Question
Trypsin cleaves :
| A. |
Arginine |
| B. |
Glutamate |
| C. |
None |
| D. |
Proline |
|
Correct Answer » A Explanation |
 |
Detailed Explanation:
Anatomical Role
– Trypsin is a serine protease enzyme produced by the pancreas.
– It functions in the small intestine to digest proteins by cleaving peptide bonds.
Clinical Reasoning for the Correct Answer
– Trypsin specifically cleaves peptide bonds at the carboxyl side of basic amino acids, primarily arginine and lysine.
– This specificity allows breakdown of dietary proteins into smaller peptides for absorption.
Why Option A is Correct:
– Arginine is a basic amino acid with a positively charged side chain.
– Trypsin hydrolyzes peptide bonds after arginine residues, facilitating protein digestion.
Why Option B is Incorrect:
– Glutamate is an acidic amino acid with a negatively charged side chain.
– Trypsin does not cleave peptide bonds at glutamate; instead, glutamyl endopeptidases target these residues.
Why Option C is Incorrect:
– Trypsin definitely cleaves peptide bonds; “None” is false.
– Without cleavage, protein digestion would not occur efficiently.
Why Option D is Incorrect:
– Proline has a unique cyclic structure that constrains peptide bonds.
– Trypsin cannot cleave peptide bonds on the carboxyl side of proline due to steric hindrance.
