Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli in soluble form | Saccharolobus solfataricus |
expression in Escherichia coli | Saccharolobus solfataricus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
65000 | - |
gel filtration, monomeric form | Saccharolobus solfataricus |
100393 | - |
1 * 100393, the enzyme possesses two different oligomeric states, calculated from sequence | Saccharolobus solfataricus |
100393 | - |
2 * 100393, the enzyme possesses two different oligomeric states, calculated from sequence | Saccharolobus solfataricus |
140000 | - |
gel filtration, dimeric form | Saccharolobus solfataricus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharolobus solfataricus | P95949 | - |
- |
Saccharolobus solfataricus P2 | P95949 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Saccharolobus solfataricus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | ATP-dependent 3'5' DNA-helicase activity. Both monomeric and dimeric forms of Hel112 possess ATPase activity. In the monomeric state the enzyme is able to bind single-stranded DNA with an affinity lower than the one observed for the fork and 3'-mis DNA. In contrast, Hel112 in the dimeric form binds single-stranded DNA with very low affinity | Saccharolobus solfataricus | ADP + phosphate | - |
? | |
ATP + H2O | only the monomeric enzyme form has an ATP-dependent 3'-5' DNA-helicase activity, whereas, both the monomeric and dimeric forms possess DNA strand-annealing capability. The Hel112 monomeric form is able to unwind forked and 3'-tailed DNA structures with high efficiency, whereas it is almost inactive on blunt-ended duplexes and bubble-containing molecules | Saccharolobus solfataricus | ADP + phosphate | - |
? | |
ATP + H2O | ATP-dependent 3'5' DNA-helicase activity. Both monomeric and dimeric forms of Hel112 possess ATPase activity. In the monomeric state the enzyme is able to bind single-stranded DNA with an affinity lower than the one observed for the fork and 3'-mis DNA. In contrast, Hel112 in the dimeric form binds single-stranded DNA with very low affinity | Saccharolobus solfataricus P2 | ADP + phosphate | - |
? | |
ATP + H2O | only the monomeric enzyme form has an ATP-dependent 3'-5' DNA-helicase activity, whereas, both the monomeric and dimeric forms possess DNA strand-annealing capability. The Hel112 monomeric form is able to unwind forked and 3'-tailed DNA structures with high efficiency, whereas it is almost inactive on blunt-ended duplexes and bubble-containing molecules | Saccharolobus solfataricus P2 | ADP + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 100393, the enzyme possesses two different oligomeric states, calculated from sequence | Saccharolobus solfataricus |
dimer | forms monomers and dimers in solution. Only the monomeric form has an ATP-dependent 3'-5' DNA-helicase activity, whereas, both the monomeric and dimeric forms possess DNA strand-annealing capability | Saccharolobus solfataricus |
monomer | 1 * 100393, the enzyme possesses two different oligomeric states, calculated from sequence | Saccharolobus solfataricus |
monomer | forms monomers and dimers in solution. Only the monomeric form has an ATP-dependent 3'-5' DNA-helicase activity, whereas, both the monomeric and dimeric forms possess DNA strand-annealing capability | Saccharolobus solfataricus |
Synonyms | Comment | Organism |
---|---|---|
Hel112 | - |
Saccharolobus solfataricus |
SSO0112 | locus name | Saccharolobus solfataricus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | - |
assay at | Saccharolobus solfataricus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Saccharolobus solfataricus |