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. 1986 Mar 15;234(3):705–715. doi: 10.1042/bj2340705

The regulatory properties of yeast pyruvate kinase. Effects of NH4+ and K+ concentrations.

N Rhodes, C N Morris, S Ainsworth, J Kinderlerer
PMCID: PMC1146629  PMID: 3521597

Abstract

The kinetics of pyruvate kinase from Saccharomyces cerevisiae were studied at 25 degrees C and pH 6.2 as a function of the concentrations of ADP, phosphoenolpyruvate, Mg2+ and either NH4+ or K+. The data were analysed by the exponential model for four substrates, obtained by extension of the model described by Ainsworth, Kinderlerer & Gregory [(1983) Biochem. J. 209, 401-411]. On that basis, it was concluded that NH4+ binding is almost non-interactive but leads to the appearance of positive interaction in the velocity response to increase in its concentration because of positive interactions with phosphoenolpyruvate and Mg2+. The data obtained with K+ lead to the same conclusions and differ only in suggesting that NH4+ is bound more strongly to the enzyme than is K+. Both data sets are used as the basis for a discussion of the substrate interactions of pyruvate kinase and it appears therefrom that the heterotropic interactions accord with what is known of the events that take place at the active site during catalysis. The paper also reports a determination of the dissociation constants for the NH4+ complexes with ADP and phosphoenolpyruvate and an examination of the simultaneous activation of pyruvate kinase by K+ and NH4+ ions.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ainsworth S. A simple model for a regulatory enzyme. J Theor Biol. 1977 Oct 7;68(3):391–413. doi: 10.1016/0022-5193(77)90068-6. [DOI] [PubMed] [Google Scholar]
  2. Ainsworth S., Gregory R. B. The exponential model for a regulatory enzyme: its extension to describe the binding of two ligands. J Theor Biol. 1978 Nov 7;75(1):97–114. doi: 10.1016/0022-5193(78)90204-7. [DOI] [PubMed] [Google Scholar]
  3. Ainsworth S., Kinderlerer J., Gregory R. B. The regulatory properties of rabbit muscle pyruvate kinase. The influence of substrate concentrations. Biochem J. 1983 Feb 1;209(2):401–411. doi: 10.1042/bj2090401. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Ainsworth S., MacFarlane N. A kinetic study of rabbit muscle pyruvate kinase. Biochem J. 1973 Feb;131(2):223–236. doi: 10.1042/bj1310223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. BURTON K. Formation constants for the complexes of adenosine di- or tri-phosphate with magnesium or calcium ions. Biochem J. 1959 Feb;71(2):388–395. doi: 10.1042/bj0710388. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gupta R. K., Mildvan A. S. Structures of enzyme-bound metal-nucleotide complexes in the phosphoryl transfer reaction of muscle pyruvate kinase. 31P NMR studies with magnesium and kinetic studies with chromium nucleotides. J Biol Chem. 1977 Sep 10;252(17):5967–5976. [PubMed] [Google Scholar]
  7. Hunsley J. R., Suelter C. H. Yeast pyruvate kinase. II. Kinetic properties. J Biol Chem. 1969 Sep 25;244(18):4819–4822. [PubMed] [Google Scholar]
  8. KACHMAR J. F., BOYER P. D. Kinetic analysis of enzyme reactions. II. The potassium activation and calcium inhibition of pyruvic phosphoferase. J Biol Chem. 1953 Feb;200(2):669–682. [PubMed] [Google Scholar]
  9. Kayne F. J. Thallium (I) activation of pyruvate kinase. Arch Biochem Biophys. 1971 Mar;143(1):232–239. doi: 10.1016/0003-9861(71)90204-9. [DOI] [PubMed] [Google Scholar]
  10. Kinderlerer J., Ainsworth S., Morris C. N., Rhodes N. The regulatory properties of yeast pyruvate kinase. Effect of pH. Biochem J. 1986 Mar 15;234(3):699–703. doi: 10.1042/bj2340699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Macfarlane N., Ainsworth S. A kinetic study of Baker's-yeast pyruvate kinase activated by fructose 1,6-diphosphate. Biochem J. 1972 Oct;129(5):1035–1047. doi: 10.1042/bj1291035. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Manchester K. L. Determination of magnesium and potassium binding constants to phosphoenolpyruvate, 2- and 3-phosphoglycerate and a number of other anions. Biochim Biophys Acta. 1980 Jun 19;630(2):225–231. doi: 10.1016/0304-4165(80)90425-0. [DOI] [PubMed] [Google Scholar]
  13. Morris C. N., Ainsworth S., Kinderlerer J. The regulatory properties of yeast pyruvate kinase. Effect of fructose 1,6-bisphosphate. Biochem J. 1986 Mar 15;234(3):691–698. doi: 10.1042/bj2340691. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Morris C. N., Ainsworth S., Kinderlerer J. The regulatory properties of yeast pyruvate kinase. Biochem J. 1984 Feb 1;217(3):641–647. doi: 10.1042/bj2170641. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Nowak T., Mildvan A. S. Nuclear magnetic resonance studies of the function of potassium in the mechanism of pyruvate kinase. Biochemistry. 1972 Jul 18;11(15):2819–2828. doi: 10.1021/bi00765a014. [DOI] [PubMed] [Google Scholar]
  16. Nowak T., Suelter C. Pyruvate kinase: activation by and catalytic role of the monovalent and divalent cations. Mol Cell Biochem. 1981 Mar 13;35(2):65–75. doi: 10.1007/BF02354821. [DOI] [PubMed] [Google Scholar]
  17. Phillips R. C., George P., Rutman R. J. Thermodynamic studies of the formation and ionization of the magnesium(II) complexes of ADP and ATP over the pH range 5 to 9. J Am Chem Soc. 1966 Jun 20;88(12):2631–2640. doi: 10.1021/ja00964a002. [DOI] [PubMed] [Google Scholar]
  18. Suelter C. H., Singleton R., Jr, Kayne F. J., Arrington S., Glass J., Mildvan A. S. Stuies on the interaction of substrate and monovalent and divalent cations with pyruvate kinase. Biochemistry. 1966 Jan;5(1):131–139. doi: 10.1021/bi00865a017. [DOI] [PubMed] [Google Scholar]
  19. WOLD F., BALLOU C. E. Studies on the enzyme enolase. I. Equilibrium studies. J Biol Chem. 1957 Jul;227(1):301–312. [PubMed] [Google Scholar]

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