Trypsinogen

Trypsinogen (EC 3.4.23.18/20/21/23/24/26) is the precursor form or zymogen of trypsin, a digestive enzyme.wikipedia
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Trypsin

trypticanti-tryptictrypsin serine proteases
Trypsinogen (EC 3.4.23.18/20/21/23/24/26) is the precursor form or zymogen of trypsin, a digestive enzyme. It is activated by enterokinase, which is found in the intestinal mucosa, to form trypsin. Trypsin cleaves the peptide bond on the carboxyl side of basic amino acids such as arginine and lysine.
Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated.

Pancreatic juice

digestive juicespancreatic fluidspancreatic juices
Produced by the pancreas, it is found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen.
Pancreatic juice is a liquid secreted by the pancreas, which contains a variety of enzymes, including trypsinogen, chymotrypsinogen, elastase, carboxypeptidase, pancreatic lipase, nucleases and amylase.

Enteropeptidase

enterokinase
It is activated by enterokinase, which is found in the intestinal mucosa, to form trypsin.
Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes.

Digestive enzyme

digestive enzymespancreatic enzymepancreatic enzymes
Trypsinogen (EC 3.4.23.18/20/21/23/24/26) is the precursor form or zymogen of trypsin, a digestive enzyme.

Pancreas

pancreaticexocrine pancreaspancreatic development
Produced by the pancreas, it is found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen. Trypsinogen (the inactive form) is stored in the pancreas so that it may be released when required for protein digestion.

Zymogen

proenzymezymogenspro-enzyme
Trypsinogen (EC 3.4.23.18/20/21/23/24/26) is the precursor form or zymogen of trypsin, a digestive enzyme.

Digestion

digestivedigestdigested
Trypsinogen (the inactive form) is stored in the pancreas so that it may be released when required for protein digestion.
For example, trypsin is secreted by pancreas in the form of trypsinogen, which is activated in the duodenum by enterokinase to form trypsin.

SPINK1

A further safeguard against inappropriate trypsin activation is the presence of inhibitors such as bovine pancreatic trypsin inhibitor (BPTI) and serine protease inhibitor Kazal-type 1 (SPINK1), which binds to any trypsin formed.
Trypsinogen is normally created and stored an inactive zymogen of trypsin in the pancreas, but occasionally will autoactivate itself.

Trypsin 1

PRSS1cationic trypsinogenprotease, serine, 1 (trypsin 1)
A mutation at Arg 117, a trypsin-sensitive site, in cationic trypsinogen has been implicated in hereditary pancreatitis, a rare form of early-onset genetic disorder.
Trypsin-1 is the main isoform of trypsinogen secreted by pancreas, the others are trypsin-2 (anionic trypsinogen), and trypsin-3 (meso-trypsinogen).

Pancreatitis

inflammation of the pancreasgallstone pancreatitispancreatic inflammation
High levels are seen in acute pancreatitis and cystic fibrosis.
There is an inherited form that results in the activation of trypsinogen within the pancreas, leading to autodigestion.

Protein precursor

precursorprecursor proteinpropeptide
Trypsinogen (EC 3.4.23.18/20/21/23/24/26) is the precursor form or zymogen of trypsin, a digestive enzyme.

Amylase

amylasesα-amylaseamylolytic
Produced by the pancreas, it is found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen.

Lipase

lipaseslipase LIPFE1104
Produced by the pancreas, it is found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen.

Chymotrypsinogen

Produced by the pancreas, it is found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen.

Gastrointestinal tract

intestinegastrointestinaldigestive tract
It is activated by enterokinase, which is found in the intestinal mucosa, to form trypsin.

Peptide bond

peptide bondsamide bondprotein backbone
Trypsin cleaves the peptide bond on the carboxyl side of basic amino acids such as arginine and lysine.

Amino acid

amino acidsresiduesresidue
Trypsin cleaves the peptide bond on the carboxyl side of basic amino acids such as arginine and lysine.

Arginine

ArgL-arginineR
Trypsin cleaves the peptide bond on the carboxyl side of basic amino acids such as arginine and lysine.

Lysine

Lyslysine degradationL-lysine
Trypsin cleaves the peptide bond on the carboxyl side of basic amino acids such as arginine and lysine. Enteropeptidase is produced by the mucosa of duodenum and it cleaves the peptide bond of trypsinogen after residue 15, which is a lysine.

Duodenum

duodenaldodecadactylumduodenal cap
Trypsinogen is released by the pancreas into the second part of the duodenum, via the pancreatic duct, along with other digestive enzymes.

Pancreatic duct

accessory pancreatic ductDuct of Santorinimain pancreatic duct
Trypsinogen is released by the pancreas into the second part of the duodenum, via the pancreatic duct, along with other digestive enzymes.

Mucous membrane

mucosamucous membranesmucosal
Enteropeptidase is produced by the mucosa of duodenum and it cleaves the peptide bond of trypsinogen after residue 15, which is a lysine.

Oxyanion hole

oxanion holeoxyanion holes
The amino group of Gly 193 orientates itself into the correct position, which completes the oxyanion hole in active site, thereby activating the protein.

Aprotinin

BPTIbovine pancreatic trypsin inhibitorTrasylol
A further safeguard against inappropriate trypsin activation is the presence of inhibitors such as bovine pancreatic trypsin inhibitor (BPTI) and serine protease inhibitor Kazal-type 1 (SPINK1), which binds to any trypsin formed.

Aspartic acid

aspartateAspL-aspartate
Trypsin autocatalytic activation of trypsinogen is also a slow process due to the presence of a large negative charge on the conserved N-terminal hexapeptide of trypsinogen, which repels the aspartate on the back of trypsin's specificity pocket.