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Gene Review

ECs4245  -  phosphoenolpyruvate carboxykinase

Escherichia coli O157:H7 str. Sakai

 
 
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Disease relevance of ECs4245

 

High impact information on ECs4245

  • Before the elucidation of the three-dimensional structures of maize C4 leaf and Escherichia coli PEPC, our truncation analysis of the sorghum C4 homologue revealed important roles for the enzyme's C-terminal alpha-helix and its appended QNTG961 tetrapeptide in polypeptide stability and overall catalysis, respectively [3].
  • We have now more finely dissected this element of PEPC structure-function by modification of the absolutely conserved C-terminal glycine of the sorghum C4 isoform by site-specific mutagenesis (G961(A/V/D)) and truncation (DeltaC1/C4) [3].
  • The importance of the strictly conserved, C-terminal glycine residue in phosphoenolpyruvate carboxylase for overall catalysis: mutagenesis and truncation of GLY-961 in the sorghum C4 leaf isoform [3].
  • Although the C4 polypeptide failed to accumulate in a PEPC- strain (XH11) of E. coli transformed with the Asp mutant, the other variants were produced at wild-type levels [3].
  • Collectively, these functional and structural observations implicate the importance of the PEPC C-terminal tetrapeptide for both catalysis and negative allosteric regulation [3].
 

Chemical compound and disease context of ECs4245

  • Finally, two reactions catalyzed by PEP carboxykinase and malic enzyme were identified by METAFoR analysis; these had previously been considered absent in E. coli cells grown in glucose-containing media [4].
  • The unfolding behaviour of S. cerevisiae PEP carboxykinase was found to be similar to that of E. coli PEP carboxykinase, however all steps take place at lower urea concentrations [5].
  • Combining the measurement data of in vivo fluxes, metabolite concentrations and enzyme activities, the in vivo regulations of PEP carboxykinase flux, PEP carboxylation, and glyoxylate shunt in E. coli are discussed [6].
  • Comparison with the crystalline structure of homologous Escherichia coli PEP carboxykinase [Tari et al. Nature Struct. Biol. 4 (1997) 990-994] shows that Lys(213) is one of the ligands to Mn(2+) at the enzyme active site [7].
  • Comparison with the crystalline structure of homologous E. coli PEP carboxykinase [Tari, L. W., Matte, A., Goldie, H., and Delbaere, L. T. J. (1997). Nature Struct. Biol. 4, 990-994] suggests that His225, Asp262, Asp263, and Thr249 are located in the active site of the protein, interacting with manganese ions [8].
 

Biological context of ECs4245

  • Key reactions are the constituents of the glyoxylate shunt and PEP carboxykinase, whose conjoint operation in this bi-functional catabolic and anabolic cycle is in sharp contrast to their generally recognized functions in anaplerosis and gluconeogenesis, respectively [9].
  • Growth in pyruvate was slowed down in the transformed strain, likely due to a futile cycle produced by the simultaneous action of PEP carboxykinase and PEP carboxylase [10].
  • A chromosomal mutation in the gutR gene, which gave rise to constitutive expression of the chromosomal gut operon, also gave rise to growth inhibition on gluconeogenic substrates as well as reduced phosphoenolpyruvate carboxykinase activity [11].
  • Backward flux from the TCA cycle to glycolysis, as indicated by significant activity of PEP carboxykinase, was found only in glucose-limited chemostat culture, demonstrating that control of this futile cycle activity is relaxed under severe glucose limitation [4].
 

Associations of ECs4245 with chemical compounds

  • A similar dissociation constant was obtained by analysis of the competitive inhibition of the CmpA protein on the carboxylation of phosphoenolpyruvate by phosphoenolpyruvate carboxylase at limiting concentrations of HCO(3)(-) [12].
  • These results suggest that high-level expression of the glucitol enzyme III of the phosphotransferase system can negatively regulate gluconeogenesis by repression or inhibition of the two key gluconeogenic enzymes, phosphoenolpyruvate carboxykinase and phosphoenolpyruvate synthase [11].
  • Flux analysis of pck deletion mutant revealed that abolishment of PEP carboxykinase activity resulted in a remarkably reduced flux through the anaplerotic PEP carboxylase and the activation of the glyoxylate shunt, with 23% of isocitrate found being channeled in the glyoxylate shunt [6].
  • For the cytosolic rat liver PEP carboxykinase, the respective values for GDP, IDP and ITP binding are 6 +/- 0.5 microM, 6.7 +/- 0.4 microM and 10.1 +/- 1.7 microM [13].
 

