Amino Acid Metabolism — MCQs

Amino Acid Metabolism Indian Medical PG Practice Questions and MCQs

Question 561: Which amino acid in Jowar is responsible for its pellagragenic effect?

A. Leucine (Correct Answer)
B. Lysine
C. Tryptophan
D. Methionine

Explanation: ***Leucine*** - A high intake of **leucine**, an essential amino acid, interferes with the metabolism of **tryptophan** and niacin, leading to **pellagra**. - Jowar (sorghum) contains high levels of leucine, which, when it forms a major part of the diet, can induce **niacin deficiency**. *Lysine* - Lysine is an essential amino acid and is generally considered to be in **limited supply** in many cereal grains, making it a desirable amino acid to increase in diets. - It does not directly contribute to the pellagragenic effect; rather, a deficiency in lysine can be a nutritional concern. *Tryptophan* - Tryptophan is a **precursor to niacin (Vitamin B3)** in the body; a deficiency in tryptophan can lead to pellagra. - The high leucine content in jowar interferes with the conversion of tryptophan to niacin, thus exacerbating niacin deficiency. *Methionine* - Methionine is an **essential sulfur-containing amino acid** important for various metabolic functions and protein synthesis. - It is not directly implicated in the pellagragenic effect associated with high jowar consumption.

Question 562: Transamination of Alanine results in formation of ?

A. Oxaloacetate
B. Pyruvate (Correct Answer)
C. Aspartate
D. Arginine

Explanation: **Pyruvate** ✓ - **Transamination** involves the transfer of an amino group from an amino acid to an α-ketoglutarate (catalyzed by aminotransferases). - When **alanine** undergoes transamination via **ALT (alanine aminotransferase)**, its amino group is transferred to α-ketoglutarate, forming glutamate, while alanine is converted to its corresponding α-keto acid, which is **pyruvate**. - Reaction: Alanine + α-Ketoglutarate ⇄ Pyruvate + Glutamate *Oxaloacetate* - **Oxaloacetate** is the α-keto acid formed from the transamination of **aspartate** (via AST/GOT). - It is a key intermediate in the **citric acid cycle** and gluconeogenesis, not a product of alanine transamination. *Aspartate* - **Aspartate** is an amino acid, not an α-keto acid. - It can be formed from oxaloacetate via transamination (reverse reaction), and is involved in the **urea cycle** and nucleotide synthesis. *Arginine* - **Arginine** is a semi-essential amino acid, not an α-keto acid or a product of alanine transamination. - It plays roles in **protein synthesis**, the urea cycle, and nitric oxide production.

Question 563: Taurine is biosynthesized from which amino acid?

A. Cysteine (Correct Answer)
B. Valine
C. Arginine
D. Leucine

Explanation: ***Cysteine*** - **Taurine** is primarily synthesized from the amino acid **cysteine** through a pathway involving **cysteine sulfinic acid** and **hypotaurine**. - This pathway utilizes enzymes like **cysteine dioxygenase** and **cysteine sulfinic acid decarboxylase**. - The biosynthetic pathway: Cysteine → Cysteine sulfinic acid → Hypotaurine → Taurine. *Arginine* - **Arginine** is a precursor for **nitric oxide**, **urea**, and **creatine**, not taurine. - It is involved in various metabolic pathways, including the **urea cycle** and protein synthesis. *Valine* - **Valine** is a **branched-chain amino acid (BCAA)** involved in protein synthesis and energy production. - It is not a direct precursor for taurine biosynthesis. *Leucine* - **Leucine** is also a **branched-chain amino acid (BCAA)** crucial for protein synthesis and muscle metabolism. - It does not participate in the synthesis of taurine.

Question 564: Hydrolysis occurs at which step of urea cycle ?

A. Formation of ornithine
B. Formation of argininosuccinate
C. Formation of citrulline
D. Cleavage of arginine (Correct Answer)

Explanation: ***Cleavage of arginine*** - The final step in the urea cycle, where **arginine** is hydrolyzed by the enzyme **arginase** to form **urea** and **ornithine**. - This reaction involves the addition of a **water molecule** across the guanidino group to release urea. *Formation of argininosuccinate* - This step involves the condensation of **citrulline** and **aspartate**, catalyzed by **argininosuccinate synthetase**. - It is an **ATP-dependent** reaction, not a hydrolysis. *Formation of citrulline* - Occurs when **carbamoyl phosphate** condenses with **ornithine**, catalyzed by **ornithine transcarbamylase**. - This reaction involves the removal of a phosphate group, not the addition of water. *Formation of ornithine* - **Ornithine** is a substrate for the formation of citrulline and is also regenerated at the end of the cycle from arginine. - Its formation from arginine is a **hydrolysis** reaction, but simply stating "formation of ornithine" is less specific than "cleavage of arginine," which directly describes the hydrolytic event.

