The graph displays the activities of wild-type and several mutated forms of subtilisin on a logarithmic scale. The mutations are identified as: • The first letter is the one-letter abbreviation for the amino acid being altered. • The number identifies the position of the residue in the primary structure. ⚫ The second letter is the one-letter abbreviation for the amino acid replacing the original one. • Uncat. refers to the estimated rate for the uncatalyzed reaction. Log₁(S-1) Wild type S221A H64A -5 D32A S221A H64A D32A -10 Uncat. 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 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. It would have more activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold faster than the uncatalyzed reaction. What could explain any residual catalytic activity of the triple mutant? The enzyme could hold two substrate molecules much closer together than they would be in solution. The enzyme could transfer a proton from a water molecule to a histidine residue, forming a nucleophilic OH- ion. The enzyme could bind the substrate and hold it in a conformation that is susceptible to attack by water. The enzyme could attack a peptide bond in the substrate using the active-site serine residue as a nucleophile.
The graph displays the activities of wild-type and several mutated forms of subtilisin on a logarithmic scale. The mutations are identified as: • The first letter is the one-letter abbreviation for the amino acid being altered. • The number identifies the position of the residue in the primary structure. ⚫ The second letter is the one-letter abbreviation for the amino acid replacing the original one. • Uncat. refers to the estimated rate for the uncatalyzed reaction. Log₁(S-1) Wild type S221A H64A -5 D32A S221A H64A D32A -10 Uncat. 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 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. It would have more activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold faster than the uncatalyzed reaction. What could explain any residual catalytic activity of the triple mutant? The enzyme could hold two substrate molecules much closer together than they would be in solution. The enzyme could transfer a proton from a water molecule to a histidine residue, forming a nucleophilic OH- ion. The enzyme could bind the substrate and hold it in a conformation that is susceptible to attack by water. The enzyme could attack a peptide bond in the substrate using the active-site serine residue as a nucleophile.
Chapter5: Unit, Percentage, Milliequivalent, Ratio, And Household Measures
Section: Chapter Questions
Problem 16SST
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Transcribed Image Text:The graph displays the activities of wild-type and several mutated forms of subtilisin on a logarithmic scale.
The mutations are identified as:
• The first letter is the one-letter
abbreviation for the amino acid
being altered.
• The number identifies the
position of the residue in the
primary structure.
⚫ The second letter is the
one-letter abbreviation for the
amino acid replacing the
original one.
• Uncat. refers to the estimated
rate for the
uncatalyzed reaction.
Log₁(S-1)
Wild type
S221A
H64A
-5
D32A
S221A
H64A
D32A
-10
Uncat.
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 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.
It would have more activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold faster
than the uncatalyzed reaction.
Transcribed Image Text:What could explain any residual catalytic activity of the triple mutant?
The enzyme could hold two substrate molecules much closer together than they would be in solution.
The enzyme could transfer a proton from a water molecule to a histidine residue, forming a nucleophilic OH- ion.
The enzyme could bind the substrate and hold it in a conformation that is susceptible to attack by water.
The enzyme could attack a peptide bond in the substrate using the active-site serine residue as a nucleophile.
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