Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1974 Jun;139(3):499–508. doi: 10.1042/bj1390499

A kinetic study of pig liver pyruvate kinase activated by fructose diphosphate

Neil Macfarlane 1, Stanley Ainsworth 1
PMCID: PMC1166314  PMID: 4850216

Abstract

The paper reports a study of the reaction between phosphoenolpyruvate, ADP and Mg2+ catalysed by pig liver pyruvate kinase when activated by fructose diphosphate and K+. The experimental results are consistent with two non-sequential mechanisms in which the substrates and products of the reaction are phosphoenolpyruvate, ADP, Mg2+, pyruvate and MgATP. Pyruvate release occurs before ADP binding. Two Mg2+ ions are involved, though the two Mg2+-binding sites cannot be occupied simultaneously. An isomerized enzyme complex forms before release of MgATP. Values were determined for the Michaelis constants of the reaction. Apparent MgATP inhibition constants are also given.

Full text

PDF
501

Selected References

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

  1. 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]
  2. Balinsky D., Cayanis E., Bersohn I. Comparative kinetic study of human pyruvate kinases isolated from adult and fetal livers and from hepatoma. Biochemistry. 1973 Feb 27;12(5):863–870. doi: 10.1021/bi00729a013. [DOI] [PubMed] [Google Scholar]
  3. CLELAND W. W. Computer programmes for processing enzyme kinetic data. Nature. 1963 May 4;198:463–465. doi: 10.1038/198463a0. [DOI] [PubMed] [Google Scholar]
  4. CLELAND W. W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochim Biophys Acta. 1963 Jan 8;67:104–137. doi: 10.1016/0006-3002(63)91800-6. [DOI] [PubMed] [Google Scholar]
  5. Dalziel K. The interpretation of kinetic data for enzyme-catalysed reactions involving three substrates. Biochem J. 1969 Sep;114(3):547–556. doi: 10.1042/bj1140547. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hess B., Kutzbach C. Identification of two types of liver pyruvate kinase. Hoppe Seylers Z Physiol Chem. 1971 Mar;352(3):453–458. doi: 10.1515/bchm2.1971.352.1.453. [DOI] [PubMed] [Google Scholar]
  7. Hunsley J. R., Suelter C. H. Yeast pyruvate kinase. I. Purification and some chemical properties. J Biol Chem. 1969 Sep 25;244(18):4815–4818. [PubMed] [Google Scholar]
  8. 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]
  9. Koster J. F., Slee R. G., Staal G. E., van Berkel T. J. The influence of glucose I,6-diphosphate on the enzymatic activity of pyruvate kinase. Biochim Biophys Acta. 1972 Mar 8;258(3):763–768. doi: 10.1016/0005-2744(72)90177-5. [DOI] [PubMed] [Google Scholar]
  10. MONOD J., CHANGEUX J. P., JACOB F. Allosteric proteins and cellular control systems. J Mol Biol. 1963 Apr;6:306–329. doi: 10.1016/s0022-2836(63)80091-1. [DOI] [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. Mildvan A. S., Cohn M. Kinetic and magnetic resonance studies of the pyruvate kinase reaction. II. Complexes of enzyme, metal, and substrates. J Biol Chem. 1966 Mar 10;241(5):1178–1193. [PubMed] [Google Scholar]
  13. Ozaki H., Shiio I. Regulation of the TCA and glyoxylate cycles in Brevibacterium flavum. II. Regulation of phosphoenolpyruvate carboxylase and pyruvate kinase. J Biochem. 1969 Sep;66(3):297–311. doi: 10.1093/oxfordjournals.jbchem.a129148. [DOI] [PubMed] [Google Scholar]
  14. Tanaka T., Harano Y., Sue F., Morimura H. Crystallization, characterization and metabolic regulation of two types of pyruvate kinase isolated from rat tissues. J Biochem. 1967 Jul;62(1):71–91. doi: 10.1093/oxfordjournals.jbchem.a128639. [DOI] [PubMed] [Google Scholar]
  15. WILKINSON G. N. Statistical estimations in enzyme kinetics. Biochem J. 1961 Aug;80:324–332. doi: 10.1042/bj0800324. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES