Answer to Question #149886 in Biochemistry for nayaa

Question

explain how allosteric regulators may inhibit or stimulate the activity of an enzyme

Answer 1

When an allosteric inhibitor binds to the enzyme, all active sites on the protein sub-units change slightly, so they work less well.

Allosteric activators can also bind to the enzyme at locations other than the active site causing an increase in function.

Cooperativity is an allosteric activator: when a substrate binds to an active site it increases the activity in the other active site.