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TAMU BICH 410 - 10_-_Enzyme_kinetics-2

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1234 Enzyme kinetics provides an avenue to explore how enzymes achieve the reduction in activation energy (and other effects) involved in catalysis.56Study carefully how the levels of all the substrates, products and enzyme complexes change with time. In succeeding images we will make simplifying assumptions that allow us to use enzyme kinetics more effectively. 78910The first crucial simplification is to use curve tangent fitting to estimate the “initial” velocity of the reaction. This allows us to ignore changes in substrate and product concentrations as the reaction proceeds. 11In general, the formation of steady state levels of the enzyme-substrate complex (ES) and free enzyme (E) can be assumed to be so rapid as to be effectively instantaneous. Michaelis-Menten kinetics assumes this state (assuming the status diagramed in the assay zone above).


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TAMU BICH 410 - 10_-_Enzyme_kinetics-2

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