Biological role of amino acids MCQs With Answer

Understanding the biological role of amino acids is essential for B. Pharm students preparing for pharmacology, biochemistry, and therapeutics. This SEO-focused guide on Biological role of amino acids MCQs With Answer explains how amino acids act as protein building blocks, neurotransmitter precursors, metabolic intermediates, and regulators of drug metabolism. Topics covered include essential versus non-essential amino acids, nitrogen balance, urea cycle, gluconeogenesis, ketogenesis, post-translational modifications, and clinical correlations relevant to pharmacy practice. Each question emphasizes mechanism, pathway, and therapeutic relevance to deepen conceptual understanding and exam readiness. Now let’s test your knowledge with 50 MCQs on this topic.

Q1. Which of the following is the primary biological role of amino acids?

  • Acting solely as energy storage molecules
  • Serving as building blocks for proteins and precursors for key metabolites
  • Forming the lipid bilayer of cell membranes
  • Transporting oxygen in the blood

Correct Answer: Serving as building blocks for proteins and precursors for key metabolites

Q2. Which amino acid is a direct precursor for the neurotransmitter serotonin?

  • Tyrosine
  • Tryptophan
  • Glutamate
  • Histidine

Correct Answer: Tryptophan

Q3. Which amino acid is essential for adults and must be obtained from the diet?

  • Alanine
  • Leucine
  • Glycine
  • Glutamine

Correct Answer: Leucine

Q4. Which amino acid serves as the primary nitrogen donor in transamination reactions?

  • Lysine
  • Glutamate
  • Phenylalanine
  • Isoleucine

Correct Answer: Glutamate

Q5. Phenylketonuria (PKU) is caused by a defect in the metabolism of which amino acid?

  • Methionine
  • Phenylalanine
  • Tryptophan
  • Arginine

Correct Answer: Phenylalanine

Q6. Which amino acid is the precursor for nitric oxide synthesis?

  • Arginine
  • Proline
  • Serine
  • Cysteine

Correct Answer: Arginine

Q7. Which amino acid contributes to disulfide bond formation critical for protein tertiary structure?

  • Serine
  • Cysteine
  • Asparagine
  • Valine

Correct Answer: Cysteine

Q8. In gluconeogenesis, which amino acids are considered glucogenic?

  • Amino acids that can be converted to acetyl-CoA only
  • Amino acids that can be converted to glucose precursors such as pyruvate or TCA intermediates
  • Amino acids that form ketogenic bodies exclusively
  • Amino acids that are only used for protein synthesis

Correct Answer: Amino acids that can be converted to glucose precursors such as pyruvate or TCA intermediates

Q9. Which pair of amino acids are strictly ketogenic (cannot form glucose)?

  • Leucine and lysine
  • Alanine and serine
  • Valine and isoleucine
  • Glutamate and glutamine

Correct Answer: Leucine and lysine

Q10. Which amino acid is the major carrier of nitrogen in the blood from peripheral tissues to liver?

  • Alanine
  • Glycine
  • Histidine
  • Methionine

Correct Answer: Alanine

Q11. Which amino acid is methyl donor via S-adenosylmethionine (SAM) pathway?

  • Tryptophan
  • Methionine
  • Threonine
  • Proline

Correct Answer: Methionine

Q12. Tyrosine is a precursor for which of the following groups of molecules?

  • Purines and pyrimidines
  • Catecholamines (dopamine, norepinephrine, epinephrine) and thyroid hormones
  • Fatty acids and cholesterol
  • Histamine and serotonin

Correct Answer: Catecholamines (dopamine, norepinephrine, epinephrine) and thyroid hormones

Q13. Which cofactor is required for transamination reactions catalyzed by aminotransferases?

  • FAD
  • Pyridoxal phosphate (PLP)
  • Biotin
  • NAD+

Correct Answer: Pyridoxal phosphate (PLP)

Q14. Which amino acid is the precursor for the antioxidant glutathione?

  • Leucine
  • Glutamate (as part of synthesis involving cysteine and glycine)
  • Phenylalanine
  • Asparagine

Correct Answer: Glutamate (as part of synthesis involving cysteine and glycine)

Q15. Which amino acid is hydroxylated by prolyl hydroxylase during collagen maturation?

  • Proline
  • Tyrosine
  • Histidine
  • Alanine

Correct Answer: Proline

Q16. Which amino acid side chain has an imidazole group and contributes to enzyme active site acid–base catalysis?

