An allosteric site on an enzyme is
- A. a second active site that binds the same substrate
- B. a site away from the active site where a regulatory molecule binds and changes the enzyme's shape
- C. the region that is denatured first by heat
- D. the point where the enzyme attaches to the cell membrane
Explanation
A molecule binding at an allosteric site alters the conformation of the whole enzyme, and therefore the shape of the active site, either activating or inhibiting it. Non competitive inhibition and feedback inhibition both work this way, which is why adding more substrate cannot overcome them. The site is chemically distinct from the active site and binds a different molecule.
Related questions
A competitive inhibitor slows an enzyme catalysed reaction by
Increasing the substrate concentration will NOT relieve the effect of
Malonate inhibits succinate dehydrogenase because it resembles succinate. This is an example of
Heavy metal ions such as mercury and silver inhibit many enzymes irreversibly because they
In feedback inhibition of a metabolic pathway