NEET-PG 2013 - Biochemistry Practice Questions

Q: The main function of Vitamin C in the body is

Cofactor for hydroxylation reactions in collagen synthesis. ***Cofactor for hydroxylation reactions in collagen synthesis*** - Vitamin C (ascorbic acid) serves as an essential **cofactor** for **prolyl hydroxylase** and **lysyl hydroxylase** enzymes. - These enzymes catalyze the **hydroxylation of proline and lysine** residues in collagen, forming **hydroxyproline** and **hydroxylysine**. - This hydroxylation is crucial for the **stability and cross-linking** of collagen triple helix structure. - Deficiency leads to **scurvy**, characterized by defective collagen synthesis, bleeding gums, poor wound healing, and bone abnormalities. - This is the **primary and main function** of Vitamin C in the human body. *Involvement as antioxidant* - While Vitamin C does act as a **water-soluble antioxidant**, protecting cells from oxidative damage by free radicals, this is a **secondary function**. - It can donate electrons to neutralize reactive oxygen species and regenerate other antioxidants like Vitamin E. - This protective role is important but not the main function compared to its role in collagen synthesis. *Regulation of lipid synthesis* - Vitamin C is **not directly involved** in the primary pathways of lipid synthesis or metabolism. - It may play a minor role in **carnitine synthesis** (needed for fatty acid oxidation), but this is not a major function. - Other nutrients like B vitamins play more significant roles in lipid metabolism regulation. *Inhibition of cell growth* - Vitamin C does **not inhibit normal cell growth**; it is essential for cell health, differentiation, and tissue repair. - While high doses may have some anti-proliferative effects in certain cancer cell lines in vitro, this is not a physiological function in the healthy body.

Q: Which of the following is NOT required for gluconeogenesis from lactate?

Transamination of pyruvate to alanine. ***Transamination of pyruvate to alanine*** - While **alanine** can be a substrate for gluconeogenesis, **lactate** is directly converted to pyruvate, which then enters the gluconeogenesis pathway. **Transamination to alanine** is not a required intermediate step for lactate-derived glucose production. - The direct conversion of **lactate to pyruvate** by **lactate dehydrogenase** is the key initial step, not its conversion to alanine. *Transport of lactate from muscle to liver* - **Lactate** produced in muscles (e.g., during intense exercise) must be transported to the **liver** via the bloodstream to be used for **gluconeogenesis** in the **Cori cycle**. - This transport is essential for clearing lactate from the periphery and supplying the liver with a gluconeogenic precursor. *Conversion of lactate to pyruvate* - **Lactate dehydrogenase** catalyzes the reversible conversion of **lactate to pyruvate**, which is the critical first step in converting lactate into a gluconeogenic substrate. - This reaction regenerates **NAD+** (not NADH), which is necessary for glycolysis to continue in muscle tissue. *None of the above* - This option is incorrect because there IS a step listed above that is not required: **transamination of pyruvate to alanine** is indeed not necessary for gluconeogenesis from lactate, making Option A the correct answer to this "NOT required" question.

Q: Which of the following statements regarding collagen synthesis is incorrect?

Hydroxylation of proline occurs in Golgi apparatus. ***Hydroxylation of proline occurs in Golgi apparatus*** - This statement is incorrect because the **hydroxylation of proline** residues occurs in the **endoplasmic reticulum** (ER), not the Golgi apparatus. - This step is critical for forming stable **triple helix** structures of collagen and requires **vitamin C**. *Synthesized in ribosomes as preprocollagen* - This statement is correct. Collagen synthesis begins in the cytoplasm, where mRNA is translated by **ribosomes** into **preprocollagen**, which contains a signal peptide. - The signal peptide directs the nascent polypeptide chain into the lumen of the **endoplasmic reticulum**. *Hydroxylation of lysine occurs in ER* - This statement is correct. Following entry into the ER, specific **lysine** residues are hydroxylated by **lysyl hydroxylase** to form hydroxylysine. - This hydroxylation, along with that of proline, is crucial for **cross-linking** and stability of the collagen molecule. *Triple helix assembly occurs in ER* - This statement is correct. After hydroxylation and glycosylation of some residues, three procollagen alpha chains self-assemble to form a **triple helix** within the **endoplasmic reticulum**. - This assembly is stabilized by **disulfide bonds** at the C-terminal ends and molecular chaperones.

Q: Which enzyme catalyzes oxidative deamination?

Glutamate dehydrogenase. ***Glutamate dehydrogenase*** - This enzyme catalyzes the conversion of **glutamate** to **α-ketoglutarate** and ammonia (NH₃), which is an oxidative deamination reaction. - It utilizes **NAD⁺ or NADP⁺** as a coenzyme to remove hydrogen atoms during the oxidation process. - Plays a crucial role in both **amino acid catabolism** and anabolism. *Glutaminase* - This enzyme hydrolyzes **glutamine** to glutamate and ammonia, which is a **hydrolytic deamidation** reaction, not an oxidative deamination. - It does not involve the oxidation of the substrate or require NAD⁺/NADP⁺ as cofactors. *Glutamine synthase* - This enzyme synthesizes **glutamine** from glutamate and ammonia, using ATP, which is a **biosynthetic** reaction, not a catabolic deamination. - It is involved in **ammonia detoxification** and amino acid synthesis, functioning in the opposite direction of deamination. *None of the options* - This option is incorrect because **glutamate dehydrogenase** is a valid correct answer. - Glutamate dehydrogenase is the primary enzyme responsible for oxidative deamination in human metabolism.

