ATP bind phosphofructokinase

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poprock

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when there is High conc of ATP--> phosphofructokinase binds ATP--> allosteriction change in shape --> inhibition of phosphofructokinase--> stops that step in glycolysis

This is negative inhibition step. My question is that even when its low in ATP, phosphofructosekinase still need to bind to ATP to do work right? So whats the diffrence in the binding mechnism?
 
when there is High conc of ATP--> phosphofructokinase binds ATP--> allosteriction change in shape --> inhibition of phosphofructokinase--> stops that step in glycolysis

This is negative inhibition step. My question is that even when its low in ATP, phosphofructosekinase still need to bind to ATP to do work right? So whats the diffrence in the binding mechnism?

this is wayyyy beyond the scope of the DAT..but...here ya go...

"in addition to its role as a substrate, ATP is also an allosteric inhibitor of this enzyme. Thus, PFK has two distict binding sites for ATP; a high-affinity substrate site and a low affinity regulatory site. In the presence of high ATP [], PFK behaves cooperatively, plots of enzyme activity versus F6P are sigmoid, and the Km for F6P is increased"
-Garrett/Grisham - Biochem - 3rd edition
 
this is wayyyy beyond the scope of the DAT..but...here ya go...

"in addition to its role as a substrate, ATP is also an allosteric inhibitor of this enzyme. Thus, PFK has two distict binding sites for ATP; a high-affinity substrate site and a low affinity regulatory site. In the presence of high ATP [], PFK behaves cooperatively, plots of enzyme activity versus F6P are sigmoid, and the Km for F6P is increased"
-Garrett/Grisham - Biochem - 3rd edition

thank you
I thought it was too much too but it was in Schuam's bio review.
 
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