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Literature summary 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

Activating Compound

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

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.11.5 0.00000013
-
Double-stranded DNA DNA-dependent ATPase activity Escherichia coli
3.1.11.5 0.085
-
ATP DNA-dependent ATPase activity Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.1.11.5 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.11.5 ATP + H2O
-
Escherichia coli ADP + phosphate
-
?
3.1.11.5 ATP + H2O biphasic activity represents DNA unwinding and ATPase activity Escherichia coli ADP + phosphate
-
?
3.1.11.5 double-stranded DNA
-
Escherichia coli intermediates with single stranded regions
-
?
3.1.11.5 double-stranded DNA + H2O ATP-dependent helicase Escherichia coli single-stranded DNA fragments
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.11.5 740
-
ATP DNA-dependent ATPase activity Escherichia coli