Product, Substrate, and Alternative Substrate Inhibition
The study of initial rate kinetics in the presence of product has proven to be a boon to the field of enzyme kinetics. Quite probably, no other single experimental protocol has received greater attention since its inception than product inhibition kinetics. Unfortunately, certain complicating factors, such as abortive ternary complex formation and substrate inhibition, have tended to limit the usefulness of this technique. Nevertheless, kinetic investigations in the presence of product remain a formidable tool available to the kineticist interested in making a choice of mechanism from among the usual possibilities. Furthermore, a good deal of insight may be obtained from such experiments regarding the binding of substrates and products at the active site and, in certain cases, at allosteric sites.
KeywordsHexa Pyruvate Oxal NADH Dition
Unable to display preview. Download preview PDF.
- 5.FROMM, H.J., NELSON, D.R.: Federation Proc. 20, abs. 229 (1961).Google Scholar
- 12.SCHWERT, G.W.: Federation Proc. 13, abs. 971 (1954).Google Scholar
- 14.CLELAND, W.W., WRATTEN, C.C.: The Mechanism of Action of Dehydrogenases, p. 103. Lexington: The University Press of Kentucky 1969.Google Scholar
- 19.FROMM, H.J., ZEWE, V.: J. Biolo Chem. 237, 3027 (1962).Google Scholar
- 22.HALDANE, J.B.S.: Enzymes, London: Longmans 1930.Google Scholar
- 24.DIXON, M., WEBB, E.C.: Enzymes. New York: Academic Press 1964.Google Scholar