  • Histidine
  • Lysine
  • Aspartate
  • Valine

Correct Answer: Histidine

Q17. The urea cycle primarily disposes of which element derived from amino acid catabolism?

  • Carbon
  • Nitrogen (ammonia)
  • Phosphorus
  • Sulfur

Correct Answer: Nitrogen (ammonia)

Q18. Which enzyme deficiency leads to hyperammonemia type I by impairing the first step of the urea cycle?

  • Ornithine transcarbamylase
  • Carbamoyl phosphate synthetase I
  • Arginase
  • Argininosuccinate lyase

Correct Answer: Carbamoyl phosphate synthetase I

Q19. Which amino acid is involved in one-carbon metabolism and is a precursor for purine synthesis?

  • Glycine
  • Leucine
  • Isoleucine
  • Tyrosine

Correct Answer: Glycine

Q20. Which amino acid contains a sulfur atom and participates in methyl group transfers after conversion to SAM?

  • Cysteine
  • Methionine
  • Serine
  • Threonine

Correct Answer: Methionine

Q21. Which transport mechanism moves amino acids across cell membranes using sodium cotransport in the intestine?

  • Simple diffusion
  • Sodium-dependent secondary active transporters
  • ABC ATP-dependent transporters
  • Endocytosis

Correct Answer: Sodium-dependent secondary active transporters

Q22. Which amino acid is a direct precursor for histamine?

  • Glutamate
  • Histidine
  • Tryptophan
  • Arginine

Correct Answer: Histidine

Q23. In amino acid catabolism, transamination transfers an amino group to which keto acid to form glutamate?

  • Oxaloacetate
  • Alpha-ketoglutarate
  • Pyruvate
  • Succinyl-CoA

Correct Answer: Alpha-ketoglutarate

Q24. Cysteine is semi-essential because it can be synthesized from which essential amino acid?

  • Methionine
  • Phenylalanine
  • Valine
  • Threonine

Correct Answer: Methionine

Q25. Which amino acid side chain is positively charged at physiological pH and often binds negatively charged substrates?

  • Aspartate
  • Lysine
  • Phenylalanine
  • Proline

Correct Answer: Lysine

Q26. Which amino acid is converted to acetyl-CoA and can contribute to ketone body formation?

  • Leucine
  • Alanine
  • Asparagine
  • Glutamine

Correct Answer: Leucine

Q27. Which amino acid is most commonly phosphorylated during signal transduction on proteins?

  • Glycine
  • Serine
  • Proline
  • Valine

Correct Answer: Serine

Q28. Which amino acid derivative acts as a neurotransmitter and is synthesized from glutamate?

  • GABA (gamma-aminobutyric acid)
  • Serotonin
  • Dopamine
  • Acetylcholine

Correct Answer: GABA (gamma-aminobutyric acid)

Q29. Which amino acid is a precursor for creatine synthesis important in muscle energy metabolism?

  • Glycine and arginine (with methionine providing methyl groups)
  • Phenylalanine alone
  • Leucine and isoleucine
  • Threonine and valine

Correct Answer: Glycine and arginine (with methionine providing methyl groups)

Q30. The isoelectric point (pI) of an amino acid is defined as:

  • The pH at which the amino acid is fully protonated
  • The pH at which the amino acid carries no net electrical charge
  • The pH at which the amino acid is completely deprotonated
  • The pH where solubility is maximal

Correct Answer: The pH at which the amino acid carries no net electrical charge

Q31. Which amino acid modification is critical for anchoring some proteins to membranes via glycosylphosphatidylinositol (GPI) anchors?

  • Ubiquitination of lysine residues
  • Addition of a GPI anchor to a C-terminus glycine
  • Phosphorylation of serine residues
  • Nitration of tyrosine residues

Correct Answer: Addition of a GPI anchor to a C-terminus glycine

Q32. Which amino acid is directly involved in bile acid conjugation (taurine conjugation)?

  • Arginine
  • Taurine (derived from cysteine)
  • Leucine
  • Phenylalanine

Correct Answer: Taurine (derived from cysteine)

Q33. Which amino acid is required for synthesis of porphyrins and thus heme?

  • Glycine (with succinyl-CoA)
  • Methionine
  • Valine
  • Threonine

Correct Answer: Glycine (with succinyl-CoA)

Q34. Which enzyme catalyzes the deamination of glutamate to release ammonia for urea cycle entry?

