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Literature summary extracted from

  • Hong, F.; Brizendine, R.K.; Carter, M.S.; Alcala, D.B.; Brown, A.E.; Chattin, A.M.; Haldeman, B.D.; Walsh, M.P.; Facemyer, K.C.; Baker, J.E.; Cremo, C.R.
    Diffusion of myosin light chain kinase on actin: A mechanism to enhance myosin phosphorylation rates in smooth muscle (2015), J. Gen. Physiol., 146, 267-280.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.18 Calmodulin dependent on Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.18 gene MYLK, recombinant expression of wild-type and truncated enzyme, the latter comprising the N-terminal 75 residues of MLCK Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.7.11.18 additional information generation of a fragment comprising the N-terminal 75 residues of MLCK Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.11.18 actin cytoskeleton MLCK and the N-terminal 75 residues of MLCK move on actin bundles and stress fibers of smooth muscle cell cytoskeletons by a random one-dimensional diffusion mechanism, modelling, overview. MLCK motion is permitted only if acto–myosin and MLCK–myosin interactions are weak Homo sapiens 15629
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.18 Ca2+ dependent on, activates Homo sapiens
2.7.11.18 Mg2+ required Homo sapiens

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] Homo sapiens smooth muscle myosin II ADP + [myosin light chain] phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.18 Homo sapiens Q15746
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.18 smooth muscle the abundance of active MLCK, which is tightly associated with the contractile apparatus, is low relative to that of smooth muscle myosin Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.18 ATP + [myosin light chain] smooth muscle myosin II Homo sapiens ADP + [myosin light chain] phosphate
-
?
2.7.11.18 additional information MLCK and truncated 1-75 MLCK interaction analysis with actin, overview Homo sapiens ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.18 MLCK
-
Homo sapiens
2.7.11.18 MYLK
-
Homo sapiens
2.7.11.18 myosin light chain kinase
-
Homo sapiens
2.7.11.18 SMM light chain kinase
-
Homo sapiens
2.7.11.18 smooth muscle myosin light chain kinase
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.18 25
-
assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.18 7.4
-
assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.18 ATP
-
Homo sapiens

General Information

EC Number General Information Comment Organism
2.7.11.18 physiological function myosin light chain kinase is required for smooth muscle contraction and regulation of tone in most of the hollow organs of the body. MLCK and the N-terminal 75 residues of MLCK move on actin bundles and stress fibers of smooth muscle cell cytoskeletons by a random one-dimensional diffusion mechanism in a Ca2+/calmodulin- and ATP-dependent manner, modelling, overview. MLCK motion is permitted only if acto-myosin and MLCK-myosin interactions are weak. One-dimensional diffusion of MLCK along actin ensures that diffusion is not rate limiting for phosphorylation, allows MLCK to locate to areas in which myosin is not yet phosphorylated, and allows MLCK to avoid getting stuck on myosins that have already been phosphorylated. Diffusion of MLCK along actin filaments may be an important mechanism for enhancing the rate of smooth muscle myosin phosphorylation in smooth muscle. In the absence of added ATP or Ca2+/calmodulin, the myosin in the stress fibers is dephosphorylated and in a rigor state (no ATP) in which actin and myosin bind strongly Homo sapiens