Practice Questions

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
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