Enzyme Mechanisms
Questions
Mechanisms
Binding Energy
Effective Molarity
Induced Fit
Lowering Activation Energy
Weak Binding of Substrate
Transition State Binding
Designing a Transition State Analog
Binding of Transition State Analog
Binding Catalysis and …
…Chemical Catalysis
General Acid-Base Catalysis
Covalent Catalysis
pH affects Enzyme Catalysis
Case Study: Diffusion Controlled Enzymes
Triose Phosphate Isomerase
Mechanism
Superoxide Dismutase: Better than Diffusion!
Answers

Questions
1. Replacement of the amino acid ________ at or near an active site of an enzyme is more likely to change enzyme activity than the replacement of ________ at or near the active site.
A) histidine; leucine
B) leucine; histidine
C) leucine; isoleucine
D) histidine; aspartate

2. The following pH dependence was found for the activity of a certain enzyme-catalyzed reaction. If it is known that the only two ionizable residues in the active site are both glutamates, which conclusion can be drawn?
A) The glutamates have different microenvironments which cause their pKa’s to differ.
B) One of the glutamates must be amidated.
C) Both glutamates have a pKa equal to 5.0.
D) Both glutamates are deprotonated during the reaction.