Penicillopepsin
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Penicillopepsin (, ''peptidase A'', ''Penicillium janthinellum aspartic proteinase'', ''acid protease A'', ''Penicillium citrinum acid proteinase'', ''Penicillium cyclopium acid proteinase'', ''Penicillium expansum acid proteinase'', ''Penicillium janthinellum acid proteinase'', ''Penicillium expansum aspartic proteinase'', ''Penicillium aspartic proteinase'', ''Penicillium caseicolum aspartic proteinase'', ''Penicillium roqueforti acid proteinase'', ''Penicillium duponti aspartic proteinase'', ''Penicillium citrinum aspartic proteinase'') is an enzyme. This enzyme catalyses the following chemical reaction : Hydrolysis of proteins with broad specificity similar to that of
pepsin A Pepsin A (, ''pepsin'', ''lactated pepsin'', ''pepsin fortior'', ''fundus-pepsin'', ''elixir lactate of pepsin'', ''P I'', ''lactated pepsin elixir'', ''P II'', ''pepsin R'', ''pepsin D'') is an enzyme. This enzyme catalyses the following chemical ...
, preferring hydrophobic residues at P1 and P1', but also cleaving Gly20-Glu in the B chain of
insulin Insulin (, from Latin ''insula'', 'island') is a peptide hormone produced by beta cells of the pancreatic islets encoded in humans by the ''INS'' gene. It is considered to be the main anabolic hormone of the body. It regulates the metabolism o ...
. Clots milk, and activates trypsinogen This enzyme is present in fungus '' Penicillium janthinellum''.


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* {{Portal bar, Biology, border=no EC 3.4.23