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Literature summary for 3.4.21.53 extracted from
- Transient kinetic experiments demonstrate the existence of a unique catalytic enzyme form in the peptide-stimulated ATPase mechanism of Escherichia coli Lon protease (2006), Biochemistry, 45, 11432-11443.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | high-affinity site of lon can be blocked with unlabeled nucleotide, conformational change associated with nucleotide binding | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| YRGITCSGRQK(benzoic acid amide) + H2O | - |
Escherichia coli | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| lon | - |
Escherichia coli |
| lon protease | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | low-affinity and high-affinity ATP sites | Escherichia coli | |
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Release 2023.1 (January 2023)
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