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Gene Review

ppc  -  phosphoenolpyruvate carboxylase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3947, JW3928, asp, glu
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Disease relevance of ppc


High impact information on ppc

  • 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 [4].
  • Collectively, these functional and structural observations implicate the importance of the PEPC C-terminal tetrapeptide for both catalysis and negative allosteric regulation [4].
  • 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) [4].
  • 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 [4].
  • 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 [4].

Chemical compound and disease context of ppc


Biological context of ppc


Associations of ppc with chemical compounds

  • Strain ALS961 (YYC202 ppc) prevented succinate accumulation, but growth was very poor [13].
  • For example, the glucose transport genes (ptsHI, ptsG, crr) in both acetate and glycerol media were down-regulated, and the ppc, glycolytic, and biosynthetic genes in acetate were also down-regulated because of the reduced fluxes [14].
  • The model study of Mn2+-bound PEPC complexed with phosphoenolpyruvate (PEP) reveals that the side chains of Arg-396, Arg-581 and Arg-713 could interact with PEP [5].
  • In light of the important position of pyruvate at the juncture of NADH-generating pathways and NADH-dissimilating branches, the results show that when PPC or PYC is expressed, the metabolic network adapts by altering the flux to lactate and the molar ratio of ethanol to acetate formation [15].
  • Histidine residues have previously been suggested to be essential for the activity of phosphoenolpyruvate carboxylase as demonstrated by chemical modification of these residues [16].

Other interactions of ppc

  • Over-expression of ppc or gltA increased the maximum cell dry weight by 91% and 23%, respectively [9].
  • The coordination sphere of Mn2+ observed in E. coli PEPC is similar to that of Mn2+ found in the pyruvate kinase structure [5].
  • The nucleotide sequence of the ppc-argE intergenic region was also solved and shown to contain six tandemly repeated REP sequences [17].

Analytical, diagnostic and therapeutic context of ppc


  1. The primary structure of phosphoenolpyruvate carboxylase of Escherichia coli. Nucleotide sequence of the ppc gene and deduced amino acid sequence. Fujita, N., Miwa, T., Ishijima, S., Izui, K., Katsuki, H. J. Biochem. (1984) [Pubmed]
  2. Identification, sequence analysis, and expression of a Corynebacterium glutamicum gene cluster encoding the three glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and triosephosphate isomerase. Eikmanns, B.J. J. Bacteriol. (1992) [Pubmed]
  3. Clustered arg genes on a BamHI segment of the Escherichia coli chromosome. Moran, M.C., Mazaitis, A.J., Vogel, R.H., Vogel, H.J. Gene (1979) [Pubmed]
  4. 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]
  5. Plausible phosphoenolpyruvate binding site revealed by 2.6 A structure of Mn2+-bound phosphoenolpyruvate carboxylase from Escherichia coli. Matsumura, H., Terada, M., Shirakata, S., Inoue, T., Yoshinaga, T., Izui, K., Kai, Y. FEBS Lett. (1999) [Pubmed]
  6. Transcriptional analysis of the gap-pgk-tpi-ppc gene cluster of Corynebacterium glutamicum. Schwinde, J.W., Thum-Schmitz, N., Eikmanns, B.J., Sahm, H. J. Bacteriol. (1993) [Pubmed]
  7. First crystallization of a phosphoenolpyruvate carboxylase from Escherichia coli. Inoue, M., Hayashi, M., Sugimoto, M., Harada, S., Kai, Y., Kasai, N., Terada, K., Izui, K. J. Mol. Biol. (1989) [Pubmed]
  8. Enhanced production of succinic acid by overexpression of phosphoenolpyruvate carboxylase in Escherichia coli. Millard, C.S., Chao, Y.P., Liao, J.C., Donnelly, M.I. Appl. Environ. Microbiol. (1996) [Pubmed]
  9. Metabolic characterisation of E. coli citrate synthase and phosphoenolpyruvate carboxylase mutants in aerobic cultures. De Maeseneire, S.L., De Mey, M., Vandedrinck, S., Vandamme, E.J. Biotechnol. Lett. (2006) [Pubmed]
  10. 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]
  11. Metabolic responses to substrate futile cycling in Escherichia coli. Chao, Y.P., Liao, J.C. J. Biol. Chem. (1994) [Pubmed]
  12. Glucose metabolism at high density growth of E. coli B and E. coli K: differences in metabolic pathways are responsible for efficient glucose utilization in E. coli B as determined by microarrays and Northern blot analyses. Phue, J.N., Noronha, S.B., Hattacharyya, R., Wolfe, A.J., Shiloach, J. Biotechnol. Bioeng. (2005) [Pubmed]
  13. Homolactate Fermentation by Metabolically Engineered Escherichia coli Strains. Zhu, Y., Eiteman, M.A., Dewitt, K., Altman, E. Appl. Environ. Microbiol. (2007) [Pubmed]
  14. Gene expression profiling by DNA microarrays and metabolic fluxes in Escherichia coli. Oh, M.K., Liao, J.C. Biotechnol. Prog. (2000) [Pubmed]
  15. Metabolic analysis of Escherichia coli in the presence and absence of the carboxylating enzymes phosphoenolpyruvate carboxylase and pyruvate carboxylase. Gokarn, R.R., Eiteman, M.A., Altman, E. Appl. Environ. Microbiol. (2000) [Pubmed]
  16. Site-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase. His138 is essential for the second partial reaction. Terada, K., Izui, K. Eur. J. Biochem. (1991) [Pubmed]
  17. Structural and biochemical characterization of the Escherichia coli argE gene product. Meinnel, T., Schmitt, E., Mechulam, Y., Blanquet, S. J. Bacteriol. (1992) [Pubmed]
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