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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How does ATP regulate the activity of PFK-1?
ATP binds to PFK-1 at the catalytic site as a competitive inhibitor, decreasing PFK-1 activity.
ATP binds to the allosteric site as an inhibitor, decreasing PFK-1 activity.
ATP binds to the catalytic site as a substrate, increasing PFK-1 activity.
ATP binds to the allosteric site as an activator, increasing PFK-1 activity.
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Transcribed Image Text:How does ATP regulate the activity of PFK-1? ATP binds to PFK-1 at the catalytic site as a competitive inhibitor, decreasing PFK-1 activity. ATP binds to the allosteric site as an inhibitor, decreasing PFK-1 activity. ATP binds to the catalytic site as a substrate, increasing PFK-1 activity. ATP binds to the allosteric site as an activator, increasing PFK-1 activity.
The graph shows the effect of ATP on the allosteric enzyme phosphofructokinase-1 (PFK-1).
PFK-1 activity (% of Vmax)
100
80
60
40
20
0
Low
[ADP]
[ATP]
High
[ADP]
For a given concentration of fructose 6-phosphate, the PFK-1 activity increases with increasing concentrations of ATP, but there
is a point beyond which increasing the concentration of ATP inhibits the enzyme.
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Transcribed Image Text:The graph shows the effect of ATP on the allosteric enzyme phosphofructokinase-1 (PFK-1). PFK-1 activity (% of Vmax) 100 80 60 40 20 0 Low [ADP] [ATP] High [ADP] For a given concentration of fructose 6-phosphate, the PFK-1 activity increases with increasing concentrations of ATP, but there is a point beyond which increasing the concentration of ATP inhibits the enzyme.
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