EC Number   |
Reaction |
Reference |
|---|
   3.4.22.16 | Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase |
mechanism: interactive catalytic-site system in which the nucleophilic character of the sulphur atom is maintained in acidic media |
638825 |
| 3.4.22.16 | Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase |
mechanism: specific interactions of an anionic active site residue with the charged alpha-amino group of substrates cause transition state stabilization which proves the enzyme to act preferentially as an aminopeptidase |
638837 |
| 3.4.22.16 | Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase |
mini-chain has definitive role in substrate-recognition, implications for enzyme function |
638836 |
| 3.4.22.16 | Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase |
number of possible subsites: three |
638821 |
| 3.4.22.16 | Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase |
same catalytic mechanism as in papain and actinidin |
638842 |
