Genomes and Genes
Gene Symbol: ppc
Description: phosphoenolpyruvate carboxylase
Alias: ECK3947, JW3928, asp, glu
Species: Escherichia coli str. K-12 substr. MG1655
- Coomes M, Mitchell B, Beezley A, Smith T. Properties of an Escherichia coli mutant deficient in phosphoenolpyruvate carboxylase catalytic activity. J Bacteriol. 1985;164:646-52 pubmed..A novel method for showing that these bands represented proteolytic fragments of phosphoenolpyruvate carboxylase was developed. ..
- Kwon Y, Kwon O, Lee H, Kim P. The effect of NADP-dependent malic enzyme expression and anaerobic C4 metabolism in Escherichia coli compared with other anaplerotic enzymes. J Appl Microbiol. 2007;103:2340-5 pubmed..malic enzyme (MaeB), as well as the other anaplerotic enzymes, including phosphoenolpyruvate carboxylase (Ppc), phosphoenolpyruvate carboxykinase (Pck) and NAD-dependent malic enzyme (MaeA), were artificially expressed and ..
- Lin H, Vadali R, Bennett G, San K. Increasing the acetyl-CoA pool in the presence of overexpressed phosphoenolpyruvate carboxylase or pyruvate carboxylase enhances succinate production in Escherichia coli. Biotechnol Prog. 2004;20:1599-604 pubmed..The study also demonstrates a feasible method for metabolic engineering to modulate enzyme activity in vivo through specific activators and inhibitors. ..
- Siddiquee K, Arauzo Bravo M, Shimizu K. Effect of a pyruvate kinase (pykF-gene) knockout mutation on the control of gene expression and metabolic fluxes in Escherichia coli. FEMS Microbiol Lett. 2004;235:25-33 pubmed..RT-PCR revealed that the glycolytic genes such as glk, pgi, pfkA and tpiA were down regulated, that ppc, pckA, maeB and mdh genes were strongly up-regulated, and that the oxidative pentose phosphate pathway genes such ..
- Terada K, Murata T, Izui K. Site-directed mutagenesis of phosphoenolpyruvate carboxylase from E. coli: the role of His579 in the catalytic and regulatory functions. J Biochem. 1991;109:49-54 pubmed..It was concluded that the imidazole group of His579 is not obligatory for the enzyme catalysis, but plays important roles in catalytic and regulatory functions. ..
- Lee B, Yen J, Yang L, Liao J. Incorporating qualitative knowledge in enzyme kinetic models using fuzzy logic. Biotechnol Bioeng. 1999;62:722-9 pubmed..The resulting models, even though they do not provide additional physical meaning in enzyme mechanisms, allow the model to incorporate semiquantitative information in metabolic pathway models. ..
- Yoshinaga T. Structural specificity of the allosteric inhibitor of phosphoenolpyruvate carboxylase of Escherichia coli. J Biochem. 1977;81:665-71 pubmed..For the photooxidized enzyme, oxaloacetate and L-malate were relatively strong inhibitors wiht I0.5 values of about 11-16 mM. The results obtained suggest that the inhibition of the native enzyme mainly reflects allosteric inhibition. ..
- Kameshita I, Tokushige M, Izui K, Katsuki H. Phosphoenolpyruvate carboxylase of Escherichia coli. Affinity labeling with bromopyruvate. J Biochem. 1979;86:1251-7 pubmed..The results indicate that bromopyruvate reacted with the enzyme as an active-site-directed reagent. ..
- Ravanal M, Goldie H, Cardemil E. Thermal stability of phosphoenolpyruvate carboxykinases from Escherichia coli, Trypanosoma brucei, and Saccharomyces cerevisiae. J Protein Chem. 2003;22:311-5 pubmed..We propose that the higher structural complexity of some PEP carboxykinases could be related to the acquisition of properties of relevance in vivo. ..
