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Literature summary for 3.4.21.53 extracted from
- Kinetic characterization of the peptidase activity of Escherichia coli lon reveals the mechanistic similarities in ATP-dependent hydrolysis of peptide and protein substrates (2002), Biochemistry, 41, 9418-9425.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| fluorogenic peptide S3 + H2O | - |
Escherichia coli | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| lon | - |
Escherichia coli |
| lon protease | - |
Escherichia coli |
| Protease La | - |
Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 7.7 | - |
fluorogenic peptide S3 | pH 7.2, 37°C | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | physiological activator | Escherichia coli | |
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Release 2023.1 (January 2023)
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