Question 565: Which enzyme deficiency is responsible for Hyperammonemia type-1?

A. Arginase deficiency
B. Arginosuccinate lyase deficiency
C. Arginosuccinate synthase deficiency
D. Carbamoyl phosphate synthetase I (CPS-1) deficiency (Correct Answer)

Explanation: ***Carbamoyl phosphate synthetase I (CPS-1) deficiency*** - This enzyme deficiency is classified as **Hyperammonemia type-1**, or **CPS1 deficiency**, and results in the inability to initiate the urea cycle. - **CPS-1** catalyzes the first committed step of the urea cycle, combining ammonia and bicarbonate to form carbamoyl phosphate. *Arginase deficiency* - This deficiency causes **Hyperargininemia**, which is a disorder of the urea cycle distinct from Hyperammonemia type-1. - Arginase is involved in the final step of the urea cycle, converting arginine to urea and ornithine. *Arginosuccinate lyase deficiency* - This deficiency leads to **Argininosuccinic aciduria**, another urea cycle disorder. - **Arginosuccinate lyase** is responsible for breaking down argininosuccinate into arginine and fumarate. *Arginosuccinate synthase deficiency* - This deficiency causes **Citrullinemia type 1**, a metabolic disorder characterized by high levels of citrulline and ammonia. - **Arginosuccinate synthase** catalyzes the condensation of citrulline and aspartate to form argininosuccinate.

Question 566: Carnitine is synthesised from -

A. Lysine (Correct Answer)
B. Histidine
C. Choline
D. Arginine

Explanation: ***Lysine*** - **Carnitine** is synthesized in the liver and kidneys from the amino acids **lysine** and methionine. - **Lysine provides the essential carbon backbone** for carnitine synthesis (trimethyllysine is the actual precursor formed from protein-bound lysine residues). - Methionine contributes methyl groups via S-adenosylmethionine (SAM), but lysine is the primary structural precursor. *Arginine* - **Arginine** is a precursor for **nitric oxide**, urea, and creatine, but not a direct precursor for carnitine synthesis. - While arginine is an amino acid, its metabolic pathways are distinct from those involved in carnitine formation. *Histidine* - **Histidine** is a precursor for **histamine** and contributes to protein synthesis, but is not involved in carnitine biosynthesis. - Its metabolic fate differs significantly from the pathway leading to carnitine. *Choline* - **Choline** is a precursor for **acetylcholine** and phospholipids, but not directly for carnitine. - Although both choline and carnitine contain methyl groups, they have different biosynthetic origins.

Question 567: Which amino acid is used by the liver in the urea cycle?

A. Glutamine
B. Glutamate
C. Aspartate (Correct Answer)
D. Ornithine

Explanation: ***Aspartate*** - **Aspartate** provides the second nitrogen atom to the urea cycle, directly contributing to the formation of **argininosuccinate** through condensation with citrulline. - It is crucial for the efficient removal of **ammonia** in the form of urea. *Glutamine* - **Glutamine** transports ammonia from peripheral tissues to the liver and kidneys, but it is typically deamidated to **glutamate** before its nitrogen can enter the urea cycle. - While it's a major ammonia carrier, it's not directly incorporated into urea as an intact amino acid. *Glutamate* - **Glutamate** can donate its amino group to form **aspartate** (via transamination with oxaloacetate) or release ammonia directly (via glutamate dehydrogenase), both of which then enter the urea cycle. - However, glutamate itself is not directly incorporated into the urea molecule in the same way aspartate is. *Ornithine* - **Ornithine** is an amino acid that participates in the urea cycle as a carrier molecule, being regenerated at the end of each cycle. - While essential for the cycle to function, it is not "used" in the sense of being consumed or providing nitrogen for urea formation - rather it acts as a catalytic intermediate that is recycled.

Question 568: Indole ring is present in?

