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

bromopyruvate     3-bromo-2-oxo-propanoic acid

Synonyms: AGN-PC-0CXXE0, CHEMBL177837, ACMC-1C0WT, AG-K-49368, ANW-43645, ...
 
 
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 NSC62343

 

Psychiatry related information on NSC62343

  • Holeboard maze-learning deficits and brain monoaminergic neurotransmitter concentrations in rats after intracerebroventricular injection of 3-bromopyruvate [6].
  • Because comparable changes of PDHc and muscarinic receptors are found in dementia of Alzhemier type, the model of bromopyruvate inhibition of PDHc in rats is suggested to be useful for experimental dementia research [7].
 

High impact information on NSC62343

  • Covalent modification of an active site residue, Cys 191, by the inhibitor 3-bromopyruvate traps the enzyme in a catalytic conformation with the active site completely inaccessible to solvent [8].
  • Although glucose metabolism was preserved, indicating that the neuronal activities were enhanced, cerebral blood flow increase during cortical neuronal activation was abolished by bromopyruvate injection into only the cerebral cortex and not other cholinergic systems [9].
  • In extending these studies, 3-bromopyruvate was found to be over 20 times less effective in inhibiting glyceraldehyde-3-phosphate dehydrogenase in intact erythrocytes than in trypanosomal cells [10].
  • 2. Moreover the dependence of the reactivity of Cys-47 toward bromopyruvate and iodoacetamide with pH resembles that found for the functional sulfhydryls of thiol proteases, which have very low pKa values and exist mainly as a mercaptide-imidazole ion pair [11].
  • The phenylalanine-sensitive isozyme of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli was inactivated by the sulfhydryl modifying reagents 5,5-dithiobis-(2-nitrobenzoate), bromopyruvate, and N-ethylmaleimide and protected from inactivation by the presence of its metal activator, Mn2+, and substrate, phosphoenolpyruvate [12].
 

Chemical compound and disease context of NSC62343

 

Biological context of NSC62343

 

Anatomical context of NSC62343

 

Associations of NSC62343 with other chemical compounds

  • The Cys-294----Ser mutant enzyme is virtually identical to the wild type with respect to pyridoxal phosphate binding (KCO = 2 microM), cofactor absorption spectrum (lambda max = 420 and 337 nm) and pH dependence (pK alpha = 7.3), pH profile for catalysis, and rate of bromopyruvic acid inactivation [20].
  • A possible impact of this observation with respect to the different responses of isocitrate lyases and PrpB upon treatment with the common inhibitor 3-bromopyruvate is discussed [21].
  • In both types of inhibition of E1, reaction of 1 mol of bromopyruvate/mol of E1 chain is required for complete inactivation, and all the evidence is consistent with reaction taking place at or near the pyruvate binding site [22].
  • It is based on reaction of bromine with enolpyruvate in acid, derivatization of formed bromopyruvate with thionitrobenzoate, and resolution by reversed-phase HPLC of the thioether derivative [23].
  • Malic enzyme from pigeon liver is alkylated by the substrate analogue bromopyruvate, resulting in the concomitant loss of its oxidative decarboxylase and oxalacetate decarboxylase activities, but not its ability to reduce alpha-keto acids [17].
 

Gene context of NSC62343

 

Analytical, diagnostic and therapeutic context of NSC62343

  • Based on these observations and a report that KDO 8-P synthase is inactivated in a time-dependent manner with 3-bromopyruvate and that the substrate PEP protects against this inactivation, all four cysteines (38, 166, 206, and 249) were individually mutated to alanines via a modified PCR methodology [28].

