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Literature summary extracted from

  • Okagaki, T.; Ye, L.H.; Samizo, K.; Tanaka, T.; Kohama, K.
    Inhibitory effect of the catalytic domain of myosin light chain kinase on actin-myosin interaction: insight into the mode of inhibition (1999), J. Biochem., 125, 1055-1060.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.18 additional information inhibition by autophosphorylation Gallus gallus

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