Question $13$ of $15$

How does ATP regulate the activity of PFK$-1?$ATP binds to the allosteric site as an inhibitor, decreasing PFK$-1$ activity.ATP binds to PFK$-1$ at the catalytic site as a competitive 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.

How do ATP levels regulate glycolysis?High levels of ATP enhance glycolysis.High levels of ATP inhibit glycolysis.ATP levels do not affect glycolysis.

The inhibition of PFK$-1$ by ATP diminishes when the ADP concentration is high, as shown in the graph. What explains this observation?The $\backslash ([\backslash$mathrm$\{$ATP$\}]/\backslash )$ ADP$]$ ratio regulates $\backslash (\backslash$mathrm$\{$PFK$\}/1\backslash )$ activity.ADP levels regulate the association of the individual PFK$-1$ monomers.Binding of ADP to the catalytic site increases PFK$-$I activity.ADP outcompetes ATP as a phosphoryl donor for PFK$-1$ at high concentrations.