You are studying the kinetics of a novel competitive inhibitor of ATP-citrate lyase that can be used to prevent obesity. What is likely true about this inhibitor? (A) This inhibitor lowers the Vmax of ATP-citrate lyase. (B) The inhibitor likely looks structurally similar to acetyl CoA. (C) The inhibitor binds to an allosteric region on ATP-citrate lyase and prevents catalysis. (D) You can distinguish between an uninhibited and inhibited enzyme by comparing the x-intercepts on a Lineweaver-Burk plot. (E) This inhibitor lowers the KM of ATP-citrate lyase

Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter27: Metabolic Integration And Organ Specialization
Section: Chapter Questions
Problem 20P: Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy...
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You are studying the kinetics of a novel competitive inhibitor of ATP-citrate lyase that can be used to prevent obesity. What is likely true about this inhibitor? (A) This inhibitor lowers the Vmax of ATP-citrate lyase. (B) The inhibitor likely looks structurally similar to acetyl CoA. (C) The inhibitor binds to an allosteric region on ATP-citrate lyase and prevents catalysis. (D) You can distinguish between an uninhibited and inhibited enzyme by comparing the x-intercepts on a Lineweaver-Burk plot. (E) This inhibitor lowers the KM of ATP-citrate lyase. Related to this question, you should also be able to: • explain the function of ATP-citrate lyase and why inhibition would prevent obesity • interpret Michaelis-Menten & Lineweaver-Burk plots related to this question • explain the differences between a competitive and non-competitive inhibitor
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