Amino Acid Metabolism — MCQs

Amino Acid Metabolism Indian Medical PG Practice Questions and MCQs

Question 571: Which cofactor is primarily associated with the activity of glutamate dehydrogenase?

A. NAD+ (Correct Answer)
B. FAD
C. FMN
D. FADH2

Explanation: ***NAD+*** - Glutamate dehydrogenase catalyzes the oxidative deamination of **glutamate** to **α-ketoglutarate** and ammonia, and this reaction primarily uses **NAD+** as an electron acceptor. - In some organisms and contexts, it can also use **NADP+**, but **NAD+** is the more common and significant cofactor for its catabolic role. *FAD* - **FAD (flavin adenine dinucleotide)** is typically associated with **flavoproteins** and enzymes involved in oxidation-reduction reactions, such as those in the **electron transport chain** and the **Krebs cycle**. - Enzymes like **succinate dehydrogenase** use FAD, not glutamate dehydrogenase. *FMN* - **FMN (flavin mononucleotide)** is another flavin coenzyme, similar to FAD, and is found in various **flavoproteins** and enzymes of the **electron transport chain**, such as **NADH dehydrogenase (Complex I)**. - It does not serve as a primary cofactor for **glutamate dehydrogenase** activity. *FADH2* - **FADH2** is the reduced form of **FAD**, carrying high-energy electrons to the **electron transport chain** for ATP synthesis. - It's a product or reactant of various metabolic pathways, but not a direct cofactor for **glutamate dehydrogenase**.

Question 572: Which of the following enzymes is not involved in the urea cycle?

A. Arginase
B. Argininosuccinate lyase
C. CPS-II (Correct Answer)
D. CPS-I

Explanation: ***CPS-II*** - Carbamoyl phosphate synthetase II is involved in **pyrimidine synthesis**, not the urea cycle. - It uses **glutamine** as a nitrogen donor and is located in the **cytosol**. *CPS-I* - Carbamoyl phosphate synthetase I is the **rate-limiting enzyme** of the urea cycle. - It catalyzes the formation of **carbamoyl phosphate** from **ammonia**, CO2, and ATP in the mitochondria. *Arginase* - Arginase is the **final enzyme** in the urea cycle, converting **arginine** to **ornithine** and **urea**. - This reaction occurs in the cytosol and releases urea for excretion. *Argininosuccinate lyase* - Argininosuccinate lyase catalyzes the cleavage of **argininosuccinate** into **fumarate** and **arginine**. - This is a key step in regenerating arginine for the final step of the urea cycle.

Question 573: Which amino acid requires ascorbic acid for its formation in the body?

A. Lysine
B. Hydroxyproline (Correct Answer)
C. Cysteine
D. Proline

Explanation: ***Hydroxyproline*** - **Ascorbic acid (Vitamin C)** is an essential cofactor for **prolyl hydroxylase** and **lysyl hydroxylase** enzymes - These enzymes catalyze the **post-translational hydroxylation** of proline and lysine residues within collagen chains to form hydroxyproline and hydroxylysine - This hydroxylation is crucial for **stabilization of the collagen triple helix** structure - Hydroxyproline is formed by **modification of proline after incorporation into collagen**, not as a free amino acid - **Scurvy** (Vitamin C deficiency) results in defective collagen due to inadequate hydroxyproline formation *Lysine* - Lysine is an **essential amino acid** obtained from diet - Does not require ascorbic acid for its synthesis or formation - While lysine residues in collagen can be hydroxylated (forming hydroxylysine), the question asks about the amino acid whose formation requires Vitamin C *Cysteine* - Cysteine is a **sulfur-containing amino acid** synthesized from methionine via transsulfuration pathway - Its synthesis does not involve ascorbic acid *Proline* - Proline is a **non-essential amino acid** synthesized from glutamate - **Proline synthesis does not require ascorbic acid** - Proline serves as the precursor that gets hydroxylated to hydroxyproline within collagen

Question 574: Which will activate carbamoyl phosphate synthase I?

A. N-acetyl glutamate (Correct Answer)
B. ATP
C. Acetyl-CoA
D. Ornithine

Explanation: **N-acetyl glutamate** - **N-acetyl glutamate** is an **allosteric activator** of **carbamoyl phosphate synthase I (CPS I)**, which is the mitochondrial enzyme that catalyzes the first committed step of the **urea cycle**. - Its synthesis is stimulated by high levels of **arginine**, linking nitrogen load to urea production. *Acetyl-CoA* - Acetyl-CoA is a common **substrate** and **product** in various metabolic pathways, but it is not a direct activator of CPS I. - It is a precursor for the synthesis of **N-acetyl glutamate**, but does not activate CPS I directly. *Ornithine* - **Ornithine** is a key intermediate of the **urea cycle**, but it does not directly activate CPS I. - It combines with carbamoyl phosphate (the product of CPS I) in the second step of the urea cycle to form citrulline. *ATP* - **ATP** is a **substrate** used by CPS I to provide energy for the synthesis of carbamoyl phosphate. - While essential for the reaction, ATP itself does not act as an allosteric activator of the enzyme.

