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Literature summary extracted from

  • Okagaki, T.; Hayakawa, K.; Samizo, K.; Kohama, K.
    Inhibition of the ATP-dependent interaction of actin and myosin by the catalytic domain of the myosin light chain kinase of smooth muscle: possible involvement in smooth muscle relaxation (1999), J. Biochem., 125, 619-626.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.18 Ca2+ Ca2+ in presence of calmodulin abolishes the inhibition of actin-myosin interaction Gallus gallus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.11.18 ATP + myosin light chain Gallus gallus inhibition of actin-myosin ineraction ADP + myosin light chain phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.18 Gallus gallus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.18
-
Gallus gallus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.18 gizzard
-
Gallus gallus
-
2.7.11.18 smooth muscle
-
Gallus gallus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.18 ATP + myosin light chain inhibition of actin-myosin ineraction Gallus gallus ADP + myosin light chain phosphate
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.18 Calmodulin calmodulin in presence of Ca2+ abolishes the inhibition of actin-myosin interaction Gallus gallus