Analytical, diagnostic and therapeutic context of ECs4245

References

  1. 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]
  2. Crystal structure of Anaerobiospirillum succiniciproducens PEP carboxykinase reveals an important active site loop. Cotelesage, J.J., Prasad, L., Zeikus, J.G., Laivenieks, M., Delbaere, L.T. Int. J. Biochem. Cell Biol. (2005) [Pubmed]
  3. The importance of the strictly conserved, C-terminal glycine residue in phosphoenolpyruvate carboxylase for overall catalysis: mutagenesis and truncation of GLY-961 in the sorghum C4 leaf isoform. Xu, W., Ahmed, S., Moriyama, H., Chollet, R. J. Biol. Chem. (2006) [Pubmed]
  4. Metabolic flux ratio analysis of genetic and environmental modulations of Escherichia coli central carbon metabolism. Sauer, U., Lasko, D.R., Fiaux, J., Hochuli, M., Glaser, R., Szyperski, T., Wüthrich, K., Bailey, J.E. J. Bacteriol. (1999) [Pubmed]
  5. Urea-induced unfolding studies of free- and ligand-bound tetrameric ATP-dependent Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase. Influence of quaternary structure on protein conformational stability. Encinas, M.V., González-Nilo, F.D., Andreu, J.M., Alfonso, C., Cardemil, E. Int. J. Biochem. Cell Biol. (2002) [Pubmed]
  6. Analysis of Escherichia coli anaplerotic metabolism and its regulation mechanisms from the metabolic responses to altered dilution rates and phosphoenolpyruvate carboxykinase knockout. Yang, C., Hua, Q., Baba, T., Mori, H., Shimizu, K. Biotechnol. Bioeng. (2003) [Pubmed]
  7. Site-directed mutagenesis study of the microenvironment characteristics of Lys213 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase. Yévenes, A., Espinoza, R., Rivas-Pardo, J.A., Villarreal, J.M., González-Nilo, F.D., Cardemil, E. Biochimie (2006) [Pubmed]
  8. Evaluation by site-directed mutagenesis of active site amino acid residues of Anaerobiospirillum succiniciproducens phosphoenolpyruvate carboxykinase. Jabalquinto, A.M., Laivenieks, M., González-Nilo, F.D., Yévenes, A., Encinas, M.V., Zeikus, J.G., Cardemil, E. J. Protein Chem. (2002) [Pubmed]
  9. A novel metabolic cycle catalyzes glucose oxidation and anaplerosis in hungry Escherichia coli. Fischer, E., Sauer, U. J. Biol. Chem. (2003) [Pubmed]
  10. Expression of PEP carboxylase from Escherichia coli complements the phenotypic effects of pyruvate carboxylase mutations in Saccharomyces cerevisiae. Flores, C.L., Gancedo, C. FEBS Lett. (1997) [Pubmed]
  11. Regulation of gluconeogenesis by the glucitol enzyme III of the phosphotransferase system in Escherichia coli. Yamada, M., Feucht, B.U., Saier, M.H. J. Bacteriol. (1987) [Pubmed]
  12. Bicarbonate binding activity of the CmpA protein of the cyanobacterium Synechococcus sp. strain PCC 7942 involved in active transport of bicarbonate. Maeda, S., Price, G.D., Badger, M.R., Enomoto, C., Omata, T. J. Biol. Chem. (2000) [Pubmed]
  13. Comparative steady-state fluorescence studies of cytosolic rat liver (GTP), Saccharomyces cerevisiae (ATP) and Escherichia coli (ATP) phospho enol pyruvate carboxykinases. Encinas, M.V., Rojas, M.C., Goldie, H., Cardemil, E. Biochim. Biophys. Acta (1993) [Pubmed]
  14. A rapeseed cold-inducible transcript encodes a phosphoenolpyruvate carboxykinase. Sáez-Vásquez, J., Raynal, M., Delseny, M. Plant Physiol. (1995) [Pubmed]
 
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