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Literature summary for 3.4.21.92 extracted from
- The ClpXP protease unfolds substrates using a constant rate of pulling but different gears (2013), Cell, 155, X636-X646.
No PubMed abstract available
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | phosphate release is the force-generating step of the ATPase cycle. Protease ClpXP translocates substrate polypeptides by highly coordinated conformational changes in up to four ATPase subunits. To unfold stable substrates like GFP, ClpXP must use this maximum successive firing capacity. The dwell duration between individual bursts of translocation is constant and governed by an internal clock, regardless of the number of translocating subunits | Escherichia coli | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ClpXP | - |
Escherichia coli |
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Release 2023.1 (January 2023)
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