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Literature summary extracted from
- Thiol proteases: comparative studies on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain (1985), J. Mol. Biol., 182, 317-329.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.22.16 | comparison of structure and primary sequences of 5 papain, actinidin, cathepsins B and H and stem bromelain yields high degree of similarity | Homo sapiens |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.22.16 | Homo sapiens | - |
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- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 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 | Homo sapiens |
aSubunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.22.16 | More | amino acid sequence | Homo sapiens |
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Release 2023.1 (January 2023)
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