A.
Providing a macroenvironment that neutralizes all charges on the substrate
✓
B.
Using covalent catalysis to form a stable enzyme substrate intermediate
✓
C.
Preferentially binding and stabilizing the transition state of the reaction
✓
D.
Lowering the pH of the bulk solution to non specifically hydrolyze the substrate
✓
A.
Nucleophilic catalyst
✓
C.
General acid catalyst
✓
D.
Allosteric modulator
✓
C.
Coenzyme binding domain
✓
B.
Allosteric regulation
✓
A.
Is permanently complementary to the product
✓
B.
Undergoes conformational change upon substrate binding
✓
D.
Is located on a separate regulatory subunit
✓
A.
High substrate specificity
✓
B.
Dependence of reaction rate on substrate concentration
✓
C.
Ability of the enzyme to stabilize the transition state
✓
D.
Formation of enzyme substrate complex
✓
A.
A flexible active site
✓
B.
A rigid, pre shaped active site complementary to the substrate
✓
C.
Random collision followed by substrate change
✓
D.
Substrate changes enzyme primary structure
✓
A.
Strong, irreversible covalent bonds
✓
B.
Weak, non covalent interactions that allow transient and reversible binding
✓
C.
Permanent dipole moments
✓
D.
Hydrophobic forces excluding all water
✓
A.
Increase the kinetic energy of all molecules in the reaction mixture
✓
B.
Provide a surface with a specific shape and chemical groups for the substrate
✓
C.
Alter the standard free energy change to make the reaction exergonic
✓
D.
Combine permanently with the product to shift the equilibrium forward
✓
