Final answer:
The pancreatic enzyme requiring an activator is trypsin, which is activated in the small intestine by the enzyme enteropeptidase, to prevent self-digestion of the pancreas.
Step-by-step explanation:
The pancreatic enzyme requiring an activator is trypsin, and its activation is a crucial step in the cascade of events that facilitate effective protein digestion. Pancreatic acinar cells produce a zymogen, or inactive precursor, called trypsinogen. This inactive form of trypsin is transformed into its active state, trypsin, by the action of an intestinal brush border enzyme called enteropeptidase. This activation occurs specifically in the duodenum of the small intestine.
Once activated, trypsin plays a central role in the digestion of proteins. Importantly, trypsin has the ability to further activate other pancreatic zymogens. For instance, trypsin can activate procarboxypeptidase into its active form, carboxypeptidase, which functions in the breakdown of peptide bonds at the C-terminal end of proteins. Additionally, trypsin can activate chymotrypsinogen, converting it into chymotrypsin, another enzyme essential for protein digestion.
The activation of these enzymes takes place in the small intestine rather than in the pancreas itself. This spatial separation is critical in preventing premature activation of digestive enzymes within the pancreas, a condition known as pancreatitis. If the activation occurred within the pancreas, the enzymes would begin digesting the pancreatic tissue, leading to inflammation and damage. Therefore, the controlled activation of trypsin and subsequent activation of other enzymes in the small intestine ensure a well-regulated and localized process of protein digestion, safeguarding the pancreas from self-digestion and maintaining the efficiency of nutrient absorption in the digestive system.