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Gene Review

pykF  -  pyruvate kinase I

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1672, JW1666
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Disease relevance of pykF


High impact information on pykF

  • From these results, we concluded that enzymatic stability of the variant was affected by the point mutation of the PK-encoding gene [4].
  • To confirm that the nucleotide change was responsible for the variant phenotype, we expressed the L-type PK with the single amino acid change in Escherichia coli and characterized the enzyme [4].
  • cDNA clones for human R-type pyruvate kinase (PK) were isolated from a human reticulocyte cDNA library, constructed by PCR with a single gene-specific primer [4].
  • The full-length cDNA was 2060 base pairs long, and the cDNA encoded 574 amino acids, the same number as that by rat R-type PK [4].
  • The variant PK was thermolabile and moved slowly in the polyacrylamide gel buffered in 10 mM Tris.HCl, pH 8.3; these characteristics were fully compatible with data obtained from the patient's PK [4].

Chemical compound and disease context of pykF

  • Cloning of the two pyruvate kinase isoenzyme structural genes from Escherichia coli: the relative roles of these enzymes in pyruvate biosynthesis [1].
  • The metabolic response to edd gene knockout in Escherichia coli JM101 and PTS- Glc+ was investigated in gluconate and glucose batch cultures and compared with other pyruvate kinase and PTS mutants previously constructed [6].
  • Based on measurements and theoretical analyses, we identified deletion of pyruvate kinase (PYK) activity as a possible route for elimination of acid formation in Bacillus subtilis cultures grown on glucose minimal media [5].
  • It is known that pyruvate kinase of E. coli becomes inactive upon prolonged dialysis in the absence of a reducing reagent, such as dithiothreitol and that the inactive enzyme is reactivated if dithiothretiol is added [7].
  • Primary structure of three peptides at the catalytic and allosteric sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli [8].

Biological context of pykF


Anatomical context of pykF

  • Membranes from cells harvested at late exponential phase showed NTP-synthesizing activity and the physical presence of Ndk but not of Pk or Pra [11].
  • At these low levels of heterologous gene expression, comparison of the distribution of PYK and PYK/LacZ transcripts across polysome gradients revealed no significant effect mediated by their striking disparity in codon usage [12].
  • Nevertheless, upon increasing B-galactosidase mRNA levels, via manipulation of plasmid copy number, a distinct decline in ribosome loading was observed for the heterologous PYK/LacZ transcript which was not mirrored by either endogenous PYK transcripts or other yeast mRNAs of high (Ribosomal protein 1) or moderate (Actin) codon bias [12].

Associations of pykF with chemical compounds

  • In contrast, due to decreased availability of pyruvate (and acetyl coenzyme A) in the pykF mutant compared with the wild type, low flux ratios were found through lactate and acetate forming pathways [9].
  • Moreover, the overall activity of the ED pathway on gluconate resulted in important increments in PTS- Glc+ and PTS- Glc+ pykF mutants [6].
  • It was also found for continuous cultivation that the enzyme activities of the oxidative PP and Entner-Doudoroff pathways increased as the dilution rate increased for the pykF- mutant [13].
  • Expression of both isoenzymes was generally higher during xylose fermentation but statistically higher in both strains only for pykF encoding the isoenzyme activated by fructose-6-phosphate, a key metabolite connecting pentose metabolism to the EMP pathway [14].
  • In the PTS- glucose+ host background, overexpression of tktA caused a further 3.7-fold increase in carbon flow, while inactivation of pykA and pykF caused a 5.8-fold increase [15].

Regulatory relationships of pykF

  • It was found that flux through phosphoenol pyruvate carboxylase and malic enzyme were up-regulated in the pykF- mutant as compared with the wild type, and acetate formation was significantly reduced in the mutant [13].

