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Literature summary for 3.4.22.2 extracted from
- Challenging a paradigm: Theoretical calculations of the protonation state of the Cys25-His159 catalytic diad in free papain (2009), Proteins Struct. Funct. Bioinform., 77, 916-926.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Carica papaya | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1' | the His-Cys catalytic diad in free papain is fully protonated, -NH(+)/-SH. The experimental pKa of 8.62 for His159 imidazole in free papain is assigned to the -NH(+)/-SH and -N/-SH equilibrium | Carica papaya |
a
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