Which enzymes activates trypsin

to directory mode

Area of ‚Äč‚ÄčExpertise - Biochemistry, metabolism

Various proteins, such as the digestive enzymes trypsin and chymotrypsin, plasmin, rennin or urokinase, are synthesized as inactive precursor peptides (zymogens) that are only activated by the proteolytic cleavage of part of the peptide. Linguistically, the precursor form is identified by adding the syllable -ogen (trypsinogen) or the prefix Pro- (prorennin). The activation can take place by a proteolytic enzyme, be autocatalytic as with trypsin or depend on the environment; For example, pepsinogen is split into pepsin by the acidic environment of the stomach. The physiological background of the zymogen activation of digestive enzymes is the protection of the organism from self-digestion. The preliminary stages remain inactive until they have reached their destination.

In blood coagulation, too, the inactive precursors of the coagulation cascade are gradually activated by proteolytic cleavage

See also: blood coagulation cascade

Learning units in which the term is dealt with

Regulation of the enzyme concentration70 min.

biochemistrymetabolismBiocatalysis

Different ways of regulating the enzyme concentration are listed: genetic regulation using the example of the lac operon, catabolite repression and proteolytic cleavage.

Chymotrypsin60 min.

biochemistrymetabolismEnzymes and enzyme classes

The enzyme chymotrypsin is described as a typical example of a serine protease. The module also deals with the zymogen activation of chymotrypsinogen, the reversible inhibition of the enzyme by the chymotrypsin inhibitor and describes the structure of active chymotrypsin and its structural features, i.e. the catalytic triad and the oxyanion hole. A 3D animation of the enzymatic catalysis of chymotrypsin is also included.