Abstract
All the kinetic mechanisms we have discussed to this point refer to the uni-reactant transformation S → P. However, most enzymes catalyse reactions between two or more substrates yielding two or more products, and the rate equations describing the mechanisms of such reactions are more complex than the ones which we have considered so far. In this treatment we shall restrict the discussion to reactions involving two substrates and two products. A number of excellent treatments of this subject are available (see bibliography) so we shall not attempt to provide an exhaustive summary, but rather aim to show the principles involved in obtaining mechanistic information.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Bisubstrate Kinetics
Anderson, S. R., Florini, J. R. and Vestling, C. S. (1964) Rat liver lactate dehydrogenase. Kinetics and specificity, J. Biol. Chem., 239, 2991–2997.
Cleland, W. W. (1963) The kinetics of enzyme-catalysed reactions with two or more substrates or products, Biochim. Biophys. Acta, 67, 104–137.
Cleland, W. W. (1970) Steady-state kinetics, in The Enzymes, 3rd ed., vol. 2, pp. 1–65, Boyer, P. D. (Ed.), Academic Press, New York.
Dixon, M., Webb, E. C., Thome, C. J. R. and Tipton, K. F. (1979) Enzymes, 3rd ed., Longman, London.
Morrison, J. F. (1965) Kinetic methods for the determination of enzyme reaction mechanisms, Austral. J. Sci., 27, 317–327.
Morrison, J. F. and James, E. (1965) The mechanism of the reaction catalysed by adenosine triphosphate-creatine phospho-transferase, Biochem. J., 97, 37–52.
Segel, I. H. (1975) Enzyme Kinetics, Wiley, New York.
Silverstein, E. and Boyer, P. D. (1964) Equilibrium reaction rates and the mechanisms of bovine heart and rabbit muscle lactate dehydrogenases, J. Biol Chem., 239, 3901–3907.
Tipton, K. F. (1974) Enzyme kinetics, in Companion to Biochemistry, ch. 6, Bull, A. T. et al. (Eds.), Longman, London.
Velick, S. F. and Vavra, J. (1962) A kinetic and equilibrium analysis of the glutamic oxalacetate transaminase mechanism, J. Biol Chem., 237, 2109–2122.
Cooperativity and Allostery
Dalziel, K. (1973) Kinetics of control enzymes, Symp. Soc. Exptl. Biol., 27, 21–48.
Frieden, C. (1979) Slow transitions and hysteretic behaviour in enzymes, Ann. Rev. Biochem., 48, 471–489.
Tipton, K. F. (1979) Kinetic properties of allosteric and cooperative enzymes, in Companion to Biochemistry, vol. 2, ch. 11, Bull, A. T., Lagnado, J. R., Thomas, J. O. and Tipton, K. F. (Eds.), Longmans, London.
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1981 C. W. Wharton and R. Eisenthal
About this chapter
Cite this chapter
Wharton, C.W., Eisenthal, R. (1981). Complex Kinetics and Cooperativity. In: Molecular Enzymology. Tertiary Level Biology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-8532-9_7
Download citation
DOI: https://doi.org/10.1007/978-1-4615-8532-9_7
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4615-8534-3
Online ISBN: 978-1-4615-8532-9
eBook Packages: Springer Book Archive