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Literature summary for 5.6.2.4 extracted from
- Archaeal MCM has separable processivity, substrate choice and helicase domains (2007), Nucleic Acids Res., 35, 988-998.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Saccharolobus solfataricus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | the central AAA+ domain possesses ATPase and helicase activity. The degenerate helix-turn-helix domain at the C-terminus of MCM exerts a negative effect on the helicase activity of the complex. Addition of the N-terminus influences both the processivity of the helicase and the choice of substrate that can be melted by the ATPase domain. The degenerate helix-turn-helix domain at the C-terminus of MCM exerts a negative effect on the helicase activity of the complex. Extensive regulatory inter-domain communication within the MCM complex | Saccharolobus solfataricus | ADP + phosphate | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| mini-chromosome maintenance complex | - |
Saccharolobus solfataricus |
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