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k₁ ES ES k.₂₁ K₂ K3 K.2 EP→ E+ P

k₁ ES ES k.₂₁ K₂ K3 K.2 EP→ E+ P

Chemistry
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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Find the change in the concentration of ES over time 

The image shows a series of chemical reactions illustrating an enzyme-catalyzed process. **Reaction Steps:** 1. \( E + S \rightleftharpoons ES \) - \( k_1 \) is the rate constant for the formation of the enzyme-substrate complex (ES) from enzyme (E) and substrate (S). - \( k_{-1} \) is the rate constant for the dissociation of the enzyme-substrate complex back into enzyme and substrate. 2. \( ES \rightleftharpoons EP \) - \( k_2 \) is the rate constant for the transformation of the enzyme-substrate complex (ES) to enzyme-product complex (EP). - \( k_{-2} \) is the rate constant for the reverse reaction. 3. \( EP \rightarrow E + P \) - \( k_3 \) is the rate constant for the final step where the enzyme-product complex (EP) dissociates to release the enzyme (E) and product (P). This sequence represents a common model in enzyme kinetics, known as the Michaelis-Menten mechanism, which describes how enzymes interact with substrates to produce products.
Transcribed Image Text:The image shows a series of chemical reactions illustrating an enzyme-catalyzed process. **Reaction Steps:** 1. \( E + S \rightleftharpoons ES \) - \( k_1 \) is the rate constant for the formation of the enzyme-substrate complex (ES) from enzyme (E) and substrate (S). - \( k_{-1} \) is the rate constant for the dissociation of the enzyme-substrate complex back into enzyme and substrate. 2. \( ES \rightleftharpoons EP \) - \( k_2 \) is the rate constant for the transformation of the enzyme-substrate complex (ES) to enzyme-product complex (EP). - \( k_{-2} \) is the rate constant for the reverse reaction. 3. \( EP \rightarrow E + P \) - \( k_3 \) is the rate constant for the final step where the enzyme-product complex (EP) dissociates to release the enzyme (E) and product (P). This sequence represents a common model in enzyme kinetics, known as the Michaelis-Menten mechanism, which describes how enzymes interact with substrates to produce products.
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