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Literature summary for 5.6.2.4 extracted from

  • Ozsoy, A.Z.; Sekelsky, J.J.; Matson, S.W.
    Biochemical characterization of the small isoform of Drosophila melanogaster RECQ5 helicase (2001), Nucleic Acids Res., 29, 2986-2993.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.4

Inhibitors

Inhibitors Comment Organism Structure
ATPgammaS
-
 Drosophila melanogaster

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.15
-
 ATP pH 8.0, 30°C, in presence of ssDNA Drosophila melanogaster
0.25
-
 dATP pH 8.0, 30°C, in presence of ssDNA Drosophila melanogaster

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
 x * 54000, small isoform of RECQ5 helicase, SDS-PAGE Drosophila melanogaster

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Purification (Commentary)

Purification (Comment) Organism
enzyme recombinantly expressed in Escherichia coli Drosophila melanogaster

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O RECQ5 unwinds duplex DNA with a 3'-5' polarity. Unwinding of longer partial duplex DNA substrates requires a higher protein concentration than does unwinding of the 20bp partial duplex substrate. The unwinding reaction catalyzed by RECQ5 requires a nucleoside 5'-phosphate. dATP is most effective. RECQ5 hydrolyzes dATP more rapidly than ATP regardless of the presence of ssDNA. Both ssDNA cofactors, M13mp18 ssDNA and poly(dT) strongly stimulate the dATPase activity of the protein Drosophila melanogaster ADP + phosphate
-
 ?
CTP + H2O RECQ5 unwinds duplex DNA with a 3'-5' polarity. The unwinding reaction catalyzed RECQ5 requires a nucleoside 5'-phosphate. dATP is most effective. ATP supports helicase reaction with 10% of the efficiency obtained with dATP Drosophila melanogaster CDP + phosphate
-
 ?
dATP + H2O RECQ5 unwinds duplex DNA with a 3'-5' polarity. Unwinding of longer partial duplex DNA substrates requires a higher protein concentration than does unwinding of the 20bp partial duplex substrate. The unwinding reaction catalyzed by RECQ5 requires a nucleoside 5'-phosphate. RECQ5 hydrolyzes dATP more rapidly than ATP regardless of the presence of ssDNA. dATP is most effective. ATP supports helicase reaction with 45% of the efficiency obtained with dATP. Both ssDNA cofactors, M13mp18 ssDNA and poly(dT) strongly stimulate the ATPase activity of the protein Drosophila melanogaster dADP + phosphate
-
 ?
dGTP + H2O RECQ5 unwinds duplex DNA with a 3'-5' polarity. The unwinding reaction catalyzed by RECQ5 requires a nucleoside 5'-phosphate. dATP is most effective. ATP supports helicase reaction with 30% of the efficiency obtained with dATP Drosophila melanogaster dGDP + phosphate
-
 ?
GTP + H2O RECQ5 unwinds duplex DNA with a 3'-5' polarity. The unwinding reaction catalyzed by RECQ5 requires a nucleoside 5'-phosphate. dATP is most effective. ATP supports helicase reaction with 35% of the efficiency obtained with dATP Drosophila melanogaster GDP + phosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 54000, small isoform of RECQ5 helicase, SDS-PAGE Drosophila melanogaster

Synonyms

Synonyms Comment Organism
RECQ5
-
 Drosophila melanogaster
RECQ5 helicase small isoform Drosophila melanogaster

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Drosophila melanogaster

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.043
-
 ATP pH 8.0, 30°C, without ssDNA Drosophila melanogaster
0.25
-
 dATP pH 8.0, 30°C, without ssDNA Drosophila melanogaster
15
-
 ATP pH 8.0, 30°C, in presence of ssDNA Drosophila melanogaster
23
-
 dATP pH 8.0, 30°C, in presence of ssDNA Drosophila melanogaster

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Drosophila melanogaster