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Literature summary for 3.4.25.2 extracted from
- Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY (1996), FEBS Lett., 398, 274-278.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 220000 | - |
gel filtration | Escherichia coli |
| 220000 | - |
ClpQ in presence of ATP | 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. |
|---|---|---|---|---|---|---|
| casein + H2O | - |
Escherichia coli | ? | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the subunits of ClpY and ClpQ are arranged in hexagonal rings. The structure of ClpQ is a double hexameric ring | Escherichia coli |
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