Any feedback?
Literature summary for 5.6.2.4 extracted from
- Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism (2005), Nat. Struct. Mol. Biol., 12, 756-762.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Saccharolobus solfataricus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K246A/R247A | indistinguishable from wild-type protein with respect to heat stability. ATPase activity of the mutated protein does not increase in the presence of DNA. Mutation reduces DNA binding | Saccharolobus solfataricus |
| K246A/R247A/K430A | completely inactive as a helicase, ATPase activity of the mutated protein does not increase in the presence of DNA, indistinguishable from wild-type protein with respect to heat stability | Saccharolobus solfataricus |
| K430A | completely inactive as a helicase, ATPase activity of the mutated protein does not increase in the presence of DNA, indistinguishable from wild-type protein with respect to heat stability | Saccharolobus solfataricus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | Q9UXG1 | - |
- |
| Saccharolobus solfataricus P2 | Q9UXG1 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Saccharolobus solfataricus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | ATPase activity of wild-type enzyme is 1.5- to 1.8-fold higher in the presence of DNA. Conformational change in the MCM complex upon binding DNA allows for this increase in the rate of ATP hydrolysis, which is required for rapid unwinding | Saccharolobus solfataricus | ADP + phosphate | - |
? |  |
| ATP + H2O | ATPase activity of wild-type enzyme is 1.5- to 1.8-fold higher in the presence of DNA. Conformational change in the MCM complex upon binding DNA allows for this increase in the rate of ATP hydrolysis, which is required for rapid unwinding | Saccharolobus solfataricus P2 | ADP + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homohexamer | the mini-chromosome maintenance complex binds as a hexamer and slides on the end of a 3'-extended single-stranded DNA tail of a Y-shaped substrate. Binding is oriented so that the motor domain of the protein faces duplex DNA | Saccharolobus solfataricus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MCM complex | - |
Saccharolobus solfataricus |
| mini-chromosome maintenance complex | - |
Saccharolobus solfataricus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 65 | - |
assay at | Saccharolobus solfataricus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Saccharolobus solfataricus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
