) [Pubmed]
 
WikiGenes - Universities