Question 575: Where does oxidative deamination primarily occur in the human body?

A. Cytoplasm of all cells
B. Mitochondria of all cells
C. Cytoplasm of liver cells
D. Mitochondria of liver cells (Correct Answer)

Explanation: ***Mitochondria of liver cells*** - **Oxidative deamination**, particularly of glutamate, is a central process in **amino acid catabolism** and occurs predominantly in the **mitochondria of liver cells**. - This process is crucial for removing the **amino group (NH3)** from amino acids, forming ammonia, which is then detoxified into urea. *Cytoplasm of all cells* - While cells have cytoplasmic metabolic pathways, the primary enzyme for oxidative deamination, **glutamate dehydrogenase**, is located in the mitochondria. - The cytoplasm primarily handles glycolysis and various synthetic pathways, but not the bulk of oxidative deamination. *Mitochondria of all cells* - Although mitochondria are the site of oxidative metabolism in most cells, the **liver** is the main organ responsible for processing exogenous amino acids and their subsequent comprehensive deamination. - Other cells perform some amino acid metabolism, but not the large-scale oxidative deamination seen in the liver. *Cytoplasm of liver cells* - The cytoplasm of liver cells is involved in various metabolic processes, including gluconeogenesis and fatty acid synthesis. - However, the key enzymes for oxidative deamination are specifically compartmentalized within the **mitochondria** of these cells, not the cytoplasm.

Question 576: Which of the following is a non-essential amino acid?

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

Explanation: ***Tyrosine*** - **Tyrosine** is considered a **non-essential amino acid** because the human body can synthesize it from the essential amino acid **phenylalanine**. - This synthesis occurs via the enzyme **phenylalanine hydroxylase**, making its dietary intake not strictly necessary if phenylalanine is available. *Phenylalanine* - **Phenylalanine** is an **essential amino acid**, meaning the human body **cannot synthesize it** and it must be obtained through the diet. - It serves as a precursor for various important molecules, including tyrosine, contributing to neurotransmitter synthesis. *Lysine* - **Lysine** is an **essential amino acid** that the human body **cannot synthesize** and must be acquired from dietary sources. - It plays a crucial role in **protein synthesis**, calcium absorption, and the production of hormones and enzymes. *Threonine* - **Threonine** is another example of an **essential amino acid** that the human body is **unable to produce** on its own. - It is important for the formation of **collagen** and elastin, and contributes to immune function.

Question 577: Methionine can enter the TCA cycle at which level?

A. Fumarate
B. Oxaloacetate
C. Succinyl-CoA (Correct Answer)
D. Citrate

Explanation: ***Succinyl - CoA*** - Methionine is a **glucogenic amino acid** that is catabolized to propionyl-CoA, which is then converted to **methylmalonyl-CoA** and finally to **succinyl-CoA**. - **Succinyl-CoA** is an intermediate of the **TCA cycle**, allowing methionine-derived carbons to enter the cycle. *Fumarate* - Fumarate is an intermediate of the TCA cycle, but methionine catabolism does not directly produce **fumarate**. - Amino acids like **phenylalanine** and **tyrosine** can be catabolized to fumarate. *Oxaloacetate* - **Oxaloacetate** is a TCA cycle intermediate and can be formed from **pyruvate** (via pyruvate carboxylase) or from certain amino acids like **aspartate** and **asparagine**. - Methionine does not directly convert to oxaloacetate. *Citrate* - **Citrate** is the first intermediate formed in the TCA cycle when **acetyl-CoA** combines with **oxaloacetate**. - Methionine catabolism does not lead to the direct formation of citrate.

Question 578: In starvation, nitrogen is primarily carried from muscle to liver and kidney by which amino acid?

