Biochemistry
Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Figure 22.3 6 shows the response of acetyl CoA carboxylase to varying amounts of citrate. Explain this effect in light of the allosteric effects that citrate has on the enzyme. Predict the effects of increasing concentrations of palmitoyl CoA.

(A)
Citrate
Partly
active
carboxylase
Inactive
carboxylase
Citrate
(B)
Dephosphorylated
Highly phosphorylated
5
10
Citrate (mM)
FIGURE 22.36 Dependence of the
catalytic activity of acetyl CoA
carboxylase on the concentration of
citrate. (A) Citrate can partly activate the
phosphorylated carboxylase. (B) The
dephosphorylated form of the carboxylase
is highly active even when citrate is absent.
Citrate partly overcomes the inhibition
produced by phosphorylation. [Information
from G. M. Mabrouk, I. M. Helmy,
K. G. Thampy, and S. J. Wakil. J. Biol.
Chem. 265:6330-6338, 1990.]
Acetyl CoA carboxylase activity
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Transcribed Image Text:(A) Citrate Partly active carboxylase Inactive carboxylase Citrate (B) Dephosphorylated Highly phosphorylated 5 10 Citrate (mM) FIGURE 22.36 Dependence of the catalytic activity of acetyl CoA carboxylase on the concentration of citrate. (A) Citrate can partly activate the phosphorylated carboxylase. (B) The dephosphorylated form of the carboxylase is highly active even when citrate is absent. Citrate partly overcomes the inhibition produced by phosphorylation. [Information from G. M. Mabrouk, I. M. Helmy, K. G. Thampy, and S. J. Wakil. J. Biol. Chem. 265:6330-6338, 1990.] Acetyl CoA carboxylase activity
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