Which enzyme is converted from trypsinogen in the pancreas?

Trypsinogen is an inactive zymogen form of the enzyme trypsin, produced by the pancreas. When trypsinogen is secreted into the small intestine, it is activated by an enzyme called enteropeptidase (or enterokinase). This activation process cleaves trypsinogen to form active trypsin.

Trypsin plays a crucial role in digestion as it catalyzes the breakdown of proteins into smaller peptides, further promoting protein digestion alongside other enzymes. The activation of trypsinogen to trypsin is a critical step in the digestive process, ensuring that proteins can be effectively digested in the small intestine.

The other choices refer to different enzymes that are also secreted as zymogens and are activated in the digestive process, but they are not direct products of the activation of trypsinogen. For example, chymotrypsinogen is converted to chymotrypsin by trypsin, while procarboxypeptidase A and proelastase are activated by other means in the digestive pathway.