MCQs
11262 questions found
C.
Bimolecular encounter of enzyme and substrate
✓
D.
Conformational change
✓
A.
Acting as a molecular scaffold
✓
B.
Shuttling protons and electrons such as NAD? or FAD
✓
C.
Forming a thioester bond
✓
D.
Transferring methyl groups
✓
A.
Act as the primary nucleophile
✓
B.
Form a hydrogen bond with histidine and enhance its basicity
✓
C.
Bind the N terminus of the substrate
✓
D.
Donate a proton directly to the leaving group
✓
A.
Amide group of asparagine
✓
B.
Hydroxyl group of serine activated to an alkoxide ion
✓
C.
Methyl group of alanine
✓
D.
Guanidinium group of arginine
✓
A.
Accepting a proton to increase pH
✓
B.
Forming a Schiff base and acting as an electron sink
✓
D.
Binding to the allosteric site
✓
D.
Hydrophobic interaction
✓
A.
Single step induced fit
✓
B.
Activation of a water molecule by a metal bound hydroxide for direct nucleophilic attack
✓
C.
Formation of a covalent phospho enzyme intermediate
✓
D.
Intercalation of hydrophobic amino acids into DNA
✓
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
✓
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
✓
