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Literature summary for 3.1.11.5 extracted from

  • Roman, L.J.; Kowalczykowski, S.C.
    Characterization of the helicase activity of the Escherichia coli RecBCD enzyme using a novel helicase assay (1989), Biochemistry, 28, 2863-2873.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
NaCl inhibitory to helicase activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0000006
-
Double-stranded DNA unwinding activity Escherichia coli
0.13
-
ATP unwinding activity Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ inhibitory on helicase activity in the presence of Mg2+ Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Escherichia coli
-
ADP + phosphate
-
?
double-stranded DNA + H2O Escherichia coli ATP-dependent helicase single-stranded DNA fragments
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Escherichia coli ADP + phosphate
-
?
double-stranded DNA unwinding in the presence of E. coli binding protein SSB or high levels of ATP Escherichia coli intermediates with single stranded regions
-
?
double-stranded DNA no unwinding on replicative form DNA Escherichia coli intermediates with single stranded regions
-
?
double-stranded DNA + H2O ATP-dependent helicase Escherichia coli single-stranded DNA fragments
-
?

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 37 15000 base pairs of DNA per min at 25°C Escherichia coli
25 37 55800 base pairs of DNA per min at 37°C Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
250
-
ATP DNA-unwinding activity Escherichia coli