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BIO NMDCAT

1785 questions found

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Practice Questions

Catalysis by approximation is achieved by

A. Denaturing the substrate
B. Binding two substrates close together to increase their effective concentration
C. Lowering the pH of the solution
D. Using a metal ion to generate hydroxyl radicals
nmdcat.online BIO NMDCAT
Jul 11, 2026

In triose phosphate isomerase, glutamate abstracts a proton from the substrate. It acts as a

A. General acid
B. Lewis acid
C. General base
D. Metal ion cofactor
nmdcat.online BIO NMDCAT
Jul 11, 2026

Activation of the catalytic serine hydroxyl group in serine proteases is achieved by

A. Bulk water
B. Histidine acting as a general base
C. Aspartate donating a proton
D. Formation of a disulfide bond
nmdcat.online BIO NMDCAT
Jul 11, 2026

Binding energy released during enzyme substrate interaction is primarily used to

A. Directly break substrate bonds
B. Increase activation energy
C. Lower activation energy by stabilizing the transition state
D. Dissociate the enzyme cofactor complex
nmdcat.online BIO NMDCAT
Jul 11, 2026

An inhibitor decreases Vmax from 100 ?mol/min to 50 ?mol/min without changing Km. This is characteristic of

A. Competitive inhibition
B. Non competitive inhibition
C. Uncompetitive inhibition
D. Irreversible inhibition
nmdcat.online BIO NMDCAT
Jul 11, 2026

In cysteine proteases, the nucleophile is the

A. Sulfhydryl group in its thiolate (S?) form
B. Hydroxyl group
C. Amide group
D. Imidazole ring
nmdcat.online BIO NMDCAT
Jul 11, 2026

Penicillin inhibits bacterial transpeptidase by

A. Competitive reversible inhibition
B. Non competitive reversible inhibition
C. Irreversible suicide inhibition
D. Allosteric regulation
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

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

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

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

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

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 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

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

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

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

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

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
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