A. Tryptophan (Correct Answer)
B. Tyrosine
C. Phenylalanine
D. Threonine

Explanation: ***Tryptophan*** - Tryptophan is an **aromatic amino acid** characterized by the presence of an **indole ring** in its side chain. - The indole ring consists of a **benzene ring fused to a pyrrole ring**, which is unique to tryptophan among the standard amino acids. *Tyrosine* - Tyrosine is an **aromatic amino acid** containing a **phenol group** (a benzene ring with a hydroxyl group), not an indole ring. - It is derived from phenylalanine and is a precursor for important molecules like **thyroid hormones** and **catecholamines**. *Phenylalanine* - Phenylalanine is an **aromatic amino acid** with a **benzyl group** (a benzene ring attached to a methylene group) in its side chain. - It lacks the distinct heterocyclic indole structure found in tryptophan. *Threonine* - Threonine is an **aliphatic amino acid** with a **hydroxyl group** on its side chain, classifying it as a **polar, uncharged amino acid**. - It does not contain any ring structures, especially not an indole ring.

Question 569: Which of the following substances is not derived from tyrosine?

A. Thyroxine
B. Melanin
C. Nicotinic acid (Correct Answer)
D. Dopamine

Explanation: ***Nicotinic acid*** - **Nicotinic acid** (niacin, vitamin B3) is synthesized from **tryptophan** in the body, not tyrosine. - It plays a crucial role in metabolism as a precursor for NAD+ and NADH, which are involved in various enzymatic reactions. *Thyroxine* - **Thyroxine** (T4), a thyroid hormone, is derived from the amino acid **tyrosine**. - **Iodine** is incorporated into tyrosine residues on thyroglobulin to form monoiodotyrosine (MIT) and diiodotyrosine (DIT), which then couple to form T4 (and T3). *Melanin* - **Melanin**, the pigment responsible for skin, hair, and eye color, is synthesized from **tyrosine** through a pathway involving the enzyme **tyrosinase**. - This process involves the hydroxylation of tyrosine to 3,4-dihydroxyphenylalanine (DOPA) and subsequent oxidation reactions. *Dopamine* - **Dopamine**, an important neurotransmitter, is synthesized from **tyrosine** in a two-step process in the brain and adrenal medulla. - Tyrosine is first hydroxylated to DOPA by **tyrosine hydroxylase**, and then DOPA is decarboxylated to dopamine by DOPA decarboxylase.

Question 570: Beta-alanine is derived from ?

A. Adenosine
B. Uracil (Correct Answer)
C. Guanosine
D. Thymine

Explanation: ***Correct Option: Uracil*** - **Uracil**, a pyrimidine base found in RNA, is the primary source of **β-alanine** through its catabolic pathway. - The degradation sequence: **Uracil** → **Dihydrouracil** → **β-Ureidopropionate** → **β-Alanine** + CO₂ + NH₃ - This pathway is catalyzed by enzymes including dihydropyrimidine dehydrogenase and β-ureidopropionase. - **β-Alanine** is also obtained from dietary sources and is a component of carnosine and pantothenic acid (Vitamin B5). *Incorrect Option: Thymine* - **Thymine** is a pyrimidine base in DNA with a similar catabolic pathway to uracil. - However, thymine produces **β-aminoisobutyrate** (NOT β-alanine) as its final product. - The pathway: **Thymine** → **Dihydrothymine** → **β-Ureidoisobutyrate** → **β-Aminoisobutyrate** - The extra methyl group on thymine (compared to uracil) results in a different end product. *Incorrect Option: Adenosine* - **Adenosine** is a purine nucleoside composed of adenine and ribose. - Purine catabolism leads to **uric acid** formation, not β-alanine. - It follows the pathway: Adenosine → Inosine → Hypoxanthine → Xanthine → Uric acid. *Incorrect Option: Guanosine* - **Guanosine** is a purine nucleoside consisting of guanine and ribose. - Like adenosine, it is catabolized to **uric acid** via xanthine. - It does not participate in β-alanine synthesis.

Practice by Chapter

Protein Digestion and Absorption

Practice Questions

Transamination and Deamination

Practice Questions

Urea Cycle

Practice Questions

Disorders of Urea Cycle

Practice Questions

Metabolism of Individual Amino Acids

Practice Questions

Inborn Errors of Amino Acid Metabolism

Practice Questions

Phenylketonuria and Alkaptonuria

Practice Questions

Homocystinuria and Methionine Metabolism

Practice Questions

Synthesis of Biologically Important Compounds from Amino Acids

Practice Questions

Nitrogen Balance

Practice Questions

Ammonia Metabolism and Toxicity

Practice Questions

One-Carbon Transfer Reactions

Practice Questions

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