We have three inhibitor and same enzyme were incubated with 5 mM of substrate and 2 mM of inhibitor.I1,competitive inhibitor, I2,uncompetitive inhibitor, I3, non-competitive inhibitor.Assuming that Vmax = 80 mM s-1 , Km = 8 mM, and KI of all three inhibitors was 10 mM, which of the inhibitors was the most efficient on V0? Explain your answer
We have three inhibitor and same enzyme were incubated with 5 mM of substrate and 2 mM of inhibitor.I1,competitive inhibitor, I2,uncompetitive inhibitor, I3, non-competitive inhibitor.Assuming that Vmax = 80 mM s-1 , Km = 8 mM, and KI of all three inhibitors was 10 mM, which of the inhibitors was the most efficient on V0? Explain your answer
Introductory Chemistry: A Foundation
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ISBN:9781337399425
Author:Steven S. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Donald J. DeCoste
Chapter21: Biochemistry
Section: Chapter Questions
Problem 28QAP: . Describe the lock-and-key model for enzymes. Why are the shapes of the enzyme and its substrate...
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We have three inhibitor and same enzyme were incubated with 5 mM of substrate and 2 mM of inhibitor.I1,competitive inhibitor, I2,uncompetitive inhibitor, I3, non-competitive inhibitor.Assuming that Vmax = 80 mM s-1 , Km = 8 mM, and KI of all three inhibitors was 10 mM, which of the inhibitors was the most efficient on V0? Explain your answer
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