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Literature summary for 3.4.21.26 extracted from
- Engineering cyclophilin into a proline-specific endopeptidase [published erratum appears in Nature 1998 Jul 16;394(6690):302 (1998), Nature, 391, 301-303.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | using structures of the cyclophilin-peptide complex for engineering a proline-specific endopeptidase activity | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.6 | 2.4 | furylacryloyl-Ala-Pro | - |
Escherichia coli |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| furylacryloyl-Ala-Pro + H2O | - |
Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cyproase I | engineered proline-specific endopeptidase | Escherichia coli |
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