pH modulation of transient state kinetics of enzymes. I. Simple theoretical models |
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Authors: | J Ricard M Crasnier |
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Affiliation: | Centre de Biochimie et de Biologie Moléculaire du CNRS, BP 71, 13402 Marseille Cedex 9, France |
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Abstract: | The effect of proton concentration on pre-steady-state kinetics has been investigated theoretically for enzyme reactions involving the breaking of one substrate into two products. Even for the simple double-intermediate mechanism the approach to the steady state may exhibit a rather complex kinetics, which is pH-dependent. This process may even exhibit damped oscillations. A change of pH may completely change this transient kinetics and even suppresses the oscillatory regime. A simple method is presented which allows estimation of the values of the rate and ionization constants. This procedure allows one to distinguish the simple double-intermediate mechanism from a more complex process where the 'fast' binding of the substrate induces a 'slow' conformation change of the enzyme. |
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Keywords: | pH modulation Transient state kinetics Double-intermediate mechanism Enzyme kinetics |
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