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BRENDA support

Literature summary for 5.6.1.8 extracted from

  • Sato, M.K.; Ishihara, T.; Tanaka, H.; Ishijima, A.; Inoue, Y.
    Velocity-dependent actomyosin ATPase cycle revealed by in vitro motility assay with kinetic analysis (2012), Biophys. J., 103, 711-718.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic parameters of the actomyosin interaction and actomyosin ATPase cycle by measurement techniques using small numbers of molecules instead of single-molecule measurement techniques, kinetic modeling, overview Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + myosin bound to actin filament at position n Oryctolagus cuniculus
-
ADP + phosphate + myosin bound to actin filament at position n+1
-
?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + myosin bound to actin filament at position n
-
Oryctolagus cuniculus ADP + phosphate + myosin bound to actin filament at position n+1
-
?

Synonyms

Synonyms Comment Organism
actomyosin ATPase
-
Oryctolagus cuniculus

General Information

General Information Comment Organism
physiological function the actomyosin interaction plays a key role in a number of cellular functions. Mechanism of the actomyosin contractile system Oryctolagus cuniculus