Enzyme kinetic studies from progress curves

Analysis of progress curves in enzyme kinetics.

Since Michaelis & Menten (1913) demonstrated that many of the problems encountered by earlier workers in enzyme kinetics could be avoided by measuring initial rates and using kinetic equations in their differential forms, most biochemists have been reluctant to use integrated rate equations. However, confining analysis to the initial linear part of a progress curve wastes much of the available ...

A ‘hit-and-run’ kinetic mechanism for the analysis enzyme progress curves under low substrate concentrations

For enzymatic progress curves conforming to the Michaelis–Menten mechanism (E + S ES → E + P) under the experimental conditions where the substrate concentration is at least several times smaller than the Michaelis constant, the minimal fitting model cast as a system of numerically integrated differential equations is the simple ‘hit-and-run’ mechanism, E + S → E + P. The best-fit value of sing...

Kinetic studies of the polygalacturonase enzyme from Colletotrichum lindemuthianum.

The intrinsic protein fluorescence of the polygalacturonase from Colletotrichium lindemuthianum was exploited in stopped-flow experiments aimed at elucidating the kinetic mechanism for this enzyme. Binding of the polymeric substrate polygalacturonic acid (PGA) essentially produced a triphasic fluorescence profile. There was an initial rapid quench in fluorescence, consistent with the rapid form...

Sensitivity, Noise and Detection of Enzyme Inhibition in Progress Curves

Design and analysis of progress curves in enzyme kinetics.

Lastly, I wish to illustrate and to stress the necessity of assessing goodness of fit by making use of several tests and not relying on only one or two such tests. Referring to Table 1, the xz test and the Runs test indicate that model 3 is a good fit, whereas the curved Rankits plot, the slow convergence, the non-linearity at the minimum sum of squares and the wide range of the coefficients of...