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Chemical Compound Review

phosphoenolpyruvate     2-phosphonooxyprop-2-enoate

Synonyms: P-enol-pyr, AG-G-92907, CHEBI:18021, AC1LCW46, CTK5D8854, ...
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Disease relevance of phosphoenolpyruvate


High impact information on phosphoenolpyruvate


Chemical compound and disease context of phosphoenolpyruvate


Biological context of phosphoenolpyruvate

  • IGF-1 receptor phosphorylation and coimmunoprecipitation of phosphatidylinositol3-kinase by antiphosphotyrosine antibodies was also observed in liver, and was associated with a decrease in mRNA levels of the key gluconeogenetic enzyme phosphoenolpyruvate carboxykinase [16].
  • Work on the phosphoenolpyruvate carboxykinase promoter using transgenic mice has been particularly informative: the cis-acting elements involved in hormonal regulation, tissue specificity and developmental inhibition of gene expression have been identified and their function in vivo examined [17].
  • Genetics of the bacterial phosphoenolpyruvate: glycose phosphotransferase system [18].
  • Glucagon and its second messenger, cAMP, are known to rapidly block expression of the L-type pyruvate kinase gene and to stimulate expression of phosphoenolpyruvate (PEP) carboxykinase gene in the liver in vivo [19].
  • In the absence of substrate this antitermination is prevented by the action of the product of gene bglF (the second gene of the operon), which encodes the beta-glucoside-specific transport protein (enzymeIIBgl of the phosphoenolpyruvate-dependent phosphotransferase system, PTS) resulting in repression of the operon [20].

Anatomical context of phosphoenolpyruvate


Associations of phosphoenolpyruvate with other chemical compounds


Gene context of phosphoenolpyruvate


Analytical, diagnostic and therapeutic context of phosphoenolpyruvate


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  3. The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression. Galinier, A., Haiech, J., Kilhoffer, M.C., Jaquinod, M., Stülke, J., Deutscher, J., Martin-Verstraete, I. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  4. Kinetic characterization and regulation of phosphoenolpyruvate-dependent methyl alpha-D-glucopyranoside transport by Salmonella typhimurium membrane vesicles. Liu, K.D., Roseman, S. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  5. Reevaluation of the accepted allosteric mechanism of phosphofructokinase from Bacillus stearothermophilus. Kimmel, J.L., Reinhart, G.D. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
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  13. 11beta-hydroxysteroid dehydrogenase type 1 knockout mice show attenuated glucocorticoid-inducible responses and resist hyperglycemia on obesity or stress. Kotelevtsev, Y., Holmes, M.C., Burchell, A., Houston, P.M., Schmoll, D., Jamieson, P., Best, R., Brown, R., Edwards, C.R., Seckl, J.R., Mullins, J.J. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  14. Fructose-specific phosphoenolpyruvate dependent phosphotransferase system of Escherichia coli: its alterations and adenylate cyclase activity. Gershanovitch, V.N., Bolshakova, T.N., Molchanova, M.L., Umyarov, A.M., Dobrynina OYu, n.u.l.l., Grigorenko YuA, n.u.l.l., Erlagaeva, R.S. FEMS Microbiol. Rev. (1989) [Pubmed]
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  17. Metabolic control of gene expression: in vivo studies with transgenic mice. McGrane, M.M., Yun, J.S., Patel, Y.M., Hanson, R.W. Trends Biochem. Sci. (1992) [Pubmed]
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  19. In vivo regulation of glycolytic and gluconeogenic enzyme gene expression in newborn rat liver. Lyonnet, S., Coupé, C., Girard, J., Kahn, A., Munnich, A. J. Clin. Invest. (1988) [Pubmed]
  20. Regulation of the bgl operon of Escherichia coli by transcriptional antitermination. Schnetz, K., Rak, B. EMBO J. (1988) [Pubmed]
  21. The phosphoenolpyruvate/phosphate translocator is required for phenolic metabolism, palisade cell development, and plastid-dependent nuclear gene expression. Streatfield, S.J., Weber, A., Kinsman, E.A., Häusler, R.E., Li, J., Post-Beittenmiller, D., Kaiser, W.M., Pyke, K.A., Flügge, U.I., Chory, J. Plant Cell (1999) [Pubmed]
  22. A new pyruvate kinase variant (PK Osaka) demonstrated by partial purification and condensation. Shinohara, K., Miwa, S., Nakashima, K., Oda, E., Kageoka, T. Am. J. Hum. Genet. (1976) [Pubmed]
  23. Regulation of hepatic fasting response by PPARgamma coactivator-1alpha (PGC-1): requirement for hepatocyte nuclear factor 4alpha in gluconeogenesis. Rhee, J., Inoue, Y., Yoon, J.C., Puigserver, P., Fan, M., Gonzalez, F.J., Spiegelman, B.M. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  24. A mutation in the peroxisome proliferator-activated receptor gamma-binding site in the gene for the cytosolic form of phosphoenolpyruvate carboxykinase reduces adipose tissue size and fat content in mice. Olswang, Y., Cohen, H., Papo, O., Cassuto, H., Croniger, C.M., Hakimi, P., Tilghman, S.M., Hanson, R.W., Reshef, L. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  25. Regulation of bacterial sugar-H+ symport by phosphoenolpyruvate-dependent enzyme I/HPr-mediated phosphorylation. Poolman, B., Knol, J., Mollet, B., Nieuwenhuis, B., Sulter, G. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
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