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Biochemistry

Metabolic pathways, enzymes, proteins

133 Q 3 Topics Take Test
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Difficulty: All Easy Medium Hard 101–110 of 133
Topics in Biochemistry
All Proteins & Enzymes 100 Carbohydrates 100 Lipids 78
Q.101 Medium Proteins & Enzymes
What is the Km (Michaelis constant) in enzyme kinetics?
A The maximum velocity of the enzyme reaction
B The substrate concentration at which enzyme shows half maximal velocity
C The dissociation constant of enzyme-product complex
D The rate of product formation per unit time
Correct Answer:  B. The substrate concentration at which enzyme shows half maximal velocity
EXPLANATION

Km is the substrate concentration at which the reaction velocity is half of Vmax (V = Vmax/2), and it represents the affinity of enzyme for substrate. Lower Km indicates higher affinity.

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Q.102 Medium Proteins & Enzymes
Which statement best describes the Lineweaver-Burk plot?
A It is a plot of substrate concentration versus enzyme concentration
B It is a reciprocal plot (1/v vs 1/[S]) used to determine Km and Vmax
C It shows the effect of temperature on enzyme activity
D It demonstrates the effect of pH on enzyme kinetics
Correct Answer:  B. It is a reciprocal plot (1/v vs 1/[S]) used to determine Km and Vmax
EXPLANATION

The Lineweaver-Burk plot is a double reciprocal plot where 1/v is plotted against 1/[S], allowing easy determination of Km (x-intercept) and Vmax (y-intercept) from linear regression.

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Q.103 Medium Proteins & Enzymes
What is the primary function of chaperone proteins in cells?
A Catalyze biochemical reactions
B Assist in proper protein folding and prevent aggregation
C Transport proteins across membranes
D Degrade misfolded proteins exclusively
Correct Answer:  B. Assist in proper protein folding and prevent aggregation
EXPLANATION

Chaperone proteins like HSP70 and HSP90 facilitate proper protein folding, prevent aggregation, and assist in maintaining protein stability, though some also work with degradation pathways.

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Q.104 Medium Proteins & Enzymes
Which of the following describes cooperative binding in enzymes?
A Binding of substrate increases affinity for subsequent substrates
B Multiple enzymes work simultaneously on different substrates
C Enzyme requires multiple cofactors for activity
D Substrate competes with product for enzyme active site
Correct Answer:  A. Binding of substrate increases affinity for subsequent substrates
EXPLANATION

Cooperative binding (positive cooperativity) occurs when binding of one substrate molecule enhances the affinity of the enzyme for additional substrate molecules, as seen in hemoglobin and phosphofructokinase.

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Q.105 Medium Proteins & Enzymes
Which cofactor is required for the activity of cytochrome c oxidase?
A NAD+
B Heme and copper
C FAD
D Zinc
Correct Answer:  B. Heme and copper
EXPLANATION

Cytochrome c oxidase contains heme a, heme a3, and copper centers (CuA and CuB) essential for electron transfer and oxygen reduction.

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Q.106 Medium Proteins & Enzymes
In hyperammonemia type 1, mutations in which enzyme lead to accumulation of ammonia and subsequent neurotoxicity?
A Carbamoyl phosphate synthetase I (CPS I)
B Glutaminase
C Urease
D Monoamine oxidase
Correct Answer:  A. Carbamoyl phosphate synthetase I (CPS I)
EXPLANATION

Hyperammonemia type 1 (Reye's syndrome-like) results from CPS I deficiency, the first enzyme in the urea cycle. CPS I catalyzes ammonia fixation to form carbamoyl phosphate. Its deficiency prevents ammonia detoxification, causing neurotoxic accumulation.

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Q.107 Medium Proteins & Enzymes
Which amino acid residue, when present in the active site, typically acts as a general acid-base catalyst in serine proteases?
A Aspartate
B Histidine
C Cysteine
D Methionine
Correct Answer:  B. Histidine
EXPLANATION

In serine proteases like trypsin and chymotrypsin, histidine (His57) acts as a general acid-base catalyst. Its imidazole ring (pKa ~6) can both accept and donate protons, facilitating the nucleophilic attack by the serine hydroxyl group on the carbonyl carbon.

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Q.108 Medium Proteins & Enzymes
What is the primary role of protein disulfide isomerases (PDI) in the endoplasmic reticulum?
A Synthesis of disulfide bonds
B Catalyzing disulfide bond rearrangement and preventing aggregation during protein folding
C Degradation of misfolded proteins
D Transport of proteins across the ER membrane
Correct Answer:  B. Catalyzing disulfide bond rearrangement and preventing aggregation during protein folding
EXPLANATION

PDI catalyzes the formation, reduction, and rearrangement of disulfide bonds. In the oxidizing ER environment, PDI helps misfolded proteins achieve correct disulfide bonding patterns, acting as both an isomerase and a chaperone to prevent aggregation.

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Q.109 Medium Proteins & Enzymes
Which of the following correctly describes the relationship between enzyme concentration and reaction velocity in zero-order kinetics?
A Velocity is independent of enzyme concentration
B Velocity is directly proportional to enzyme concentration at saturation
C Velocity increases exponentially with enzyme concentration
D Velocity decreases as enzyme concentration increases
Correct Answer:  B. Velocity is directly proportional to enzyme concentration at saturation
EXPLANATION

In zero-order kinetics (when substrate >> Km), all enzyme active sites are saturated. Velocity is directly proportional to enzyme concentration since V = kcat[E]total when enzyme is the limiting factor.

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Q.110 Medium Proteins & Enzymes
What is the Hill coefficient (n) when it equals 1.0 in enzyme kinetics, and what does this indicate?
A Positive cooperativity with multiple binding sites
B Negative cooperativity between subunits
C No cooperativity; the enzyme follows Michaelis-Menten kinetics
D The enzyme is inhibited competitively
Correct Answer:  C. No cooperativity; the enzyme follows Michaelis-Menten kinetics
EXPLANATION

A Hill coefficient of 1.0 indicates no cooperativity and follows simple Michaelis-Menten kinetics. n > 1 indicates positive cooperativity (like hemoglobin), while n < 1 indicates negative cooperativity.

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