Q: What is the main enzyme involved in glycogen breakdown (glycogenolysis)?

Glycogen phosphorylase. ***Glycogen phosphorylase*** - This is the **rate-limiting and primary enzyme** for **glycogenolysis**, the breakdown of glycogen into glucose units. - It cleaves **α-1,4-glycosidic bonds** in glycogen, releasing **glucose-1-phosphate** units. - Regulated by both **allosteric mechanisms** and **hormonal control** (epinephrine, glucagon). - Works until it reaches 4 glucose residues from a branch point, where debranching enzyme takes over. *Glycogen synthase* - This is the main enzyme for **glycogenesis** (glycogen synthesis), not breakdown. - It catalyzes formation of α-1,4-glycosidic bonds to build glycogen chains. - This is the opposite direction of metabolism from what the question asks about. *Glucose-6-phosphatase* - This enzyme is involved in **gluconeogenesis** and the final step of converting **glucose-6-phosphate to free glucose**. - It is NOT directly involved in glycogen breakdown itself, but rather in the subsequent conversion pathway. - Found primarily in **liver and kidney** to release free glucose into blood. *Hexokinase* - This enzyme phosphorylates free glucose to **glucose-6-phosphate** (opposite direction). - It is involved in **glucose utilization**, not glycogen breakdown. - It traps glucose inside cells for metabolism or glycogen synthesis.

Q: Fructose intolerance is due to deficiency of which enzyme?

Aldolase B. ***Aldolase B*** - **Hereditary fructose intolerance** is a genetic disorder caused by a deficiency in the enzyme **aldolase B**. - This deficiency leads to an accumulation of **fructose-1-phosphate** in the liver, kidneys, and small intestine, causing **hypoglycemia**, **vomiting**, and **liver damage** upon exposure to fructose. *Fructokinase* - A deficiency in **fructokinase** causes **essential fructosuria**, a benign metabolic disorder. - This condition is asymptomatic because **fructose** simply accumulates in the blood and urine without causing significant clinical problems. *Triokinase* - **Triokinase**, also known as **glycerol kinase**, is involved in glycerol metabolism, converting glycerol to **glycerol-3-phosphate**. - Its deficiency is not directly linked to fructose intolerance and typically presents with **hyperglycerolemia**. *Aldolase A* - **Aldolase A** is one of the three aldolase isoenzymes (A, B, and C) and is primarily involved in **glycolysis**, specifically in the breakdown of **fructose-1,6-bisphosphate**. - A deficiency in aldolase A can lead to **hemolytic anemia** and **myopathy**, not directly fructose intolerance.

Q: Trypsinogen is converted to trypsin by?

Removal of specific amino acids from trypsinogen. ***Removal of specific amino acids from trypsinogen*** - Trypsinogen is an **inactive zymogen** that is activated by the enzymatic cleavage of a **short N-terminal peptide**. - This cleavage event, primarily catalyzed by **enteropeptidase** (or trypsin itself), transforms trypsinogen into active **trypsin**, a process known as **proteolytic activation**. *Combination of 2 molecules of trypsinogen* - The activation of trypsinogen to trypsin is a **unimolecular conformational change** followed by proteolytic cleavage, not a combination reaction between two zymogen molecules. - While trypsin can activate other trypsinogen molecules, the initial activation does not involve the physical combination of two zymogen molecules. *Phosphorylation* - **Phosphorylation** is a common regulatory mechanism in proteins but is not the primary method for activating inactive trypsinogen. - Trypsinogen activation relies on a **proteolytic cleavage event**, rather than the addition of a phosphate group. *Addition of alkyl group* - The addition of an **alkyl group** is not a known mechanism for the physiological activation of trypsinogen. - Enzymatic activation typically involves **hydrolysis of peptide bonds** or other specific post-translational modifications.

Q: Which of the following is not an androgen?

17α-hydroxyprogesterone. ***17α-hydroxyprogesterone*** - This is a **progesterone derivative** and an intermediate in the synthesis of androgens and corticosteroids, but it does **not possess significant androgenic activity** itself. - Its primary role is as a precursor, rather than a direct androgen. *Testosterone* - **Testosterone** is the **primary male sex hormone** and a potent androgen, responsible for the development of male secondary sexual characteristics. - It plays crucial roles in muscle mass, bone density, libido, and erythropoiesis. *Dihydrotestosterone* - **Dihydrotestosterone (DHT)** is a potent androgen, formed from testosterone by the enzyme 5α-reductase. - DHT is responsible for the development of external male genitalia during fetal development and contributes to prostate growth and male pattern baldness in adults. *Androstenedione* - **Androstenedione** is a **weak androgen** and an important **precursor hormone** in the biosynthesis of testosterone and estrogens. - It is produced in the adrenal glands and gonads, serving as an intermediate step in steroidogenesis.

