Cloned (Comment) | Organism |
---|---|
- |
Saccharolobus solfataricus |
Protein Variants | Comment | Organism |
---|---|---|
E307A | inactive in DNA unwinding and partially active in the ATPase assay | Saccharolobus solfataricus |
K265A/E307A | completely abolished ATPase activity | Saccharolobus solfataricus |
K265A/R372I | completely abolished ATPase activity | Saccharolobus solfataricus |
R372I | very low levels of ATPase activity and no helicase activity | Saccharolobus solfataricus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
NaCl | above 100 mM | Saccharolobus solfataricus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | the enzyme requires a divalent cation (Mg2+, Mn2+, or Ca2+) for its helicase activity, with Mg2+ being the preferred cofactor. The enzyme exists in solution as a salt-stable dimer and is capable of assembling into a salt-sensitive oligomer that is significantly larger than a hexamer in the presence of a divalent cation (Mg2+) and an adenine nucleotide (ATP, dATP, or ADP) or its analog (ATPgammaS or AMPPNP) | Saccharolobus solfataricus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharolobus solfataricus | - |
- |
- |
Saccharolobus solfataricus P2 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Saccharolobus solfataricus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | the enzyme unwinds double-stranded DNA (dsDNA) in a 3'-to-5' direction in the presence of ATP over a wide range of temperatures, from 37°C to 75°C, and possesses DNA-stimulated ATPase activity. dATP can substitute for ATP to a limited extent, the enzyme is unable to bind ssDNA | Saccharolobus solfataricus | ADP + phosphate | - |
? | |
ATP + H2O | the enzyme unwinds double-stranded DNA (dsDNA) in a 3'-to-5' direction in the presence of ATP over a wide range of temperatures, from 37°C to 75°C, and possesses DNA-stimulated ATPase activity. dATP can substitute for ATP to a limited extent, the enzyme is unable to bind ssDNA | Saccharolobus solfataricus P2 | ADP + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
oligomer | the enzyme exists in solution as a salt-stable dimer and is capable of assembling into a salt-sensitive oligomer that is significantly larger than a hexamer in the presence of a divalent cation (Mg2+) and an adenine nucleotide (ATP, dATP, or ADP) or its analog (ATPgammaS or AMPPNP). Both N-terminal and C-terminal portions of ORF735 (87 and 160 amino acid residues, respectively, in size) are required for protein dimerization but dispensable for the formation of the higher-order oligomer. The protein unwinds DNA only as a large oligomer | Saccharolobus solfataricus |
Synonyms | Comment | Organism |
---|---|---|
ORF735 protein | - |
Saccharolobus solfataricus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | - |
assay at | Saccharolobus solfataricus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Saccharolobus solfataricus |