Simple enzyme kinetic mechanisms that can give all possible velocity profiles with chemically reasonable rate constant values
- 1 October 1983
- journal article
- research article
- Published by Elsevier in Journal of Theoretical Biology
- Vol. 104 (4) , 485-491
- https://doi.org/10.1016/0022-5193(83)90241-2
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- The probability of obtaining complex kinetic curves for enzyme mechanisms with cubic terms in the pseudo-steady state rate equationsJournal of Theoretical Biology, 1982
- The probability that complex enzyme kinetic curves can be caused by activators or inhibitorsBiochemical Journal, 1981
- Deviations from Michaelis–Menten kinetics. Computation of the probabilities of obtaining complex curves from simple kinetic schemesBiochemical Journal, 1980
- Deviations from Michaelis-Menten kinetics. The possibility of complicated curves for simple kinetic schemes and the computer fitting of experimental data for acetylcholinesterase, acid phosphatase, adenosine deaminase, arylsulphatase, benzylamine oxidase, chymotrypsin, fumarase, galactose dehydrogenase, β-galactosidase, lactate dehydrogenase, peroxidase and xanthine oxidaseBiochemical Journal, 1980
- The 3:3 function in enzyme kinetics possible shapes of vS and (1v)(1S) plots for third degree steady-state rate equationsJournal of Theoretical Biology, 1977
- The quantitative analysis of ligand binding and initial-rate data for allosteric and other complex enzyme mechanismsBiochemical Journal, 1976
- Sigmoid curves, non-linear double-reciprocal plots and allosterismBiochemical Journal, 1975
- Statistical Methods for Determination of Empirical Rate Equations for Enzyme Reactions.Acta Chemica Scandinavica, 1970
- A Schematic Method of Deriving the Rate Laws for Enzyme-Catalyzed ReactionsThe Journal of Physical Chemistry, 1956