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At 37°C, the serine protease subtilisin has keat = 50 s¹ and KM = 1.4 x 10-4 M. It is proposed that the N155 side chain contributes a hydrogen bond to the oxyanion hole of subtilisin. J. A. Wells and colleagues reported (1986, Phil. Trans. R. Soc. Lond. A 317:415-423) the following kinetic parameters for the N155T mutant of subtilisin: keat = 0.02 s¹ and KM 2x 10-4 M. ▾ Part C Is the effect of the N155T mutation what you would expect for a residue that makes up part of the oxyanion hole? How do the reported values of keat and KM support your answer? Check all that apply. The oxyanion is formed after S binds. For a mutation of a residue that only interacts with the oxyanion intermediate, one would not expect KM to change significantly. The oxyanion is formed after S goes away. For a mutation of a residue that only interacts with the oxyanion intermediate, one would expect KM to change significantly. Okeat should be reduced due to the gain of enthalpic stabilization of the transition state. Okeat should be reduced due to the loss of enthalpic stabilization of the transition state. Submit Request Answer

At 37°C, the serine protease subtilisin has keat = 50 s¹ and KM = 1.4 x 10-4 M. It is proposed that the N155 side chain contributes a hydrogen bond to the oxyanion hole of subtilisin. J. A. Wells and colleagues reported (1986, Phil. Trans. R. Soc. Lond. A 317:415-423) the following kinetic parameters for the N155T mutant of subtilisin: keat = 0.02 s¹ and KM 2x 10-4 M. ▾ Part C Is the effect of the N155T mutation what you would expect for a residue that makes up part of the oxyanion hole? How do the reported values of keat and KM support your answer? Check all that apply. The oxyanion is formed after S binds. For a mutation of a residue that only interacts with the oxyanion intermediate, one would not expect KM to change significantly. The oxyanion is formed after S goes away. For a mutation of a residue that only interacts with the oxyanion intermediate, one would expect KM to change significantly. Okeat should be reduced due to the gain of enthalpic stabilization of the transition state. Okeat should be reduced due to the loss of enthalpic stabilization of the transition state. Submit Request Answer

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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82.17.2

At 37 °C, the serine protease subtilisin has kcat = 50 s¯¹ and KM = 1.4 × 10-4 M. It is proposed that the N155 side chain contributes a hydrogen bond to the oxyanion hole of subtilisin. J. A. Wells and colleagues reported (1986, Phil. Trans. R. Soc. Lond. A 317:415-423) the following kinetic parameters for the N155T mutant of subtilisin: kcat 0.02 s and KM 2 x 10-4 M. = - Correct Part C Is the effect of the N155T mutation what you would expect for a residue that makes up part of the oxyanion hole? How do the reported values of kcat and KM support your answer? Check all that apply. The oxyanion is formed after S binds. For a mutation of a residue that only interacts with the oxyanion intermediate, one would not expect KM to change significantly. The oxyanion is formed after S goes away. For a mutation of a residue that only interacts with the oxyanion intermediate, one would expect KM to change significantly. kcat should be reduced due to the gain of enthalpic stabilization of the transition state. kcat should be reduced due to the loss of enthalpic stabilization of the transition state. Submit Part D Assuming that the T155 side chain cannot H-bond to the oxyanion intermediate, by how much (in kJ/mol) does N155 appear to stabilize the transition state at 37 °C? Express your answer to two significant figures and include the appropriate units. Request Answer Value Submit μÅ C Units Request Answer ?
Transcribed Image Text:At 37 °C, the serine protease subtilisin has kcat = 50 s¯¹ and KM = 1.4 × 10-4 M. It is proposed that the N155 side chain contributes a hydrogen bond to the oxyanion hole of subtilisin. J. A. Wells and colleagues reported (1986, Phil. Trans. R. Soc. Lond. A 317:415-423) the following kinetic parameters for the N155T mutant of subtilisin: kcat 0.02 s and KM 2 x 10-4 M. = - Correct Part C Is the effect of the N155T mutation what you would expect for a residue that makes up part of the oxyanion hole? How do the reported values of kcat and KM support your answer? Check all that apply. The oxyanion is formed after S binds. For a mutation of a residue that only interacts with the oxyanion intermediate, one would not expect KM to change significantly. The oxyanion is formed after S goes away. For a mutation of a residue that only interacts with the oxyanion intermediate, one would expect KM to change significantly. kcat should be reduced due to the gain of enthalpic stabilization of the transition state. kcat should be reduced due to the loss of enthalpic stabilization of the transition state. Submit Part D Assuming that the T155 side chain cannot H-bond to the oxyanion intermediate, by how much (in kJ/mol) does N155 appear to stabilize the transition state at 37 °C? Express your answer to two significant figures and include the appropriate units. Request Answer Value Submit μÅ C Units Request Answer ?
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