- Sabe H, Miwa T, Kodaki T, Izui K, Hiraga S, Katsuki H. Molecular cloning of the phosphoenolpyruvate carboxylase gene, ppc, of Escherichia coli. Gene. 1984;31:279-83 pubmedThe ColE1 hybrid plasmid, pLC20-10, carrying the ppc gene and the argECBH gene cluster of Escherichia coli K-12, was characterized. The ppc gene coding for phosphoenolpyruvate carboxylase (EC 4.1.1...
- Terada K, Izui K. Site-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase. His138 is essential for the second partial reaction. Eur J Biochem. 1991;202:797-803 pubmed..Mutation of His579 to asparagine (H579N) produced an enzyme which had 69% of the wild-type carboxylase activity, but its affinity for P-pyruvate was decreased by 24-fold. ..
- Kameshita I, Tokushige M, Katsuki H. Phosphoenolpyruvate carboxylase of Escherichia coli. Essential arginyl residues for catalytic and regulatory functions. J Biochem. 1978;84:795-803 pubmed
- Alper H, Fischer C, Nevoigt E, Stephanopoulos G. Tuning genetic control through promoter engineering. Proc Natl Acad Sci U S A. 2005;102:12678-83 pubmed..The multifaceted characterization of promoter strength enabled identification of optimal expression levels for ppc and dxs, which maximized the desired phenotype...
- Moran M, Mazaitis A, Vogel R, Vogel H. Clustered arg genes on a BamHI segment of the Escherichia coli chromosome. Gene. 1979;8:25-34 pubmedBamHI cleavage of DNAs from transducing phages gamma darg13 (ppc, argECBH, bfe), gamma darg14 (ppc, argECBH) and gamma darg23 (argECBH) yields three purely gamma DNA segments (and, in one case, a fourth), as well as several Excherichia ..
- Tomar A, Eiteman M, Altman E. The effect of acetate pathway mutations on the production of pyruvate in Escherichia coli. Appl Microbiol Biotechnol. 2003;62:76-82 pubmedWe compared pyruvate accumulation in six strains of Escherichia coli and their corresponding ppc mutants. Each strain contained a mutation of a gene involved in the pathway to acetate synthesis...
- Matsumura H, Xie Y, Shirakata S, Inoue T, Yoshinaga T, Ueno Y, et al. Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases. Structure. 2002;10:1721-30 pubmed..On the basis of these molecular structures, the mechanisms for the carboxylation reaction and for the allosteric regulation of PEPC are proposed. ..
- Meinnel T, Schmitt E, Mechulam Y, Blanquet S. Structural and biochemical characterization of the Escherichia coli argE gene product. J Bacteriol. 1992;174:2323-31 pubmed..The nucleotide sequence of the ppc-argE intergenic region was also solved and shown to contain six tandemly repeated REP sequences...
- VanBogelen R, Sankar P, Clark R, Bogan J, Neidhardt F. The gene-protein database of Escherichia coli: edition 5. Electrophoresis. 1992;13:1014-54 pubmed..It will be updated twice yearly. This edition of the gene-protein database is estimated to contain entries for one-sixth of the protein-encoding genes of E. coli. ..
- Kai Y, Matsumura H, Izui K. Phosphoenolpyruvate carboxylase: three-dimensional structure and molecular mechanisms. Arch Biochem Biophys. 2003;414:170-9 pubmed..Information derived from these three-dimensional structures, combined with related biochemical studies, has established models for the reaction mechanism and allosteric regulation of this important C-fixing enzyme. ..
- Izui K, Matsumura H, Furumoto T, Kai Y. Phosphoenolpyruvate carboxylase: a new era of structural biology. Annu Rev Plant Biol. 2004;55:69-84 pubmed..We present the reaction mechanism of PEPC in which we assign the roles of individual amino acid residues. We discuss the unique molecular property of PEPC kinase and its possible regulation at the post-translational level. ..
