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Literature summary for 5.6.2.3 extracted from

  • Hughes, P.; Baldacci, G.
    A DNA helicase purified by replication protein A (RPA) affinity chromatography from mouse FM3A cells (1997), Nucleic Acids Res., 25, 3881-3888 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information weak stimulation is observed in the presence of Escherichia coli single strand DNA binding protein Mus musculus
NaCl low concentrations of NaCl (50 mM) stimulate the ATPase activity of the enzyme Mus musculus
replication protein A helicase activity is strongly stimulated by RPA on DNA substrates containing duplex regions longer than 18 bp Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
ADP at a concentration of 2 mM ATP, DNA helicase activity is inhibited 30% by 2 mM ADP Mus musculus
ATPgammaS at a concentration of 2 mM ATP, DNA helicase activity is inhibited 38 and 73% by 0.2 and 2 mM ATPgammaS, respectively Mus musculus
additional information p[NH]ppA is not inhibitory even at 2 mM Mus musculus
N-ethylmaleimide
-
Mus musculus
NaCl the helicase activity of the enzyme is mildly inhibited by increased salt concentrations of 50 and 100 mM NaCl Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ absolute requirement for Mg2+, 7 mM used in assay conditions Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
phosphocellulose column chromatography, Affi-gel 10-RPA affinity column chromatography, and heparin-Sepharose column chromatography Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
FM3A cell
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
32P-labeled partial duplex DNA bound to nitrocellulose membranes the enzyme unwinds DNA in the 5'-3' direction in relation to the strand to which it binds and has an absolute necessity for single-stranded regions of DNA for the ATPase activity Mus musculus ?
-
?

Subunits

Subunits Comment Organism
? x * 28000 + x * 21000, SDS-PAGE Mus musculus

Cofactor

Cofactor Comment Organism Structure
ATP the DNA helicase displays an identical Km value of 0.6 mM for the hydrolysis of both ATP and dATP Mus musculus
dATP the DNA helicase displays an identical Km value of 0.6 mM for the hydrolysis of both ATP and dATP Mus musculus