  • Glutamate dehydrogenase
  • Glutamine synthetase
  • Alanine aminotransferase
  • Phenylalanine hydroxylase

Correct Answer: Glutamate dehydrogenase

Q35. Branched-chain amino acids (BCAAs) are primarily metabolized in which tissue?

  • Liver
  • Muscle
  • Adipose tissue
  • Kidney

Correct Answer: Muscle

Q36. Which amino acid contributes sulfur for synthesis of coenzyme A and lipoic acid indirectly through methionine?

  • Leucine
  • Methionine
  • Tyrosine
  • Alanine

Correct Answer: Methionine

Q37. Which amino acid residue often undergoes N-linked glycosylation in secreted proteins?

  • Asparagine (N-linked)
  • Serine
  • Tyrosine
  • Proline

Correct Answer: Asparagine (N-linked)

Q38. Which amino acid is a precursor for melatonin synthesis in the pineal gland?

  • Tyrosine
  • Tryptophan
  • Histidine
  • Arginine

Correct Answer: Tryptophan

Q39. Which metabolic fate describes amino acids that give rise to both glucose and ketone precursors?

  • Exclusively glucogenic
  • Exclusively ketogenic
  • Both glucogenic and ketogenic
  • Neither glucogenic nor ketogenic

Correct Answer: Both glucogenic and ketogenic

Q40. Which amino acid is oxidized to produce fumarate in the TCA cycle intermediates list?

  • Phenylalanine and tyrosine (via fumarate)
  • Leucine only
  • Glycine only
  • Lysine only

Correct Answer: Phenylalanine and tyrosine (via fumarate)

Q41. In drug development, why is knowledge of amino acid transporters important?

  • They are irrelevant to drug absorption and targeting
  • They influence oral absorption, BBB penetration, and targeted delivery of peptide-like drugs
  • They only transport lipids
  • They solely regulate hormonal secretion

Correct Answer: They influence oral absorption, BBB penetration, and targeted delivery of peptide-like drugs

Q42. Which amino acid side chain is aromatic and can participate in stacking interactions in proteins?

  • Alanine
  • Phenylalanine
  • Serine
  • Arginine

Correct Answer: Phenylalanine

Q43. Which inherited disorder results from defective homogentisate oxidase leading to accumulation of homogentisic acid from tyrosine degradation?

  • Alkaptonuria
  • Phenylketonuria
  • Maple syrup urine disease
  • Homocystinuria

Correct Answer: Alkaptonuria

Q44. Which amino acid can be phosphorylated on a protein and also serve as a precursor for glycine and serine interconversion?

  • Threonine
  • Serine
  • Valine
  • Tyrosine

Correct Answer: Serine

Q45. Which enzyme converts phenylalanine to tyrosine and requires tetrahydrobiopterin (BH4)?

  • Tyrosine hydroxylase
  • Phenylalanine hydroxylase
  • Phenylalanine ammonia-lyase
  • Tyrosinase

Correct Answer: Phenylalanine hydroxylase

Q46. Which amino acid is critically involved in metal ion binding in metalloproteins via its thiol group?

  • Cysteine
  • Glycine
  • Asparagine
  • Glutamate

Correct Answer: Cysteine

Q47. Homocystinuria is most commonly associated with a defect in which metabolic process?

  • Branched-chain amino acid catabolism
  • Methionine metabolism and remethylation/transsulfuration pathways
  • Tryptophan to serotonin conversion
  • Glycine cleavage system

Correct Answer: Methionine metabolism and remethylation/transsulfuration pathways

Q48. Which amino acid is often involved in helix-breaking due to its rigid cyclic structure?

  • Proline
  • Glutamine
  • Leucine
  • Threonine

Correct Answer: Proline

Q49. Which amino acid generally increases during starvation to provide substrate for gluconeogenesis in the liver?

  • Branched-chain amino acids (e.g., alanine from muscle transamination)
  • Histidine only
  • Phenylalanine only
  • Methionine only

Correct Answer: Branched-chain amino acids (e.g., alanine from muscle transamination)

Q50. Why is pyridoxal phosphate (PLP) an important pharmacologically relevant cofactor in amino acid metabolism?

  • It functions as an electron carrier in the ETC
  • It is required for transamination, decarboxylation, and racemization reactions affecting neurotransmitter and amino acid drug metabolism
  • It stores methyl groups for DNA methylation
  • It transports amino acids across membranes

Correct Answer: It is required for transamination, decarboxylation, and racemization reactions affecting neurotransmitter and amino acid drug metabolism

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