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Literature summary for 2.7.11.18 extracted from

  • Leachman, S.A.; Gallagher, P.J.; Herring, B.P.; McPhaul, M.J.; Stull, J.T.
    Biochemical properties of chimeric skeletal and smooth muscle myosin light chain kinases (1992), J. Biol. Chem., 267, 4930-4938.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.18

Cloned(Commentary)

Cloned (Comment) Organism
skeletal muscle enzyme Gallus gallus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
 Gallus gallus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + myosin light chain Gallus gallus
-
 ADP + myosin light chain phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Gallus gallus
-
smooth muscle
-
 Gallus gallus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + myosin light chain
-
 Gallus gallus ADP + myosin light chain phosphate
-
 ?

Subunits

Subunits Comment Organism
More skeletal muscle myosin light chain kinases from different species share more identity than skeletal muscle and smooth muscle myosin light chain kinases from the same species Gallus gallus

Cofactor

Cofactor Comment Organism Structure
Calmodulin requirement Gallus gallus
Calmodulin trypsin or chymotrypsin digested smooth muscle enzyme is independent of Ca2+/calmodulin Gallus gallus