A.
Nucleophilic catalyst
✓
B.
General acid base catalyst
✓
C.
Metal ion coordinator
✓
A.
Destabilizes the substrate through desolvation, strain, or distortion, raising its energy closer to the transition state
✓
B.
Permanently alters the substrate to make it more reactive
✓
C.
Destabilizes its own structure by removing metal ions
✓
D.
Operates most efficiently only in the cellular ground state
✓
A.
Activates proofreading ability
✓
B.
Seals the active site and positions catalytic residues correctly
✓
C.
Causes cofactor release
✓
D.
Permanently denatures other enzyme molecules
✓
A.
More intermediate steps with lower activation energy barriers
✓
B.
Fewer intermediate steps
✓
C.
A single step without a transition state
✓
D.
Higher activation energy
✓
A.
Initial substrate binding
✓
B.
Diffusion of enzyme and substrate
✓
C.
Chemical conversion of substrate into product
✓
A.
Forming transient covalent bonds
✓
B.
Using charged side chains to stabilize charge in the transition state
✓
C.
Creating a completely non polar environment
✓
D.
Mechanically unfolding the substrate
✓
A.
Attract substrates from distant cells
✓
B.
Bind substrates close together and in the correct orientation
✓
C.
Generate a new substrate molecule
✓
D.
Increase proximity to regulatory molecules
✓
B.
Electrostatic catalysis
✓
B.
Binding site for hydrophobic side chains
✓
C.
General base catalyst
✓
D.
Metal chelating ligand
✓
A.
Providing a microenvironment different from the bulk aqueous solution
✓
B.
Orienting the substrates precisely for a reaction
✓
C.
Increasing the local concentration of substrates
✓
D.
Permanently increasing the average kinetic energy of the substrate population
✓
