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Literature summary for 3.4.21.103 extracted from
- The P1 and P1 residue specificities of physarolisin I, a serine-carboxyl peptidase from the true slime mold Physarum polycephalum (2009), Biosci. Biotechnol. Biochem., 73, 1168-1171.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Physarum polycephalum | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | in the combinatorial chromogenic peptide Lys-Pro-X-Glu-P1*Nph-X-Leu, the enzyme prefers specifically Nle (100%), Asp (86%), Leu (84%), Glu (78%), and Ala (66%) in decreasing order of relative activity at the P1 position and the rate varies over 100fold between the most preferred Nle (100%) and the least preferred Pro (0.7%) | Physarum polycephalum | ? | - |
? |  |
| additional information | small hydrophobic residues are preferred at the P1' position, Ile for the P3 position and/or Gln in the P2' position are not optimal for the enzyme | Physarum polycephalum | ? | - |
? | |
| oxidized insulin B chain + H2O | the major cleavage sites are Gly8-Ser9, Leu11-Val12, Cys19-Gly20, Gly20-Glu21, and Phe24-Phe25 | Physarum polycephalum | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| physarolisin I | formerly called physaropepsin | Physarum polycephalum |
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