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Literature summary for 5.6.2.3 extracted from

  • Lee, C.; Seo, Y.S.
    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.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.3

Activating Compound

Activating Compound Comment Organism Structure
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
poly(dI*C) weakly supports ATPase activity Schizosaccharomyces pombe
Poly(dT) weakly supports ATPase activity Schizosaccharomyces pombe

Inhibitors

Inhibitors Comment Organism Structure
NaCl 57% inhibition at 0.2 M, 81% inhibition at 0.4 M Schizosaccharomyces pombe

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.65
-
 ATP pH 7.8, 37°C Schizosaccharomyces pombe

Metals/Ions

Metals/Ions Comment Organism Structure
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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
63000
-
 1 * 63000, SDS-PAGE Schizosaccharomyces pombe
65000
-
 gel filtration, glycerol gradient analysis Schizosaccharomyces pombe

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Schizosaccharomyces pombe

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
additional information non-hydrolysable ATP analogues do not support helicase activity. DNA helicase II lacks any detectable RNA-unwinding activity Schizosaccharomyces pombe ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 63000, SDS-PAGE Schizosaccharomyces pombe

Synonyms

Synonyms Comment Organism
DNA helicase II
-
 Schizosaccharomyces pombe

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Schizosaccharomyces pombe

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
 assay at Schizosaccharomyces pombe

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.9 the enzyme functions efficiently over wide ranges of pH from 6.5 to 8.9 Schizosaccharomyces pombe