Q: Which type of RNA is most commonly associated with pseudouridine?

transfer RNA (tRNA). ***Transfer RNA (tRNA)*** - **Pseudouridine (ψ)** is one of the most abundant modified nucleosides in RNA, and **tRNA contains the highest proportion** of pseudouridine modifications among all RNA types. - **tRNA molecules can contain up to 10-15% modified bases**, with pseudouridine being particularly abundant in the **TψC arm** (thymine-pseudouridine-cytosine loop). - These modifications are critical for **tRNA stability, proper folding, and accurate codon-anticodon recognition** during translation. - Pseudouridine enhances base stacking and stabilizes RNA structure through additional hydrogen bonding capability. *Ribosomal RNA (rRNA)* - While rRNA does contain pseudouridine modifications, they are present in **lower proportions compared to tRNA**. - rRNA pseudouridine modifications do play important roles in **ribosomal assembly and function**, but tRNA remains the RNA type most commonly associated with this modification. *Messenger RNA (mRNA)* - **mRNA is generally much less modified** than tRNA or rRNA. - Pseudouridine modifications in mRNA are relatively rare in prokaryotes and were only recently discovered to be more common in eukaryotic mRNA. - When present, they may affect **mRNA stability and translation efficiency**. *DNA* - **DNA does not contain pseudouridine** as this is an RNA-specific modification. - Pseudouridine is formed by **post-transcriptional isomerization** of uridine residues in RNA.

Q: Carboxypeptidase contains which mineral?

Zinc. ***Zinc*** - **Carboxypeptidase** is a **metalloenzyme**, meaning it requires a metal ion for its catalytic activity. - **Zinc** acts as a crucial cofactor in the active site of carboxypeptidase, enabling its proteolytic function. *Copper* - **Copper** is a component of enzymes like **cytochrome c oxidase** and **superoxide dismutase**, but not carboxypeptidase. - Its presence is essential for processes like **electron transport** and **antioxidant defense**. *Iron* - **Iron** is a central component of **hemoglobin** and **myoglobin** for oxygen transport, and in enzymes like **catalase** and **peroxidase**. - It is not involved in the catalytic mechanism of carboxypeptidase. *None of the options* - This option is incorrect because **Zinc** is a known and essential mineral for the function of carboxypeptidase. - Carboxypeptidase is a metalloenzyme, and a metal cofactor is required for its activity.

Question 1

The main function of Vitamin C in the body is

Accepted Answer

Cofactor for hydroxylation reactions in collagen synthesis

Answer

Regulation of lipid synthesis

Answer

Involvement as antioxidant

Answer

Inhibition of cell growth

Question 2

Which of the following is NOT required for gluconeogenesis from lactate?

Accepted Answer

Transamination of pyruvate to alanine

Answer

Transport of lactate from muscle to liver

Answer

Conversion of lactate to pyruvate

Answer

None of the above

Question 3

Which of the following statements regarding collagen synthesis is incorrect?

Accepted Answer

Hydroxylation of proline occurs in Golgi apparatus

Answer

Hydroxylation of lysine occurs in ER

Answer

Synthesized in ribosomes as preprocollagen

Answer

Triple helix assembly occurs in ER

Question 4

Which enzyme catalyzes oxidative deamination?

Accepted Answer

Glutamate dehydrogenase

Answer

Glutaminase

Answer

Glutamine synthase

Answer

None of the options

Question 5

What is the main enzyme involved in glycogen breakdown (glycogenolysis)?

Accepted Answer

Glycogen phosphorylase

Answer

Glycogen synthase

Answer

Glucose-6-phosphatase

Answer

Hexokinase

Question 6

Fructose intolerance is due to deficiency of which enzyme?

Accepted Answer

Aldolase B

Answer

Aldolase A

Answer

Fructokinase

Answer

Triokinase

Question 7

Trypsinogen is converted to trypsin by?

Accepted Answer

Removal of specific amino acids from trypsinogen

Answer

Combination of 2 molecules of trypsinogen

Answer

Phosphorylation

Answer

Addition of alkyl group

Question 8

Which of the following is not an androgen?

Accepted Answer

17α-hydroxyprogesterone

Answer

Testosterone

Answer

Dihydrotestosterone

Answer

Androstenedione

Question 9

Which type of RNA is most commonly associated with pseudouridine?

Accepted Answer

transfer RNA (tRNA)

Answer

messenger RNA (mRNA)

Answer

ribosomal RNA (rRNA)

Answer

DNA

Question 10

Carboxypeptidase contains which mineral?

Accepted Answer

Zinc

Answer

Copper

Answer

Iron

Answer

None of the options

NEET-PG 2013 — Biochemistry