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. 1974 Sep;141(3):789–805. doi: 10.1042/bj1410789

A kinetic analysis of enzyme systems involving four substrates

Keith R F Elliott 1,*, Keith F Tipton 1
PMCID: PMC1168185  PMID: 4463962

Abstract

A treatment of kinetic data for enzyme mechanisms involving four substrates is described. The initial-rate equations and product-inhibition patterns for such mechanisms are presented. The treatment is extended to include analysis of enzyme mechanisms involving three substrates in which two molecules of one substrate are used.

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Selected References

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

  1. 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]
  2. CLELAND W. W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory. Biochim Biophys Acta. 1963 Feb 12;67:173–187. doi: 10.1016/0006-3002(63)91815-8. [DOI] [PubMed] [Google Scholar]
  3. Cha S. A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady state. J Biol Chem. 1968 Feb 25;243(4):820–825. [PubMed] [Google Scholar]
  4. 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]
  5. Elliott K. R., Tipton K. F. Kinetic studies of bovine liver carbamoyl phosphate synthetase. Biochem J. 1974 Sep;141(3):807–816. doi: 10.1042/bj1410807. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Elliott K. R., Tipton K. F. Product inhibition studies on bovine liver carbamoyl phosphate synthetase. Biochem J. 1974 Sep;141(3):817–824. doi: 10.1042/bj1410817. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. FRIEDEN C. Glutamic dehydrogenase. III. The order of substrate addition in the enzymatic reaction. J Biol Chem. 1959 Nov;234:2891–2896. [PubMed] [Google Scholar]
  8. Fromm H. J. The use of competitive inhibitors in studying the mechanism of action of some enzyme systems utilizing three substrates. Biochim Biophys Acta. 1967 Jul 11;139(2):221–230. doi: 10.1016/0005-2744(67)90026-5. [DOI] [PubMed] [Google Scholar]
  9. KNAPPE J., RINGELMANN E., LYNEN F. [On beta-hydroxy-beta-methylglutaryl reductase of yeast. On the biosynthesis of terpene. IX]. Biochem Z. 1959;332:195–213. [PubMed] [Google Scholar]
  10. LAGERKVIST U. Biosynthesis of guanosine 5'-phosphate. II. Amination of xanthosine 5'-phosphate by purified enzyme from pigeon liver. J Biol Chem. 1958 Jul;233(1):143–149. [PubMed] [Google Scholar]
  11. LAZZARINI R. A., ATKINSON D. E. A triphosphopyridine nucleotide-specific nitrite reductase from Escherichia coli. J Biol Chem. 1961 Dec;236:3330–3335. [PubMed] [Google Scholar]
  12. METZENBERG R. L., HALL L. M., MARSHALL M., COHEN P. P. Studies on the biosynthesis of carbamyl phosphate. J Biol Chem. 1957 Dec;229(2):1019–1025. [PubMed] [Google Scholar]
  13. Morrison J. F., Ebner K. E. Studies on galactosyltransferase. Kinetic investigations with N-acetylglucosamine as the galactosyl group acceptor. J Biol Chem. 1971 Jun 25;246(12):3977–3984. [PubMed] [Google Scholar]
  14. PREISS J., HANDLER P. Biosynthesis of diphosphopyridine nucleotide. II. Enzymatic aspects. J Biol Chem. 1958 Aug;233(2):493–500. [PubMed] [Google Scholar]
  15. Palmer J. M., Wedding R. T. Purification and properties of succinyl-CoA synthetase from Jerusalem artichoke mitochondria. Biochim Biophys Acta. 1966 Jan 11;113(1):167–174. doi: 10.1016/s0926-6593(66)80131-5. [DOI] [PubMed] [Google Scholar]
  16. Pettersson G. Dalziel rate behaviour in ternary-complex mechanisms for enzyme reactions involving two substrates. Biochim Biophys Acta. 1972 Jul 13;276(1):1–11. doi: 10.1016/0005-2744(72)90002-2. [DOI] [PubMed] [Google Scholar]
  17. Plapp B. V. On calculation of rate and dissociation constants from kinetic constants for the Ordered Bi Bi mechanism of liver alcohol dehydrogenase. Arch Biochem Biophys. 1973 May;156(1):112–114. doi: 10.1016/0003-9861(73)90347-0. [DOI] [PubMed] [Google Scholar]
  18. Rudolph F. B., Fromm H. J. Kinetics of three substrate enzyme systems. Treatment of partially random mechanisms using equilibrium assumptions. J Theor Biol. 1973 May;39(2):363–371. doi: 10.1016/0022-5193(73)90105-7. [DOI] [PubMed] [Google Scholar]
  19. UTTER M. F., KEECH D. B. Formation of oxaloacetate from pyruvate and carbon dioxide. J Biol Chem. 1960 May;235:PC17–PC18. [PubMed] [Google Scholar]
  20. WONG J. T., HANES C. S. Kinetic formulations for enzymic reactions involving two substrates. Can J Biochem Physiol. 1962 Jun;40:763–804. [PubMed] [Google Scholar]
  21. Warren G. B., Tipton K. F. Pig liver pyruvate carboxylase. The reaction pathway for the carboxylation of pyruvate. Biochem J. 1974 May;139(2):311–320. doi: 10.1042/bj1390311. [DOI] [PMC free article] [PubMed] [Google Scholar]

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