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Literature summary for 5.6.1.8 extracted from

  • Kulikova, N.; Pronina, O.E.; Dabrowska, R.; Borovikov, Y.S.
    Caldesmon restricts the movement of both C- and N-termini of tropomyosin on F-actin in ghost fibers during the actomyosin ATPase cycle (2006), Biochem. Biophys. Res. Commun., 345, 280-286.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
caldesmon caldesmon molecules are located along the thin filament and inhibit in vitro the actomyosin ATPase activity Oryctolagus cuniculus
tropomyosin tropomyosin together with troponin inhibits the actomyosin ATPase activity in vitro Oryctolagus cuniculus
Troponin troponin together with tropomyosin inhibits the actomyosin ATPase activity in vitro 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
-
ir

Organism

Organism UniProt Comment Textmining
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
-
ir

Synonyms

Synonyms Comment Organism
actomyosin ATPase
-
Oryctolagus cuniculus
myosin ATPase
-
Oryctolagus cuniculus