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Literature summary for 2.7.11.18 extracted from

  • Hong, F.; Facemyer, K.C.; Carter, M.S.; Jackson, d.e.l..R.; Haldeman, B.D.; Ruana, N.; Sutherland, C.; Walsh, M.P.; Cremo, C.R.; Baker, J.E.
    Kinetics of myosin light chain kinase activation of smooth muscle myosin in an in vitro model system (2013), Biochemistry, 52, 8489-8500.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Calmodulin dependent on Gallus gallus
methylcellulose enhances the rate of MLCK-induced phosphorylation of smooth muscle myosin and MLCK-induced mechanical activation of smooth muscle myosin to move actin filaments Gallus gallus
additional information kinetics of myosin light chain kinase activation of smooth muscle myosin in an in vitro model system, overview. Actin has no activating effect on the enzyme activity Gallus gallus

Protein Variants

Protein Variants Comment Organism
additional information the kinase activity of biotinylated-MLCK is comparable to MLCK without biotinylation using the regulatory light chain as the substrate. Biotinylated-MLCK and biotinylated-MLCK with attached streptavidin tag are able to fully phosphorylate smooth muscle myosin regulatory light chain Gallus gallus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of myosin light chain kinase activation of smooth muscle myosin in an in vitro model system, kinetic modelling, overview. The dissociation of MLCK from phosphorylated smooth muscle myosin is rate-limiting and that the rate of the phosphorylation step is faster than this dissociation rate. Association to smooth muscle myosin is much faster than to smooth muscle myosin. The probability of MLCK interacting with unphosphorylated versus smooth muscle myosin is 55-460 times greater Gallus gallus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ dependent on Gallus gallus
Mg2+ required 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 P11799
-
-

Source Tissue

Source Tissue Comment Organism Textmining
gizzard
-
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
-
?
ATP + [myosin light chain] smooth muscle myosin regulatory light chain phosphorylation at Ser19 Gallus gallus ADP + [myosin light chain] phosphate
-
?
additional information static substrate binding structure of streptavidin-tagged enzyme, overview Gallus gallus ?
-
?

Synonyms

Synonyms Comment Organism
myosin light chain kinase
-
Gallus gallus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Gallus gallus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Gallus gallus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Gallus gallus

General Information

General Information Comment Organism
physiological function MLCK-induced phosphorylation of smooth muscle myosin and MLCK-induced mechanical activation of smooth muscle myosin to move actin filaments, likely by increasing the time the MLCK remains close to the surface-attached myosin Gallus gallus