- Peng L, Shimizu K. Effect of ppc gene knockout on the metabolism of Escherichia coli in view of gene expressions, enzyme activities and intracellular metabolite concentrations. Appl Microbiol Biotechnol. 2004;: pubmed..comparative analyses of gene expressions, enzyme activities and intracellular metabolite concentrations between the ppc knockout Escherichia coli strain JWK3928 and its parent strain BW25113...
- Kai Y, Matsumura H, Inoue T, Terada K, Nagara Y, Yoshinaga T, et al. Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition. Proc Natl Acad Sci U S A. 1999;96:823-8 pubmed..The importance of this loop in catalytic activity was also shown. Thus, the crystal-structure determination of PEPC revealed two mobile loops bearing the enzymatic functions and accompanying allosteric inhibition by L-aspartate. ..
- Fong S, Palsson B. Metabolic gene-deletion strains of Escherichia coli evolve to computationally predicted growth phenotypes. Nat Genet. 2004;36:1056-8 pubmed..These results show that computational models can be used to predict the eventual effects of genetic modifications. ..
- Millard C, Chao Y, Liao J, Donnelly M. Enhanced production of succinic acid by overexpression of phosphoenolpyruvate carboxylase in Escherichia coli. Appl Environ Microbiol. 1996;62:1808-10 pubmed..Under optimized conditions, induction of the carboxylase resulted in a 3.5-fold increase in the concentration of succinic acid, making succinic acid the major fermentation product by weight. ..
- Yano M, Terada K, Umiji K, Izui K. Catalytic role of an arginine residue in the highly conserved and unique sequence of phosphoenolpyruvate carboxylase. J Biochem. 1995;117:1196-200 pubmed..5) of HCO3- in R587S was about 100-fold that in the wild-type enzyme, whereas the respective values for PEP and Mg2+ were 20- and 15-fold, indicative of this residue participating in the binding of HCO3-. ..
- Fong S, Nanchen A, Palsson B, Sauer U. Latent pathway activation and increased pathway capacity enable Escherichia coli adaptation to loss of key metabolic enzymes. J Biol Chem. 2006;281:8024-33 pubmed..that underlie adaptive evolution of four metabolic gene deletion mutants of Escherichia coli (delta pgi, delta ppc, delta pta, and delta tpi) in parallel evolution experiments of each mutant...
- Zhu J, Shimizu K. Effect of a single-gene knockout on the metabolic regulation in Escherichia coli for D-lactate production under microaerobic condition. Metab Eng. 2005;7:104-15 pubmedThe effects of several single-gene knockout mutants (pykF, ppc, pflA, pta, and adhE mutants) on the metabolic flux distribution in Escherichia coli were investigated under microaerobic condition...
- Fujita N, Miwa T, Ishijima S, Izui K, Katsuki H. The primary structure of phosphoenolpyruvate carboxylase of Escherichia coli. Nucleotide sequence of the ppc gene and deduced amino acid sequence. J Biochem. 1984;95:909-16 pubmedThe nucleotide sequence of the ppc gene, the structural gene for phosphoenolpyruvate carboxylase [EC 220.127.116.11], of Escherichia coli K-12 was determined...
- Izui K, Miwa T, Kajitani M, Fujita N, Sabe H, Ishihama A, et al. Promoter analysis of the phosphoenolpyruvate carboxylase gene of Escherichia coli. Nucleic Acids Res. 1985;13:59-71 pubmedIn order to find the promoter region of phosphoenolpyruvate carboxylase [EC 18.104.22.168] gene (ppc), in vitro transcription was performed using truncated DNA fragments as templates...
- De Maeseneire S, De Mey M, Vandedrinck S, Vandamme E. Metabolic characterisation of E. coli citrate synthase and phosphoenolpyruvate carboxylase mutants in aerobic cultures. Biotechnol Lett. 2006;28:1945-53 pubmed..Here we examine if over-expression of citrate synthase (gltA) or phosphoenolpyruvate carboxylase (ppc) can eliminate acetate production. Knock-out as well as over-expression mutants were constructed and characterized...