Editing Trypsin (section)

== Function ==

In the [[duodenum]], trypsin [[catalysis|catalyzes]] the [[hydrolysis]] of [[peptide bonds]], breaking down proteins into smaller peptides. The peptide products are then further hydrolyzed into amino acids via other proteases, rendering them available for absorption into the blood stream. Tryptic digestion is a necessary step in protein absorption, as proteins are generally too large to be absorbed through the lining of the [[small intestine]].<ref name="tdmu.edu.ua">{{cite web|url=http://intranet.tdmu.edu.ua/data/kafedra/internal/distance/lectures_stud/English/2%20course/Elective%20course%20(Clinical%20biochemistry)/10.%20METABOLISM%20OF%20AMINOACIDS.%20DIGESTION%20OF%20%20PROTEINS..htm|title=Digestion of Proteins|date=July 14, 2015<!--last mod date from page info-->|website=Elective course (Clinical biochemistry)|publisher=Ternopil National Medical University|access-date=April 11, 2020|archive-date=August 8, 2020|archive-url=https://web.archive.org/web/20200808171058/http://intranet.tdmu.edu.ua/data/kafedra/internal/distance/lectures_stud/English/2|url-status=dead}}</ref>

Trypsin is produced as the inactive [[zymogen]] trypsinogen in the pancreas. When the pancreas is stimulated by [[cholecystokinin]], it is then secreted into the first part of the small intestine (the [[duodenum]]) via the [[pancreatic duct]]. Once in the small intestine, the enzyme [[enteropeptidase|enterokinase]] (also called enteropeptidase) activates trypsinogen into trypsin by [[proteolytic cleavage]]. The trypsin then activates additional trypsin, [[chymotrypsin]] and [[carboxypeptidase]].