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Literature summary for 2.7.11.18 extracted from

  • Gao, Y.; Kawano, K.; Yoshiyama, S.; Kawamichi, H.; Wang, X.; Nakamura, A.; Kohama, K.
    Myosin light chain kinase stimulates smooth muscle myosin ATPase activity by binding to the myosin heads without phosphorylating the myosin light chain (2003), Biochem. Biophys. Res. Commun., 305, 16-21.
    View publication on PubMed
Search for more literature for 2.7.11.18

Cloned(Commentary)

Cloned (Comment) Organism
expression of a C-terminal enzyme fragment comprising residues 860-1176 as GST-fusion protein in Escherichia coli strain Bl21(DE3), the GST-tag slightly reduces the activity of the recombinant enzyme fragment compared to the untagged fragment Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ complex formation with calmodulin Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [myosin light chain] Bos taurus the multifunctional regulatory enzyme stimulates smooth muscle myosin ATPase activity by binding to the myosin heads without phosphorylating the myosin light chain, kinetics, overview ADP + [myosin light chain] phosphate
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 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
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-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged C-terminal enzyme fragment by glutathione affinity chromatography Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
smooth muscle
-
 Bos taurus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [myosin light chain]
-
 Bos taurus ADP + [myosin light chain] phosphate
-
 ?
ATP + [myosin light chain] the multifunctional regulatory enzyme stimulates smooth muscle myosin ATPase activity by binding to the myosin heads without phosphorylating the myosin light chain, kinetics, overview Bos taurus ADP + [myosin light chain] phosphate
-
 ?

Synonyms

Synonyms Comment Organism
MLCK
-
 Bos taurus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Bos taurus
Calmodulin binding site I at residue 1002-1022, binding site II at residues 26-42, complex formation with Ca2+ Bos taurus