Phosphofructokinase 1 (PFK1) activity is regulated by the concentration of ATP through allostery. Increasing the cellular concentration of ATP decreases the affinity of the enzyme for the substrate fructose-6-phosphate. Given that ATP is also one of the substrates for PFK1, how does this regulation mechanism work so effectively? a) ATP can bind to two places on PFK, when ATP is bound in the other site,  PFK changes conformation leading to lower affinity for fructose-6-phosphate b) At high concentrations, ATP binds and reverses the PFK reaction c) ATP decreases the activity of aldolase, leading to product inhibition of PFK d) ATP at high concentration binds in place of fructose-6-phosphate

Biochemistry
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Chapter1: Biochemistry: An Evolving Science
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Phosphofructokinase 1 (PFK1) activity is regulated by the concentration of ATP through allostery. Increasing the cellular concentration of ATP decreases the affinity of the enzyme for the substrate fructose-6-phosphate. Given that ATP is also one of the substrates for PFK1, how does this regulation mechanism work so effectively?


a) ATP can bind to two places on PFK, when ATP is bound in the other site,  PFK changes conformation leading to lower affinity for fructose-6-phosphate
b) At high concentrations, ATP binds and reverses the PFK reaction
c) ATP decreases the activity of aldolase, leading to product inhibition of PFK
d) ATP at high concentration binds in place of fructose-6-phosphate
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