A. Alanine (Correct Answer)
B. Glycine
C. Aspartic acid
D. Asparagine

Explanation: ***Alanine*** - During starvation, muscles break down proteins, and the amino groups from these proteins are transferred to **pyruvate** to form **alanine** via the **glucose-alanine cycle (Cahill cycle)**. - **Alanine** is then released into the bloodstream and transported primarily to the **liver**, where its carbon skeleton can be used for **gluconeogenesis** and the amino group enters the urea cycle. - Note: While alanine is the primary carrier to the liver, **glutamine** is the main nitrogen carrier to the kidney. However, among the given options, alanine is unequivocally the correct answer. *Aspartic acid* - While aspartate is involved in amino group transfer and is a crucial component of the **urea cycle**, it is not the primary carrier for inter-organ nitrogen transport from muscle to liver during starvation. - Its role is more localized within the liver for the urea cycle rather than as a transport amino acid. *Glycine* - Glycine plays roles in various metabolic pathways, including synthesis of heme, purines, and conjugation reactions, but it is not the primary amino acid for carrying nitrogen from muscle to liver during starvation. - Its small size and simple structure make it less suitable for efficient nitrogen transport compared to alanine. *Asparagine* - Asparagine has a minor role in nitrogen transport but is not the primary carrier during starvation. - It is synthesized from **aspartate** and ammonia and is typically involved in protein synthesis and nitrogen storage in some tissues.

Question 579: Neonatal tyrosinemia is due to deficiency of which enzyme?

A. Tyrosine transaminase
B. Hydroxyphenyl pyruvate hydroxylase (Correct Answer)
C. Fumarylacetoacetate hydroxylase
D. Tyrosinase

Explanation: ***Hydroxyphenyl pyruvate hydroxylase*** - **Neonatal (transient) tyrosinemia** is caused by delayed maturation or deficiency of **hydroxyphenylpyruvate hydroxylase** (also called 4-hydroxyphenylpyruvate dioxygenase or HPPD). - This enzyme converts 4-hydroxyphenylpyruvate to homogentisic acid in tyrosine catabolism. - Common in **premature infants** and newborns, leading to elevated tyrosine levels in blood. - The condition is **benign and self-limiting**, usually resolving with **vitamin C supplementation** or as the enzyme matures. - Note: Severe hereditary deficiency of this enzyme causes **tyrosinemia type III**, a distinct and rare disorder. *Fumarylacetoacetate hydroxylase* - Deficiency of **fumarylacetoacetate hydroxylase (FAH)** causes **tyrosinemia type I** (hepatorenal tyrosinemia), NOT neonatal tyrosinemia. - This is a severe hereditary disorder with liver failure, renal tubular dysfunction, and accumulation of toxic metabolites like succinylacetone. - Distinct from the benign transient neonatal form. *Tyrosine transaminase* - Deficiency of **tyrosine transaminase** (tyrosine aminotransferase) causes **tyrosinemia type II** (Richner-Hanhart syndrome). - Presents with corneal ulcers, palmoplantar hyperkeratosis, and sometimes intellectual disability. *Tyrosinase* - Deficiency of **tyrosinase** causes **albinism**, characterized by lack of melanin pigment in skin, hair, and eyes. - Not involved in tyrosine catabolism but in melanin synthesis.

Question 580: Which enzyme is deficient in Isovaleric acidemia?

A. Isovaleryl CoA dehydrogenase (Correct Answer)
B. Phenylalanine hydroxylase
C. Arginase
D. Methylmalonyl CoA mutase

Explanation: ***Isovaleryl CoA dehydrogenase*** - **Isovaleric acidemia** is an **autosomal recessive** metabolic disorder caused by a deficiency in the enzyme **isovaleryl-CoA dehydrogenase** - This enzyme is crucial for the metabolism of **leucine**, a branched-chain amino acid, leading to the accumulation of toxic byproducts like **isovaleryl-CoA** and **isovaleric acid** - Characteristic **sweaty feet odor** due to isovaleric acid accumulation *Phenylalanine hydroxylase* - A deficiency in **phenylalanine hydroxylase** is responsible for **phenylketonuria (PKU)**, a different metabolic disorder involving the metabolism of **phenylalanine** - This enzyme converts **phenylalanine to tyrosine**, and its deficiency leads to the accumulation of phenylalanine and its metabolites, causing neurological damage if untreated *Arginase* - A deficiency in **arginase** causes **argininemia (hyperargininemia)**, which is a disorder of the **urea cycle** - This enzyme converts **arginine into urea and ornithine**, and its deficiency leads to the buildup of arginine and ammonia in the blood, causing neurological symptoms and developmental delay *Methylmalonyl CoA mutase* - A deficiency in **methylmalonyl CoA mutase** causes **methylmalonic acidemia**, another organic acidemia distinct from isovaleric acidemia - This disorder involves **propionate metabolism** and can present with metabolic acidosis, but affects a different metabolic pathway than leucine catabolism

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

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