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Gene Review

pck  -  phosphoenolpyruvate carboxykinase [ATP]

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3390, JW3366, pckA
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Disease relevance of pck


High impact information on pck


Chemical compound and disease context of pck


Biological context of pck


Associations of pck with chemical compounds


Other interactions of pck

  • Further increases in either Pck or Pps above the optimal levels become growth inhibitory, and the growth yield for oxygen is reduced, indicating less efficient growth [8].
  • The transcription start point for argH mRNA was determined by primer extension analysis and found to be within the coding sequence of the upstream gene, identified as the phosphoenolpyruvate carboxykinase gene (ppc) [16].

Analytical, diagnostic and therapeutic context of pck


  1. Crystallization of the calcium-activated phosphoenolpyruvate carboxykinase from Escherichia coli K12. Delbaere, L.T., Vandonselaar, M., Glaeske, D., Jabs, C., Goldie, H. J. Mol. Biol. (1991) [Pubmed]
  2. Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase. Tari, L.W., Matte, A., Pugazhenthi, U., Goldie, H., Delbaere, L.T. Nat. Struct. Biol. (1996) [Pubmed]
  3. Effect of overexpression of Actinobacillus succinogenes phosphoenolpyruvate carboxykinase on succinate production in Escherichia coli. Kim, P., Laivenieks, M., Vieille, C., Zeikus, J.G. Appl. Environ. Microbiol. (2004) [Pubmed]
  4. Metabolic responses to substrate futile cycling in Escherichia coli. Chao, Y.P., Liao, J.C. J. Biol. Chem. (1994) [Pubmed]
  5. The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3). Sudom, A.M., Prasad, L., Goldie, H., Delbaere, L.T. J. Mol. Biol. (2001) [Pubmed]
  6. Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold. Matte, A., Goldie, H., Sweet, R.M., Delbaere, L.T. J. Mol. Biol. (1996) [Pubmed]
  7. Mechanisms of activation of phosphoenolpyruvate carboxykinase from Escherichia coli by Ca2+ and of desensitization by trypsin. Sudom, A., Walters, R., Pastushok, L., Goldie, D., Prasad, L., Delbaere, L.T., Goldie, H. J. Bacteriol. (2003) [Pubmed]
  8. Control of gluconeogenic growth by pps and pck in Escherichia coli. Chao, Y.P., Patnaik, R., Roof, W.D., Young, R.F., Liao, J.C. J. Bacteriol. (1993) [Pubmed]
  9. A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring oxaloacetate decarboxylase activity. Hou, S.Y., Chao, Y.P., Liao, J.C. J. Bacteriol. (1995) [Pubmed]
  10. Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae. Medina, V., Pontarollo, R., Glaeske, D., Tabel, H., Goldie, H. J. Bacteriol. (1990) [Pubmed]
  11. Analysis of metabolic and physiological responses to gnd knockout in Escherichia coli by using C-13 tracer experiment and enzyme activity measurement. Jiao, Z., Baba, T., Mori, H., Shimizu, K. FEMS Microbiol. Lett. (2003) [Pubmed]
  12. Alteration of growth yield by overexpression of phosphoenolpyruvate carboxylase and phosphoenolpyruvate carboxykinase in Escherichia coli. Chao, Y.P., Liao, J.C. Appl. Environ. Microbiol. (1993) [Pubmed]
  13. Ascaris suum: cloning of a cDNA encoding phosphoenolpyruvate carboxykinase. Geary, T.G., Winterrowd, C.A., Alexander-Bowman, S.J., Favreau, M.A., Nulf, S.C., Klein, R.D. Exp. Parasitol. (1993) [Pubmed]
  14. Mutation Arg336 to Lys in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase originates an enzyme with increased oxaloacetate decarboxylase activity. Llanos, L., Briones, R., Yévenes, A., González-Nilo, F.D., Frey, P.A., Cardemil, E. FEBS Lett. (2001) [Pubmed]
  15. Genetic and physiological characterization of Escherichia coli mutants deficient in phosphoenolpyruvate carboxykinase activity. Goldie, A.H., Sanwal, B.D. J. Bacteriol. (1980) [Pubmed]
  16. Cloning, characterization, and nucleotide sequence analysis of the argH gene from Campylobacter jejuni TGH9011 encoding argininosuccinate lyase. Hani, E.K., Chan, V.L. J. Bacteriol. (1994) [Pubmed]
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