Abstract

Publisher Summary The progress curves of enzyme-catalyzed reactions are a rich source of kinetic information. Provided suitable methods are used to analyze the data, relatively few such curves can allow a full quantitative description of the dependence of activity on the concentrations of substrates and products. Although difficulties in data analysis have impeded the development of this technique, there is now little reason that it could not be applied to a wide variety of enzyme kinetic studies. Problems of enzyme instability that distort the progress curves from the shape dictated purely from the effects of substrate depletion and inhibitory product accumulation can now be overcome, by including enzyme decay in the kinetic scheme. Straightforward methods are available for analyzing all the unbranched reaction mechanisms, with two or fewer substrates and products, and there is no reason to suppose that more complex situations, such as random mechanisms, will not become amenable to progress curve analysis in the near future.

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