Editing Chymotrypsin (section)

== Activation ==

Chymotrypsin is [[protein biosynthesis|synthesized]] in the pancreas.  Its [[wiktionary:Precursor|precursor]] is [[chymotrypsinogen]]. Trypsin activates chymotrypsinogen by cleaving peptidic bonds in positions Arg15 – Ile16 and produces π-chymotrypsin. In turn, aminic group (-NH3<sup>+</sup>) of the Ile16 residue interacts with the side chain of Asp194, producing the "oxyanion hole" and the hydrophobic "S1 pocket". Moreover, chymotrypsin induces its own activation by cleaving in positions 14–15, 146–147, and 148–149, producing α-chymotrypsin (which is more active and stable than π-chymotrypsin).<ref>{{cite book |last1=Phillips |first1=Jo |title=Fundamentals of Enzymology |date=2019 |publisher=EDTECH |isbn=9781839471605 |page=117}}</ref> The resulting molecule is a three-[[peptide|polypeptide]] molecule interconnected via [[disulfide bond]]s.