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
Human Heredity: Principles and Issues (MindTap Course List)
11th Edition
ISBN:9781305251052
Author:Michael Cummings
Publisher:Michael Cummings
Chapter10: From Proteins To Phenotypes
Section: Chapter Questions
Problem 9QP: a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein...
Related questions
Question
82.17.2
Expert Solution
This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
Step by step
Solved in 3 steps
Recommended textbooks for you
Human Heredity: Principles and Issues (MindTap Co…
Biology
ISBN:
9781305251052
Author:
Michael Cummings
Publisher:
Cengage Learning
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning
Human Heredity: Principles and Issues (MindTap Co…
Biology
ISBN:
9781305251052
Author:
Michael Cummings
Publisher:
Cengage Learning
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning