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Literature summary extracted from
- Isolation and characterization of a processive DNA helicase from the fission yeast Schizosaccharomyces pombe that translocates in a 5'-to-3' direction (1998), Biochem. J., 334, 377-386.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.6.2.3 | additional information | synthetic RNA poly(U) does not support ATP hydrolysis at all. Unlike DNA helicase I, DNA helicase II is not stimulated by SpRPA or Escherichia coli SSB at low ATP concentrations | Schizosaccharomyces pombe | |
| 5.6.2.3 | poly(dI*C) | weakly supports ATPase activity | Schizosaccharomyces pombe | |
| 5.6.2.3 | Poly(dT) | weakly supports ATPase activity | Schizosaccharomyces pombe |  |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.6.2.3 | NaCl | 57% inhibition at 0.2 M, 81% inhibition at 0.4 M | Schizosaccharomyces pombe | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.6.2.3 | 0.65 | - |
ATP | pH 7.8, 37°C | Schizosaccharomyces pombe | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.6.2.3 | Mg2+ | the enzyme requires MgCl2 for its activity. It is not active in the presence of MnCl2 or CaCl2 (1 mM) | Schizosaccharomyces pombe | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.6.2.3 | 63000 | - |
1 * 63000, SDS-PAGE | Schizosaccharomyces pombe |
| 5.6.2.3 | 65000 | - |
gel filtration, glycerol gradient analysis | Schizosaccharomyces pombe |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.6.2.3 | Schizosaccharomyces pombe | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.6.2.3 | - |
Schizosaccharomyces pombe |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.6.2.3 | ATP + H2O | the enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. The enzyme favours adenosine nucleotides (ATP and dATP) as its energy source, but utilizes to limited extents GTP, CTP, dGTP and dCTP. ATP and dATP support unwinding activity with equal efficiency. GTP, dGTP, CTP, dCTP support unwinding activity to limited extents (5-12% of that with ATP at 1.5 mM). The ATPase activity of DNA helicase II increases proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continues to increase up to the longest time tested (3 h), whereas it ceases to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time is not affected by DNA species used. The enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive | Schizosaccharomyces pombe | ADP + phosphate | - |
? | |
| 5.6.2.3 | CTP + H2O | the enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. The enzyme favours adenosine nucleotides (ATP and dATP) as its energy source, but utilizes to limited extents GTP, CTP, dGTP and dCTP. ATP and dATP support unwinding activity with equal efficiency. GTP, dGTP, CTP, dCTP support unwinding activity to limited extents (5-12% of that with ATP at 1.5 mM). The ATPase activity of DNA helicase II increases proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continues to increase up to the longest time tested (3 h), whereas it ceases to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time is not affected by DNA species used. The enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive | Schizosaccharomyces pombe | CDP + phosphate | - |
? | |
| 5.6.2.3 | dATP + H2O | the enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. The enzyme favours adenosine nucleotides (ATP and dATP) as its energy source, but utilizes to limited extents GTP, CTP, dGTP and dCTP. ATP and dATP support unwinding activity with equal efficiency. GTP, dGTP, CTP, dCTP support unwinding activity to limited extents (5-12% of that with ATP at 1.5 mM). The ATPase activity of DNA helicase II increases proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continues to increase up to the longest time tested (3 h), whereas it ceases to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time is not affected by DNA species used. The enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive | Schizosaccharomyces pombe | dADP + phosphate | - |
? | |
| 5.6.2.3 | dCTP + H2O | the enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. The enzyme favours adenosine nucleotides (ATP and dATP) as its energy source, but utilizes to limited extents GTP, CTP, dGTP and dCTP. ATP and dATP support unwinding activity with equal efficiency. GTP, dGTP, CTP, dCTP support unwinding activity to limited extents (5-12% of that with ATP at 1.5 mM). The ATPase activity of DNA helicase II increases proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continues to increase up to the longest time tested (3 h), whereas it ceases to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time is not affected by DNA species used. The enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive | Schizosaccharomyces pombe | dCDP + phosphate | - |
? | |
| 5.6.2.3 | dGTP + H2O | the enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. The enzyme favours adenosine nucleotides (ATP and dATP) as its energy source, but utilizes to limited extents GTP, CTP, dGTP and dCTP. ATP and dATP support unwinding activity with equal efficiency. GTP, dGTP, CTP, dCTP support unwinding activity to limited extents (5-12% of that with ATP at 1.5 mM). The ATPase activity of DNA helicase II increases proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continues to increase up to the longest time tested (3 h), whereas it ceases to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time is not affected by DNA species used. The enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive | Schizosaccharomyces pombe | dGDP + phosphate | - |
? | |
| 5.6.2.3 | GTP + H2O | the enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. The enzyme favours adenosine nucleotides (ATP and dATP) as its energy source, but utilizes to limited extents GTP, CTP, dGTP and dCTP. ATP and dATP support unwinding activity with equal efficiency. GTP, dGTP, CTP, dCTP support unwinding activity to limited extents (5-12% of that with ATP at 1.5 mM). The ATPase activity of DNA helicase II increases proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continues to increase up to the longest time tested (3 h), whereas it ceases to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time is not affected by DNA species used. The enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive | Schizosaccharomyces pombe | GDP + phosphate | - |
? | |
| 5.6.2.3 | additional information | non-hydrolysable ATP analogues do not support helicase activity. DNA helicase II lacks any detectable RNA-unwinding activity | Schizosaccharomyces pombe | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.6.2.3 | monomer | 1 * 63000, SDS-PAGE | Schizosaccharomyces pombe |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.6.2.3 | DNA helicase II | - |
Schizosaccharomyces pombe |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.6.2.3 | 37 | - |
assay at | Schizosaccharomyces pombe |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.6.2.3 | 7.8 | - |
assay at | Schizosaccharomyces pombe |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.6.2.3 | 6.5 | 8.9 | the enzyme functions efficiently over wide ranges of pH from 6.5 to 8.9 | Schizosaccharomyces pombe |
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