Review Note

Last Update: 11/14/2024 10:52 PM

Current Deck: URMOM SUGMA DECK+::Biochemistry

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The steady state approximation of the Michaelis Menten Equation supposes that concentration of the {{c1::enzyme-substrate complex [ES]}} remains constant throughout the experiment.
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The [ES] level is kept steady because any ES consumed by the catalytic step (ie, by conversion of ES to E + P) is quickly regenerated by Step 1. In other words, the rate of ES destruction by catalysis is matched by the rate of ES production from binding.

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c5.1-The-Michaelis-Menten-Equation

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