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Literature summary for 3.4.25.2 extracted from
- Binding of MG132 or deletion of the Thr active sites in HslV subunits increases the affinity of HslV protease for HslU ATPase and makes this interaction nucleotide-independent (2008), J. Biol. Chem., 283, 33258-33266.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O | the N-terminal Thr active sites of HslV are involved in the communication between HslV and HslU in addition to its role in the catalysis of peptide bond cleavage | Escherichia coli | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| hslVU | - |
Escherichia coli |
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Release 2023.1 (January 2023)
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