Binding Models 2 Modes of E-S Complex Formation

• Two models have been developed to describe

formation of the enzyme-substrate complex

• Lock-and-key model: substrate binds to that portion

of the enzyme with a complementary shape

• Induced fit model: binding of the substrate induces a

change in the conformation of the enzyme that results
in a complementary fit

Formation of Product An Example of Enzyme Catalysis

• Chymotrypsin catalyzes
• The selective hydrolysis of peptide bonds where the
carboxyl is contributed by Phe and Tyr

• It also catalyzes hydrolysis of the ester bonds

3
An Example of Enzyme Catalysis (Cont’d) Non-Allosteric Enzyme Behavior
• Point at which the rate of
reaction does not change,
enzyme is saturated,
maximum rate of reaction
is reached

ATCase: An Example of Allosteric Behavior Michaelis-Menten Kinetics

• Sigmoidal shape- characteristic of allosterism • Initial rate of an enzyme-catalyzed reaction versus
substrate concentration
• Again Max. velocity reached, but different mechanism