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Literature summary for 5.6.2.4 extracted from

  • De Felice, M.; Aria, V.; Esposito, L.; De Falco, M.; Pucci, B.; Rossi, M.; Pisani, F.M.
    A novel DNA helicase with strand-annealing activity from the crenarchaeon Sulfolobus solfataricus (2007), Biochem. J., 408, 87-95.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.4

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli in soluble form Saccharolobus solfataricus
expression in Escherichia coli Saccharolobus solfataricus

Molecular Weight [Da]

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

Organism UniProt Comment Textmining
Saccharolobus solfataricus P95949
-
-
Saccharolobus solfataricus P2 P95949
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

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

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

Synonyms Comment Organism
Hel112
-
 Saccharolobus solfataricus
SSO0112 locus name Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 assay at Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Saccharolobus solfataricus