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A. The inhibitor constants for three inhibitors of por- cine citrate synthase are summarized in the table on the right. The compounds were all determined to bind in the active site as competitive inhibitors of acetyl-CoA. Because they bind as competitive inhibitors, all three inhibitors must exhibit structural similarity to some part of acetyl-CoA. Look up in the textbook the structural formu- las for Coenzyme A, ATP, and NADH. What is the largest structural fragment of each inhibitor that is responsible for competitive inhibition? Draw the molecular fragment common to each inhibitor that competes with the binding of acetyl-CoA in the active site of citrate synthase. Bromoacetyl-CoA ATP NADH K₁ (µm) 25.7 6800 8300 B While the inhibitor constants listed in part (b) above were determined in vitro for purified citrate synthase, does their inhibitory action have any relevance to the flux of metabolites through the TCA cycle in vivo? If so, explain.

A. The inhibitor constants for three inhibitors of por- cine citrate synthase are summarized in the table on the right. The compounds were all determined to bind in the active site as competitive inhibitors of acetyl-CoA. Because they bind as competitive inhibitors, all three inhibitors must exhibit structural similarity to some part of acetyl-CoA. Look up in the textbook the structural formu- las for Coenzyme A, ATP, and NADH. What is the largest structural fragment of each inhibitor that is responsible for competitive inhibition? Draw the molecular fragment common to each inhibitor that competes with the binding of acetyl-CoA in the active site of citrate synthase. Bromoacetyl-CoA ATP NADH K₁ (µm) 25.7 6800 8300 B While the inhibitor constants listed in part (b) above were determined in vitro for purified citrate synthase, does their inhibitory action have any relevance to the flux of metabolites through the TCA cycle in vivo? If so, explain.

Biochemistry
Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter25: Nitrogen Acquisition And Amino Acid Metabolism
Section: Chapter Questions
Problem 17P
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A. The inhibitor constants for three inhibitors of por- cine citrate synthase are summarized in the table on the right. The compounds were all determined to bind in the active site as competitive inhibitors of acetyl-CoA. Because they bind as competitive inhibitors, all three inhibitors must exhibit structural similarity to some part of acetyl-CoA. Look up in the textbook the structural formu- las for Coenzyme A, ATP, and NADH. What is the largest structural fragment of each inhibitor that is responsible for competitive inhibition? Draw the molecular fragment common to each inhibitor that competes with the binding of acetyl-CoA in the active site of citrate synthase. Bromoacetyl-CoA ATP NADH K₁ (μM) 25.7 6800 8300 B While the inhibitor constants listed in part (b) above were determined in vitro for purified citrate synthase, does their inhibitory action have any relevance to the flux of metabolites through the TCA cycle in vivo? If so, explain.
Transcribed Image Text:A. The inhibitor constants for three inhibitors of por- cine citrate synthase are summarized in the table on the right. The compounds were all determined to bind in the active site as competitive inhibitors of acetyl-CoA. Because they bind as competitive inhibitors, all three inhibitors must exhibit structural similarity to some part of acetyl-CoA. Look up in the textbook the structural formu- las for Coenzyme A, ATP, and NADH. What is the largest structural fragment of each inhibitor that is responsible for competitive inhibition? Draw the molecular fragment common to each inhibitor that competes with the binding of acetyl-CoA in the active site of citrate synthase. Bromoacetyl-CoA ATP NADH K₁ (μM) 25.7 6800 8300 B While the inhibitor constants listed in part (b) above were determined in vitro for purified citrate synthase, does their inhibitory action have any relevance to the flux of metabolites through the TCA cycle in vivo? If so, explain.
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