The inhibition of PFK-1 by ATP diminishes when the ADP concentration is high, as shown in the graph What explains this observation? ADP levels regulate the association of the individual PFK-1 monomers. The [ATP]/[ADP] ratio regulates PFK-1 activity. ADP outcompetes ATP as a phosphoryl donor for PFK-1 at high concentrations. O Binding of ADP to the catalytic site increases PFK-1 activity.
The inhibition of PFK-1 by ATP diminishes when the ADP concentration is high, as shown in the graph What explains this observation? ADP levels regulate the association of the individual PFK-1 monomers. The [ATP]/[ADP] ratio regulates PFK-1 activity. ADP outcompetes ATP as a phosphoryl donor for PFK-1 at high concentrations. O Binding of ADP to the catalytic site increases PFK-1 activity.
Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter18: Glycolysis
Section: Chapter Questions
Problem 21P
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![The inhibition of PFK-1 by ATP diminishes when the ADP concentration is high, as shown in the graph.
What explains this observation?
ADP levels regulate the association of the individual PFK-1 monomers.
The [ATP]/[ADP] ratio regulates PFK-1 activity.
ADP outcompetes ATP as a phosphoryl donor for PFK-1 at high concentrations.
Binding of ADP to the catalytic site increases PFK-1 activity.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Ff153f65b-a5bd-400b-be2c-4cde890c9d0b%2Fffbb17d0-25c0-416e-98f6-d717be1c3380%2F6eu4ye9_processed.jpeg&w=3840&q=75)
Transcribed Image Text:The inhibition of PFK-1 by ATP diminishes when the ADP concentration is high, as shown in the graph.
What explains this observation?
ADP levels regulate the association of the individual PFK-1 monomers.
The [ATP]/[ADP] ratio regulates PFK-1 activity.
ADP outcompetes ATP as a phosphoryl donor for PFK-1 at high concentrations.
Binding of ADP to the catalytic site increases 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.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Ff153f65b-a5bd-400b-be2c-4cde890c9d0b%2Fffbb17d0-25c0-416e-98f6-d717be1c3380%2Fd6vqnd_processed.jpeg&w=3840&q=75)
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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