Other interactions of pykF


Analytical, diagnostic and therapeutic context of pykF


  1. Cloning of the two pyruvate kinase isoenzyme structural genes from Escherichia coli: the relative roles of these enzymes in pyruvate biosynthesis. Ponce, E., Flores, N., Martinez, A., Valle, F., Bolívar, F. J. Bacteriol. (1995) [Pubmed]
  2. The allosteric regulation of pyruvate kinase. Valentini, G., Chiarelli, L., Fortin, R., Speranza, M.L., Galizzi, A., Mattevi, A. J. Biol. Chem. (2000) [Pubmed]
  3. Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon. Sakai, H., Ohta, T. Eur. J. Biochem. (1993) [Pubmed]
  4. cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. Kanno, H., Fujii, H., Hirono, A., Miwa, S. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  5. Characterization of growth and acid formation in a Bacillus subtilis pyruvate kinase mutant. Fry, B., Zhu, T., Domach, M.M., Koepsel, R.R., Phalakornkule, C., Ataai, M.M. Appl. Environ. Microbiol. (2000) [Pubmed]
  6. Participation of the Entner-Doudoroff pathway in Escherichia coli strains with an inactive phosphotransferase system (PTS- Glc+) in gluconate and glucose batch cultures. Ponce, E., García, M., Muñoz, M.E. Can. J. Microbiol. (2005) [Pubmed]
  7. Effect of desdanine on nucleoside diphosphate kinase and pyruvate kinase of Escherichia coli. Saeki, T., Hori, M., Umezawa, H. J. Antibiot. (1975) [Pubmed]
  8. Primary structure of three peptides at the catalytic and allosteric sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli. Speranza, M.L., Valentini, G., Iadarola, P., Stoppini, M., Malcovati, M., Ferri, G. Biol. Chem. Hoppe-Seyler (1989) [Pubmed]
  9. Effect of a pyruvate kinase (pykF-gene) knockout mutation on the control of gene expression and metabolic fluxes in Escherichia coli. Siddiquee, K.A., Arauzo-Bravo, M.J., Shimizu, K. FEMS Microbiol. Lett. (2004) [Pubmed]
  10. Effect of a single-gene knockout on the metabolic regulation in Escherichia coli for D-lactate production under microaerobic condition. Zhu, J., Shimizu, K. Metab. Eng. (2005) [Pubmed]
  11. Characterization of membrane-associated Pseudomonas aeruginosa Ras-like protein Pra, a GTP-binding protein that forms complexes with truncated nucleoside diphosphate kinase and pyruvate kinase to modulate GTP synthesis. Chopade, B.A., Shankar, S., Sundin, G.W., Mukhopadhyay, S., Chakrabarty, A.M. J. Bacteriol. (1997) [Pubmed]
  12. Translation and stability of an Escherichia coli beta-galactosidase mRNA expressed under the control of pyruvate kinase sequences in Saccharomyces cerevisiae. Purvis, I.J., Loughlin, L., Bettany, A.J., Brown, A.J. Nucleic Acids Res. (1987) [Pubmed]
  13. Metabolic flux analysis of pykF gene knockout Escherichia coli based on 13C-labeling experiments together with measurements of enzyme activities and intracellular metabolite concentrations. Al Zaid Siddiquee, K., Arauzo-Bravo, M.J., Shimizu, K. Appl. Microbiol. Biotechnol. (2004) [Pubmed]
  14. Global gene expression differences associated with changes in glycolytic flux and growth rate in Escherichia coli during the fermentation of glucose and xylose. Gonzalez, R., Tao, H., Shanmugam, K.T., York, S.W., Ingram, L.O. Biotechnol. Prog. (2002) [Pubmed]
  15. A direct comparison of approaches for increasing carbon flow to aromatic biosynthesis in Escherichia coli. Gosset, G., Yong-Xiao, J., Berry, A. J. Ind. Microbiol. (1996) [Pubmed]
  16. Frur mediates catabolite activation of pyruvate kinase (pykF) gene expression in Escherichia coli. Bledig, S.A., Ramseier, T.M., Saier, M.H. J. Bacteriol. (1996) [Pubmed]
  17. 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]
  18. Serial 13C-based flux analysis of an L-phenylalanine-producing E. coli strain using the sensor reactor. Wahl, A., El Massaoudi, M., Schipper, D., Wiechert, W., Takors, R. Biotechnol. Prog. (2004) [Pubmed]
  19. Direct genomic sequencing of bacterial DNA: the pyruvate kinase I gene of Escherichia coli. Ohara, O., Dorit, R.L., Gilbert, W. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  20. Affinity labelling of the catalytic and allosteric ATP binding sites on pyruvate kinase type I from Escherichia coli. Valentini, G., Iadarola, P., Ferri, G., Speranza, M.L. Biol. Chem. Hoppe-Seyler (1995) [Pubmed]
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