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Literature summary extracted from
- On the specificity of streptococcal proteinase (1966), J. Biol. Chem., 241, 3331-3339.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.22.10 | Nalpha-benzyloxycarbonyl-Phe-Phe | strong inhibition of hydrolysis of Nalpha-benzyloxycarbonyl-Phe-Tyr | Streptococcus sp. |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.22.10 | Streptococcus sp. | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.22.10 | insulin + H2O | reduced carboxymethylated phenylalanine chain, one of the most rapidly hydrolyzed Phe-Tyr linkages is in the Phe-Phe-Tyr sequence | Streptococcus sp. | ? | - |
? | |
| 3.4.22.10 | Nalpha-benzyloxycarbonyl-Phe-Phe + H2O | - |
Streptococcus sp. | ? | - |
? | |
| 3.4.22.10 | Nalpha-benzyloxycarbonyl-Phe-Tyr + H2O | - |
Streptococcus sp. | ? | - |
? | |
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Release 2023.1 (January 2023)
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