References

  1. Active-site residues of 2-keto-4-hydroxyglutarate aldolase from Escherichia coli. Bromopyruvate inactivation and labeling of glutamate 45. Vlahos, C.J., Dekker, E.E. J. Biol. Chem. (1990) [Pubmed]
  2. Crystalline pyruvate, phosphate dikinase from Bacteroides symbiosus. Modification of essential histidyl residues and bromopyruvate inactivation. Yoshida, H., Wood, H.G. J. Biol. Chem. (1978) [Pubmed]
  3. Hexokinase II: cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondria. Mathupala, S.P., Ko, Y.H., Pedersen, P.L. Oncogene (2006) [Pubmed]
  4. Bromopyruvate inactivation of 2-keto-3-deoxy-6-phosphogalactonate aldolase of Pseudomonas saccharophila. Kinetics and stereochemistry. Meloche, H.P., Monti, C.T. Biochemistry (1975) [Pubmed]
  5. Renal and spermatozoal toxicity of alpha-bromohydrin, 3-bromolactate and 3-bromopyruvate. Jones, A.R., Porter, K.E., Dobbie, M.S. Journal of applied toxicology : JAT. (1996) [Pubmed]
  6. Holeboard maze-learning deficits and brain monoaminergic neurotransmitter concentrations in rats after intracerebroventricular injection of 3-bromopyruvate. Froelich, L., Ding, A., Hoyer, S. Pharmacol. Biochem. Behav. (1995) [Pubmed]
  7. Changes in pyruvate dehydrogenase complex (PDHc) activity and [3H]QNB-receptor binding in rat brain subsequent to intracerebroventricular injection of bromopyruvate. Frölich, L., Strauss, M., Kornhuber, J., Hoyer, S., Sorbi, S., Riederer, P., Amaducci, L. Journal of neural transmission. Parkinson's disease and dementia section. (1990) [Pubmed]
  8. Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis. Sharma, V., Sharma, S., Hoener zu Bentrup, K., McKinney, J.D., Russell, D.G., Jacobs, W.R., Sacchettini, J.C. Nat. Struct. Biol. (2000) [Pubmed]
  9. Focal cortical blood flow activation is regulated by intrinsic cortical cholinergic neurons. Fukuyama, H., Ouchi, Y., Matsuzaki, S., Ogawa, M., Yamauchi, H., Nagahama, Y., Kimura, J., Yonekura, Y., Shibasaki, H., Tsukada, H. Neuroimage (1996) [Pubmed]
  10. Glucose catabolism in African trypanosomes. Evidence that the terminal step is catalyzed by a pyruvate transporter capable of facilitating uptake of toxic analogs. Barnard, J.P., Reynafarje, B., Pedersen, P.L. J. Biol. Chem. (1993) [Pubmed]
  11. Peculiar spectroscopic and kinetic properties of Cys-47 in human placental glutathione transferase. Evidence for an atypical thiolate ion pair near the active site. Lo Bello, M., Parker, M.W., Desideri, A., Polticelli, F., Falconi, M., Del Boccio, G., Pennelli, A., Federici, G., Ricci, G. J. Biol. Chem. (1993) [Pubmed]
  12. Essential cysteines in 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. Analysis by chemical modification and site-directed mutagenesis of the phenylalanine-sensitive isozyme. Stephens, C.M., Bauerle, R. J. Biol. Chem. (1992) [Pubmed]
  13. Escherichia coli pyruvate dehydrogenase complex. Thiamin pyrophosphate-dependent inactivation by 3-bromopyruvate. Apfel, M.A., Ikeda, B.H., Speckhard, D.C., Frey, P.A. J. Biol. Chem. (1984) [Pubmed]
  14. 2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans: characterization and comparison of both enzymes. Brock, M., Darley, D., Textor, S., Buckel, W. Eur. J. Biochem. (2001) [Pubmed]
  15. Cross-linking between 16S ribosomal RNA and protein S4 in Escherichia coli ribosomal 30S subunits effected by treatment with bisulfite/hydrazine and bromopyruvate. Nitta, N., Kuge, O., Yui, S., Negishi, K., Hayatsu, H. Eur. J. Biochem. (1986) [Pubmed]
  16. Inactivation of H(+)-vacuolar ATPase by the energy blocker 3-bromopyruvate, a new antitumour agent. Dell'antone, P. Life Sci. (2006) [Pubmed]
  17. Mechanism of pigeon liver malic enzyme: kinetics, specificity, and half-site stoichiometry of the alkylation of a cysteinyl residue by the substrate-inhibitor bromopyruvate. Chang, G.G., Hsu, R.Y. Biochemistry (1977) [Pubmed]
  18. The anti-glycolytic activity of 3-bromopyruvate on mature boar spermatozoa in vitro. Jones, A.R., Gillan, L., Milmlow, D. Contraception. (1995) [Pubmed]
  19. Altered K+ current of ventricular myocytes in rats with chronic myocardial infarction. Rozanski, G.J., Xu, Z., Zhang, K., Patel, K.P. Am. J. Physiol. (1998) [Pubmed]
  20. Evidence that cysteine 298 is in the active site of tryptophan indole-lyase. Phillips, R.S., Gollnick, P.D. J. Biol. Chem. (1989) [Pubmed]
  21. Crystal structure of 2-methylisocitrate lyase (PrpB) from Escherichia coli and modelling of its ligand bound active centre. Grimm, C., Evers, A., Brock, M., Maerker, C., Klebe, G., Buckel, W., Reuter, K. J. Mol. Biol. (2003) [Pubmed]
  22. 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]
  23. Enolpyruvate: chemical determination as a pyruvate kinase intermediate. Seeholzer, S.H., Jaworowski, A., Rose, I.A. Biochemistry (1991) [Pubmed]
  24. Investigation of red blood cell carbonic anhydrase, glucose 6-phosphate dehydrogenase, hexokinase enzyme activities, and zinc concentration in patients with hyperthyroid diseases. Odçikin, E., Ozdemir, H., Ciftçi, M., Capoğlu, I. Endocr. Res. (2002) [Pubmed]
  25. Modification of yeast pyruvate kinase by an active site-directed reagent, bromopyruvate. Yun, S.L., Suelter, C.H. J. Biol. Chem. (1979) [Pubmed]
  26. Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization. Laber, B., Gomis-Rüth, F.X., Romão, M.J., Huber, R. Biochem. J. (1992) [Pubmed]
  27. Use of chemical modification in the crystallization of isocitrate lyase from Escherichia coli. Abeysinghe, S.I., Baker, P.J., Rice, D.W., Rodgers, H.F., Stillman, T.J., Ko, Y.H., McFadden, B.A., Nimmo, H.G. J. Mol. Biol. (1991) [Pubmed]
  28. Essential cysteines in 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase from Escherichia coli: analysis by chemical modification and site-directed mutagenesis. Salleh, H.M., Patel, M.A., Woodard, R.W. Biochemistry (1996) [Pubmed]
 
WikiGenes - Universities