If the dipeptide is an inhibitor then it can be a competitive or noncompetitve inhibitor. Competitive inhibitors act by binding to the active site of an enzyme (where a substrate would bind) and thus "compete" with the substrate molecule for the binding site on the enzyme. If the dipeptide is a noncompetitive inhibitor it would bind to an area on the enzyme that is NOT the active site but another site. This other site is called an allosteric site. When the inhibitor molecule binds to the allosteric site it changes the shape of the active site on the enzyme and prevents substrates from binding. This can be tested by creating an experiment in which the enzyme concentration is constant and the substrate concentration is constant. By slowing adding the inhibitor molecule at gradual rates while measuring rate of product formation one could confirm that the molecule is an inhibitor molecule if product formation rates slow or stop as more inhibitor molecules are added.
Work Step by Step
See answer above.