Explore: Enterokinase

Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase

enterokinase into its active form trypsin. Chymotrypsinogen, which is an inactive (zymogenic) protease that, once activated by duodenal enterokinase,

peptide: DYKDHD-G-DYKDHD-I-DYKDDDDK (with the final tag encoding an enterokinase cleavage site). FLAG-tag can be fused to the C-terminus or the N-terminus

proteins to amino acids or small peptides. Enteropeptidase (also known as enterokinase) is responsible for activating pancreatic trypsinogen into trypsin, which

trypsin is trypsinogen, which is activated by a very specific protease, enterokinase, secreted by the mucosa of the duodenum. The trypsin, once activated

proenzymes. When released into the duodenum, they are activated by the enzyme enterokinase present in the lining of the duodenum. The proenzymes are cleaved, creating

in the inactive form trypsinogen, it is activated by the intestinal enterokinase in intestinal juice. Trypsin can then activate other protease enzymes

domain contains multiple extracellular SEA (sea urchin sperm protein, enterokinase, and agrin) modules, a transmembrane domain, and a cytoplasmic tail.

pancreas in the form of trypsinogen, which is activated in the duodenum by enterokinase to form trypsin. Trypsin then cleaves proteins to smaller polypeptides

duodenum) via the pancreatic duct. Once in the small intestine, the enzyme enterokinase (also called enteropeptidase) activates trypsinogen into trypsin by proteolytic