MCQs

10982 questions found

Practice Questions

In lysozyme, Glu35 remains protonated because its microenvironment is

A. Highly hydrophilic
B. Hydrophobic and non polar
C. Rich in lysine residues
D. Completely neutral
nmdcat.online BIO NMDCAT
Jul 11, 2026

The x intercept of a Lineweaver Burk plot equals

A. -1/Vmax
B. -1/Km
C. Vmax/Km
D. Km/Vmax
nmdcat.online BIO NMDCAT
Jul 11, 2026

A conjugated protein enzyme differs from a simple protein enzyme because it requires

A. Four identical subunits
B. A non protein chemical component
C. A macromolecular substrate
D. An allosteric inhibitor
nmdcat.online BIO NMDCAT
Jul 11, 2026

Replacing a catalytic lysine with arginine has no effect on Kcat. This suggests lysine primarily functioned in

A. Covalent catalysis
B. Electrostatic stabilization
C. Nucleophilic attack
D. General acid catalysis
nmdcat.online BIO NMDCAT
Jul 11, 2026

Ribonuclease A provides a classic example of general acid base catalysis using

A. Two aspartates
B. Two tyrosines
C. Two histidines
D. Two cysteines
nmdcat.online BIO NMDCAT
Jul 11, 2026

A perfect enzyme operating at the diffusion controlled limit means the rate limiting step is

A. Product formation
B. Product release
C. Bimolecular encounter of enzyme and substrate
D. Conformational change
nmdcat.online BIO NMDCAT
Jul 11, 2026

The catalytic mechanism of an oxidoreductase most likely involves a coenzyme capable of

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
nmdcat.online BIO NMDCAT
Jul 11, 2026

In the catalytic triad of chymotrypsin, the aspartate residue functions to

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
nmdcat.online BIO NMDCAT
Jul 11, 2026

Covalent catalysis typically requires a powerful nucleophile. A classic example is the

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
nmdcat.online BIO NMDCAT
Jul 11, 2026

Pyridoxal phosphate (PLP) functions in aminotransferases by

A. Accepting a proton to increase pH
B. Forming a Schiff base and acting as an electron sink
C. Hydrolyzing ATP
D. Binding to the allosteric site
nmdcat.online BIO NMDCAT
Jul 11, 2026

A mutation changes glutamate to glutamine in the active site. Km remains unchanged, but Kcat decreases 100 fold. The glutamate most likely participated in

A. Substrate binding
B. Acid base catalysis
C. Covalent catalysis
D. Hydrophobic interaction
nmdcat.online BIO NMDCAT
Jul 11, 2026

Restriction endonucleases primarily rely on which catalytic mechanism?

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
nmdcat.online BIO NMDCAT
Jul 11, 2026

A particular enzyme mechanism involves a histidine residue that first donates a proton and later accepts a proton. This histidine acts as a

A. Nucleophilic catalyst
B. General acid base catalyst
C. Metal ion coordinator
D. Hydrophobic anchor
nmdcat.online BIO NMDCAT
Jul 11, 2026

In the context of enzyme mechanism, the term “ground state destabilization” refers to the concept that the enzyme

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
nmdcat.online BIO NMDCAT
Jul 11, 2026

In the induced fit model, substrate binding triggers a conformational change that

A. Activates proofreading ability
B. Seals the active site and positions catalytic residues correctly
C. Causes cofactor release
D. Permanently denatures other enzyme molecules
nmdcat.online BIO NMDCAT
Jul 11, 2026

The involvement of an enzyme in a reaction means the reaction pathway will have

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
nmdcat.online BIO NMDCAT
Jul 11, 2026

An enzyme fully saturated with substrate is operating at Vmax. At this stage, the rate limiting step is most likely

A. Initial substrate binding
B. Diffusion of enzyme and substrate
C. Chemical conversion of substrate into product
D. Product release
nmdcat.online BIO NMDCAT
Jul 11, 2026

The concept of electrostatic catalysis involves active site residues

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
nmdcat.online BIO NMDCAT
Jul 11, 2026

The proximity effect in enzyme catalysis refers to the enzyme’s ability to

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
nmdcat.online BIO NMDCAT
Jul 11, 2026
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