Procarboxypeptidase A and B are converted into what by trypsin?

Procarboxypeptidase A and B are inactive precursors or zymogens that require activation to perform their role in protein digestion. This activation is catalyzed by trypsin, an enzyme that specifically cleaves these zymogens at particular sites to convert them into their active forms, known as carboxypeptidase A and B.

Carboxypeptidases are enzymes that function in the gastrointestinal tract, facilitating the digestion of proteins by removing amino acids from the carboxyl end of peptide chains. Thus, the transformation of procarboxypeptidase A and B into their active forms by trypsin is fundamental for the effective breakdown of dietary proteins into absorbable units. The conversion into active carboxypeptidases is necessary for their physiological function, making them crucial in the overall process of digestion.