Trypsinogen is converted into which active enzyme?

The conversion of trypsinogen into its active form, trypsin, is a key process in the digestive system. Trypsinogen is an inactive enzyme that is produced by the pancreas. Its activation is crucial for the digestive process because trypsin plays a vital role in breaking down proteins in the small intestine.

The activation of trypsinogen occurs when it is exposed to enterokinase, an enzyme secreted by the small intestine. This enzyme cleaves trypsinogen, converting it into trypsin. Once active, trypsin not only continues the protein digestion process by cleaving peptide bonds in protein molecules but also activates other digestive enzymes like chymotrypsin and proelastase, amplifying the digestive process.

While the other options listed (chymotrypsin, proelastase, and carboxypeptidase) are also digestive enzymes that play significant roles in protein digestion, they are either products of different inactive precursors or are not directly derived from the activation of trypsinogen. Thus, recognizing trypsin as the active enzyme derived from trypsinogen helps in understanding the cascade effect of enzyme activation within the digestive tract.