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How would the activity of a reaction catalyzed by a version of subtilisin with all three residues in the catalytic triad mutated compare to the activity of the uncatalyzed reaction? It would have more activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold faster than the uncatalyzed reaction. It would have more activity, because the reaction catalyzed by the triple mutant is approximately three-fold faster than the uncatalyzed reaction. It would have less activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold slower than the uncatalyzed reaction. ○ It would have the same activity, because the reaction catalyzed by the triple mutant proceeds at the same rate as the uncatalyzed reaction. ○ It would have less activity, because the reaction catalyzed by the triple mutant is approximately three-fold slower than the uncatalyzed reaction.

How would the activity of a reaction catalyzed by a version of subtilisin with all three residues in the catalytic triad mutated compare to the activity of the uncatalyzed reaction? It would have more activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold faster than the uncatalyzed reaction. It would have more activity, because the reaction catalyzed by the triple mutant is approximately three-fold faster than the uncatalyzed reaction. It would have less activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold slower than the uncatalyzed reaction. ○ It would have the same activity, because the reaction catalyzed by the triple mutant proceeds at the same rate as the uncatalyzed reaction. ○ It would have less activity, because the reaction catalyzed by the triple mutant is approximately three-fold slower than the uncatalyzed reaction.

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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The graph illustrates the activities of wild-type and several mutated forms of subtilisin using a logarithmic scale. ### Explanation of Mutations: - **First Letter**: One-letter abbreviation for the amino acid being altered. - **Number**: Indicates the position of the residue in the primary structure. - **Second Letter**: One-letter abbreviation for the amino acid replacing the original one. - **Uncat.**: Represents the estimated rate for the uncatalyzed reaction. ### Graph Description: - **Y-axis**: Logarithmic scale of catalytic activity (log k_cat in s^-1). - **Bars**: - **Wild type**: Highest activity, shown by a green bar. - **S221A, H64A, D32A**: Reduced activity, each shown by red bars with varied heights. - **S221A H64A D32A**: Further reduced activity, shown by a red speckled bar. - **Uncat.**: Represents the uncatalyzed reaction rate, indicated by a gray bar showing the lowest activity. ### Question: How would the activity of a reaction catalyzed by a version of subtilisin with all three residues in the catalytic triad mutated compare to the activity of the uncatalyzed reaction? - **Options**: - It would have more activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold faster than the uncatalyzed reaction. - It would have more activity, because the reaction catalyzed by the triple mutant is approximately three-fold faster than the uncatalyzed reaction. - It would have less activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold slower than the uncatalyzed reaction.
Transcribed Image Text:The graph illustrates the activities of wild-type and several mutated forms of subtilisin using a logarithmic scale. ### Explanation of Mutations: - **First Letter**: One-letter abbreviation for the amino acid being altered. - **Number**: Indicates the position of the residue in the primary structure. - **Second Letter**: One-letter abbreviation for the amino acid replacing the original one. - **Uncat.**: Represents the estimated rate for the uncatalyzed reaction. ### Graph Description: - **Y-axis**: Logarithmic scale of catalytic activity (log k_cat in s^-1). - **Bars**: - **Wild type**: Highest activity, shown by a green bar. - **S221A, H64A, D32A**: Reduced activity, each shown by red bars with varied heights. - **S221A H64A D32A**: Further reduced activity, shown by a red speckled bar. - **Uncat.**: Represents the uncatalyzed reaction rate, indicated by a gray bar showing the lowest activity. ### Question: How would the activity of a reaction catalyzed by a version of subtilisin with all three residues in the catalytic triad mutated compare to the activity of the uncatalyzed reaction? - **Options**: - It would have more activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold faster than the uncatalyzed reaction. - It would have more activity, because the reaction catalyzed by the triple mutant is approximately three-fold faster than the uncatalyzed reaction. - It would have less activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold slower than the uncatalyzed reaction.
**Question 1:** How would the activity of a reaction catalyzed by a version of subtilisin with all three residues in the catalytic triad mutated compare to the activity of the uncatalyzed reaction? - ○ It would have more activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold faster than the uncatalyzed reaction. - ○ It would have more activity, because the reaction catalyzed by the triple mutant is approximately three-fold faster than the uncatalyzed reaction. - ○ It would have less activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold slower than the uncatalyzed reaction. - ○ It would have the same activity, because the reaction catalyzed by the triple mutant proceeds at the same rate as the uncatalyzed reaction. - ○ It would have less activity, because the reaction catalyzed by the triple mutant is approximately three-fold slower than the uncatalyzed reaction. **Question 2:** What could explain any residual catalytic activity of the triple mutant? - ○ The enzyme could bind the substrate and hold it in a conformation that is susceptible to attack by water. - ○ The enzyme could transfer a proton from a water molecule to a histidine residue, forming a nucleophilic OH⁻ ion. - ○ The enzyme could hold two substrate molecules much closer together than they would be in solution. - ○ The enzyme could attack a peptide bond in the substrate using the active-site serine residue as a nucleophile.
Transcribed Image Text:**Question 1:** How would the activity of a reaction catalyzed by a version of subtilisin with all three residues in the catalytic triad mutated compare to the activity of the uncatalyzed reaction? - ○ It would have more activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold faster than the uncatalyzed reaction. - ○ It would have more activity, because the reaction catalyzed by the triple mutant is approximately three-fold faster than the uncatalyzed reaction. - ○ It would have less activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold slower than the uncatalyzed reaction. - ○ It would have the same activity, because the reaction catalyzed by the triple mutant proceeds at the same rate as the uncatalyzed reaction. - ○ It would have less activity, because the reaction catalyzed by the triple mutant is approximately three-fold slower than the uncatalyzed reaction. **Question 2:** What could explain any residual catalytic activity of the triple mutant? - ○ The enzyme could bind the substrate and hold it in a conformation that is susceptible to attack by water. - ○ The enzyme could transfer a proton from a water molecule to a histidine residue, forming a nucleophilic OH⁻ ion. - ○ The enzyme could hold two substrate molecules much closer together than they would be in solution. - ○ The enzyme could attack a peptide bond in the substrate using the active-site serine residue as a nucleophile.
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