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Practice Questions

Stereospecificity in enzyme action means the enzyme can

A. Change its own stereochemistry
B. Produce racemic products
C. Distinguish between optical isomers and act on only one
D. Convert every substrate into its optical isomer
nmdcat.online BIO NMDCAT
Jul 11, 2026

Pepsin has an optimum pH of about 2 because

A. Its coenzyme works only at low pH
B. Catalytic residues require a specific protonation state
C. The substrate is active only at pH 2
D. Product inhibition occurs at higher pH
nmdcat.online BIO NMDCAT
Jul 11, 2026

Stabilization of a negatively charged tetrahedral intermediate is achieved by the

A. Hydrophobic pocket
B. Oxyanion hole
C. Zinc ion
D. Allosteric site
nmdcat.online BIO NMDCAT
Jul 11, 2026

In glyceraldehyde 3 phosphate dehydrogenase, the catalytic cysteine is activated by a neighboring

A. Aspartate
B. Histidine
C. Zinc ion
D. Arginine
nmdcat.online BIO NMDCAT
Jul 11, 2026

In a multistep enzyme mechanism, the overall reaction rate is determined by the step with the

A. Lowest activation energy
B. Highest activation energy
C. Greatest entropy change
D. Largest number of water molecules
nmdcat.online BIO NMDCAT
Jul 11, 2026

An enzyme that catalyzes reactions without any non protein component relies solely on

A. Quaternary structure
B. Amino acid side chains arranged in the active site
C. Alpha helices
D. Signal peptide
nmdcat.online BIO NMDCAT
Jul 11, 2026

A Bi substrate reaction following a Sequential Ordered mechanism is characterized by

A. Random substrate binding
B. Both substrates bind before any product is released, in a compulsory order
C. Product leaves before all substrates bind
D. Reaction rate is independent of the second substrate
nmdcat.online BIO NMDCAT
Jul 11, 2026

The active site of an enzyme is often described as a “microenvironment.” A key characteristic of this microenvironment is

A. A completely uniform charge distribution
B. A significantly lowered dielectric constant that enhances electrostatic interactions
C. A pH always equal to 7.0
D. An unlimited supply of free water molecules
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

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

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

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

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

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

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

The catalytic efficiency of an enzyme is best described by the ratio

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

During the mechanism of chymotrypsin, the “pong” step involves

A. Release of the unaltered second substrate
B. Binding of a water molecule and its nucleophilic attack on the acyl enzyme intermediate
C. Binding of an allosteric inhibitor
D. Auto degradation of the enzyme
nmdcat.online BIO NMDCAT
Jul 11, 2026

Formation of a covalent enzyme substrate intermediate after the first product leaves is characteristic of

A. Sequential ordered mechanism
B. Sequential random mechanism
C. Ping pong double displacement mechanism
D. Concerted acid base mechanism
nmdcat.online BIO NMDCAT
Jul 11, 2026

A ping pong mechanism refers to a kinetic sequence where

A. Substrate inhibits product
B. One product is released before all substrates bind
C. Cooperative binding occurs
D. Non competitive inhibition occurs
nmdcat.online BIO NMDCAT
Jul 11, 2026
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