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In biochemistry, a zymogen (/ ˈ z aɪ m ə dʒ ən,-m oʊ-/ [1] [2]), also called a proenzyme (/ ˌ p r oʊ ˈ ɛ n z aɪ m / [3] [4]), is an inactive precursor of an enzyme.A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme.
Trypsinogen (/ ˌ t r ɪ p ˈ s ɪ n ə dʒ ə n,-ˌ dʒ ɛ n / [1] [2]) is the precursor form (or zymogen) of trypsin, a digestive enzyme. It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen. It is cleaved to its active form, trypsin, by enteropeptidase, which is found in the ...
Enzyme precursors are called zymogens or proenzymes. Examples are enzymes of the digestive tract in humans. Some protein precursors are secreted from the cell. Many of these are synthesized with an N-terminal signal peptide that targets them for secretion. Like other proteins that contain a signal peptide, their name is prefixed by pre.
Arg 117 is a trypsin-sensitive site which can be cleaved by another trypsin and becomes inactivated. This site may be a fail-safe mechanism by which trypsin, when activated within the pancreas, may become inactivated. Mutation at this cleavage site would result in a loss of control and permit autodigestion, causing pancreatitis. [10]
Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes.
The pancreas is located in the visceral region, and is a major part of the digestive system required for proper digestion and subsequent assimilation of macronutrient substances required for living. Pancreatic juice is alkaline in nature due to the high concentration of bicarbonate ions. Bicarbonate is useful in neutralizing the acidic gastric ...
Protein half-life helps determine the overall rate as this designates the first step in protein catabolism. Depending on whether this step is short or long will influence the rest of the metabolic process. One key component in determining the protein half-life is based on the N-end rule.
It is one of three principal endopeptidases (enzymes cutting proteins in the middle) in the human digestive system, the other two being chymotrypsin and trypsin. There are also exopeptidases which remove individual amino acids at both ends of proteins (carboxypeptidases produced by the pancreas and aminopeptidases secreted by the small intestine).