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1. The change in enzyme shape from the binding of a noncompetitive inhibitor is an example of allostery. Allosteric regulation occurs when a non-substrate molecule binds or modifies an allosteric site, which is a site other than the active site of an enzyme, inducing the enzyme to change its shape. When the inhibitor releases, the enzyme returns to its original conformation, allowing the substrate to bind to the active site and convert into products. 2. Allosteric regulators can be inhibitors or
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Regulation of PFK-1 The effect of ATP on the allosteric enzyme PFK-1 is shown below. For a given concentration of fructose 6 -phosphate, the PFK- 1 activity increases with increasing concentrations of ATP, but a point is reached beyond which increasing the concentration of ATP inhibits the enzyme. (FIGURE CAN'T COPY) (a) Explain how ATP can be both a substrate and an inhibitor of PFK-1. How is the enzyme regulated by ATP? (b) In what ways is glycolysis regulated by ATP levels? (c) The inhibition
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