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Gene Review

ppc  -  phosphoenolpyruvate carboxylase

Escherichia coli O157:H7 str. EDL933

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Disease relevance of ppc

  • This fragment was able to complement the E. coli ppc mutant and conferred PEP carboxylase activity to the mutant [1].

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 [2].
  • 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) [2].
  • 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 [2].
  • 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 [2].
  • Collectively, these functional and structural observations implicate the importance of the PEPC C-terminal tetrapeptide for both catalysis and negative allosteric regulation [2].

Chemical compound and disease context of ppc


Biological context of ppc


Associations of ppc 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)(-) [5].
  • Conformational change of phosphoenolpyruvate carboxylase (orthophosphate: oxaloacetate carboxy-lyase (phosphorylating), EC induced by allosteric effectors was investigated using a hydrophobic probe, 1-anilinonaphthalene-8-sulfonate (ANS) [6].

Analytical, diagnostic and therapeutic context of ppc

  • Additionally, these DNAs yield segments, ordered from left to right, of length (in kilobases [kb]) determined by electron microscopy and 0.7% agarose slab gel electrophoresis as follows: lambdadarg13 (ppc argECBH bfe), 13.9, 2.8, 1.5, and 5.6; lambdadarg14 (ppc argECBH), 3.0, 2.0, 17.3, and 6.2; and lambdadarg23 (argECBH), 18.4 and 6 [7].


  1. The phosphoenolpyruvate carboxylase gene of Corynebacterium glutamicum: molecular cloning, nucleotide sequence, and expression. Eikmanns, B.J., Follettie, M.T., Griot, M.U., Sinskey, A.J. Mol. Gen. Genet. (1989) [Pubmed]
  2. 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]
  3. Phosphoenolpyruvate carboxylase of Escherichia coli. Hydrophobic chromatography using specific elution with allosteric inhibitor. Izui, K., Fujita, N., Katsuki, H. J. Biochem. (1982) [Pubmed]
  4. Construction of a plasmid for high level expression of Escherichia coli phosphoenolpyruvate carboxylase. Terada, K., Fujita, N., Katsuki, H., Izui, K. Biosci. Biotechnol. Biochem. (1995) [Pubmed]
  5. 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]
  6. Phosphoenolpyruvate carboxylase of Escherichia coli. Studies on multiple conformational states elicited by allosteric effectors with a fluorescent probe, 1-anilinonaphthalene-8-sulfonate. Yoshinaga, T. Biochim. Biophys. Acta (1976) [Pubmed]
  7. EcoRI cleavage sites in the argECBH region of the Escherichia coli chromosome. Devine, E.A., Moran, M.C., Jederlinic, P.J., Mazaitis, A.J., Vogel, H.J. J. Bacteriol. (1977) [Pubmed]
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