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Literature summary for 2.7.11.18 extracted from

  • Nakamura, A.; Xie, C.; Zhang, Y.; Gao, Y.; Wang, H.H.; Ye, L.H.; Kishi, H.; Okagaki, T.; Yoshiyama, S.; Hayakawa, K.; Ishikawa, R.; Kohama, K.
    Role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, a review dedicated to Dr. Setsuro Ebashi (2008), Biochem. Biophys. Res. Commun., 369, 135-143.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Calmodulin dependent on, antagonizes the binding to actin Gallus gallus
Calmodulin dependent on, antagonizes the binding to actin, residues 26-41 of MLCK act as a CaM-binding region that regulates the binding of MLCK to actin, Ca/CaM is also binds at the Ala796-Ser815 sequence to regulate the kinase activity MLCK Bos taurus
additional information oxytoxin and phorbol ester do not affect the enzyme activity Gallus gallus

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis Gallus gallus
expression of wild-type full-length MLCK and of several enzyme fragments in Escherichia coli with the use of a cold-shock promoter Bos taurus

Protein Variants

Protein Variants Comment Organism
additional information downregulation of MLCK in cultured smooth muscle cells reveals that MLC20 phosphorylation is not obligatory for the smooth muscle to contract, overview Gallus gallus

Inhibitors

Inhibitors Comment Organism Structure
additional information non-kinase, inhibitory activity of N-terminal, actin-binding domain of MLCK Bos taurus
additional information oxytoxin and phorbol ester do not affect the enzyme activity. Non-kinase, inhibitory activity of N-terminal, actin-binding domain of MLCK Gallus gallus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ dependent on, antagonizes the binding to actin Gallus gallus
Ca2+ dependent on, antagonizes the binding to actin, Ca/CaM binds at the Ala796-Ser815 sequence to regulate the kinase activity MLCK Bos taurus
Mg2+
-
Gallus gallus
Mg2+
-
Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
155000
-
-
Bos taurus

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
-
?
ATP + myosin light chain Bos taurus
-
ADP + myosin light chain phosphate
-
?
additional information Bos taurus actin-myosin interaction of smooth muscle could be activated by the non-kinase activity of MLCK, a mechanism that is quite independent of MLC20 phosphorylation, role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, overview ?
-
?
additional information Gallus gallus actin-myosin interaction of smooth muscle could be activated by the non-kinase activity of MLCK, a mechanism that is quite independent of MLC20 phosphorylation, role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, overview. MLCK phosphorylated at Ser828 stimulates the ATPase activity of unphosphorylated myosin more effectively than the control MLCK ?
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Gallus gallus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein protein kinase A phosphorylates MLCK in its regulatory domain at Ser1021 and Ser1034. The kinase activity of MLCK phosphorylated at Ser1021 is reduced, whereas that of MLCK phosphorylated at Ser1034 is not reduced Bos taurus
phosphoprotein protein kinase A phosphorylates MLCK in its regulatory domain at Ser815 and Ser828. The kinase activity of MLCK phosphorylated at Ser815 is reduced, whereas that of MLCK phosphorylated at Ser828 is not reduced Gallus gallus

Purification (Commentary)

Purification (Comment) Organism
native enzyme from gizzard muscle Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
cardiac muscle
-
Gallus gallus
-
cardiac muscle
-
Bos taurus
-
skeletal muscle
-
Gallus gallus
-
skeletal muscle
-
Bos taurus
-
smooth muscle from gizzard Gallus gallus
-
smooth muscle from stomach Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + myosin light chain
-
Gallus gallus ADP + myosin light chain phosphate
-
?
ATP + myosin light chain
-
Bos taurus ADP + myosin light chain phosphate
-
?
ATP + myosin light chain the enzyme has effects on the actin-myosin interaction in vitro, binding of full-length and fragmented enzyme, overview. The Asp-Phe-Arg-X-X-Leu motif plays a major role in the binding of MLCK to myofibrils. Regulation of actin–myosin interaction by MLCK through its non-kinase activity, overview Bos taurus ADP + myosin light chain phosphate
-
?
ATP + myosin light chain the enzyme has effects on the actin-myosin interaction in vitro, regulation of actin-myosin interaction by MLCK through its non-kinase activity, overview Gallus gallus ADP + myosin light chain phosphate
-
?
additional information actin-myosin interaction of smooth muscle could be activated by the non-kinase activity of MLCK, a mechanism that is quite independent of MLC20 phosphorylation, role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, overview Bos taurus ?
-
?
additional information actin-myosin interaction of smooth muscle could be activated by the non-kinase activity of MLCK, a mechanism that is quite independent of MLC20 phosphorylation, role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, overview. MLCK phosphorylated at Ser828 stimulates the ATPase activity of unphosphorylated myosin more effectively than the control MLCK Gallus gallus ?
-
?

Subunits

Subunits Comment Organism
More MLCK domain structure, a fusion protein consisting of the N-terminal actin-binding domain, the central catalytic domain, and the C-terminal myosin-binding domain Bos taurus
More MLCK domain structure, a fusion protein consisting of the Nterminal actin-binding domain, the central catalytic domain, and the C-terminal myosin-binding domain Gallus gallus

Synonyms

Synonyms Comment Organism
MLCK
-
Gallus gallus
MLCK
-
Bos taurus
myosin light chain kinase
-
Gallus gallus
myosin light chain kinase
-
Bos taurus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Gallus gallus
ATP ATP-binding motif X-Gly-X-Gly-X-XGly-X Bos taurus