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When testing the effect of substrate concentration on the reaction rate, there comes a point at which increasing the substrate concentration has no effect on the reaction rate. That is, the reaction rate remains the same and no longer increases. Which of the statements below would explain this? Select one: O A. The enzyme is denatured OB. The substrate is denatured OC. All available enzymes are saturated or full with substrates. O D. The enzyme concentration is too high

When testing the effect of substrate concentration on the reaction rate, there comes a point at which increasing the substrate concentration has no effect on the reaction rate. That is, the reaction rate remains the same and no longer increases. Which of the statements below would explain this? Select one: O A. The enzyme is denatured OB. The substrate is denatured OC. All available enzymes are saturated or full with substrates. O D. The enzyme concentration is too high

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
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### Effects of Substrate Concentration on Reaction Rate **Question:** When testing the effect of substrate concentration on the reaction rate, there comes a point at which increasing the substrate concentration has no effect on the reaction rate. That is, the reaction rate remains the same and no longer increases. Which of the statements below would explain this? **Choices:** - **A.** The enzyme is denatured - **B.** The substrate is denatured - **C.** All available enzymes are saturated or full with substrates - **D.** The enzyme concentration is too high ### Explanation: This question addresses a key concept in enzyme kinetics. Enzymes and substrates interact in biochemical reactions. As the substrate concentration increases, the reaction rate initially increases because more substrate molecules are available to bind with enzyme molecules. However, there is a limit to this increase. - **Option A:** The enzyme is denatured - This would not explain the pattern described, as denatured enzymes lose their activity, leading to a decrease rather than a plateau in the reaction rate. - **Option B:** The substrate is denatured - This would also not lead to a plateau in reaction rate, as a denatured substrate would not participate in the reaction properly. - **Option C:** All available enzymes are saturated or full with substrates - This is the correct answer. It explains that once all the enzyme active sites are occupied by substrate molecules, maximum reaction rate (Vmax) is achieved. Beyond this point, adding more substrate does not increase the reaction rate, resulting in a plateau. - **Option D:** The enzyme concentration is too high - This is not relevant to the plateau effect. A higher enzyme concentration would generally increase the reaction rate, not cause it to remain constant. Given the conditions described in the question, the correct answer is **C. All available enzymes are saturated or full with substrates**. This concept is central to understanding enzyme saturation and Michaelis-Menten kinetics, important topics in biochemistry and molecular biology.
Transcribed Image Text:### Effects of Substrate Concentration on Reaction Rate **Question:** When testing the effect of substrate concentration on the reaction rate, there comes a point at which increasing the substrate concentration has no effect on the reaction rate. That is, the reaction rate remains the same and no longer increases. Which of the statements below would explain this? **Choices:** - **A.** The enzyme is denatured - **B.** The substrate is denatured - **C.** All available enzymes are saturated or full with substrates - **D.** The enzyme concentration is too high ### Explanation: This question addresses a key concept in enzyme kinetics. Enzymes and substrates interact in biochemical reactions. As the substrate concentration increases, the reaction rate initially increases because more substrate molecules are available to bind with enzyme molecules. However, there is a limit to this increase. - **Option A:** The enzyme is denatured - This would not explain the pattern described, as denatured enzymes lose their activity, leading to a decrease rather than a plateau in the reaction rate. - **Option B:** The substrate is denatured - This would also not lead to a plateau in reaction rate, as a denatured substrate would not participate in the reaction properly. - **Option C:** All available enzymes are saturated or full with substrates - This is the correct answer. It explains that once all the enzyme active sites are occupied by substrate molecules, maximum reaction rate (Vmax) is achieved. Beyond this point, adding more substrate does not increase the reaction rate, resulting in a plateau. - **Option D:** The enzyme concentration is too high - This is not relevant to the plateau effect. A higher enzyme concentration would generally increase the reaction rate, not cause it to remain constant. Given the conditions described in the question, the correct answer is **C. All available enzymes are saturated or full with substrates**. This concept is central to understanding enzyme saturation and Michaelis-Menten kinetics, important topics in biochemistry and molecular biology.
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