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Literature summary for 3.1.11.5 extracted from

  • Roman, L.J.; Kowalczykowski, S.C.
    Characterization of the adenosinetriphosphatase activity of the Escherichia coli RecBCD enzyme: relationship of ATP hydrolysis to the unwinding of duplex DNA (1989), Biochemistry, 28, 2873-2881.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
NaCl ATP molecules hydrolyzed per base pair unwound slightly increased Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
E. coli single stranded DNA binding protein ATPase activity complete inhibited by SSB Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00000013
-
 Double-stranded DNA DNA-dependent ATPase activity Escherichia coli
0.085
-
 ATP DNA-dependent ATPase activity 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
-
 ?
ATP + H2O biphasic activity represents DNA unwinding and ATPase activity Escherichia coli ADP + phosphate
-
 ?
double-stranded DNA
-
 Escherichia coli intermediates with single stranded regions
-
 ?
double-stranded DNA + H2O ATP-dependent helicase Escherichia coli single-stranded DNA fragments
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
740
-
 ATP DNA-dependent ATPase activity Escherichia coli