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Information on EC 2.7.11.18 - myosin-light-chain kinase and Organism(s) Bos taurus and UniProt Accession Q28824

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IUBMB Comments
Requires Ca2+ and calmodulin for activity. The 20-kDa light chain from smooth muscle myosin is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors, but more slowly.
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Bos taurus
UNIPROT: Q28824
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The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mlck, myosin light chain kinase, myosin light-chain kinase, mlc kinase, smooth muscle myosin light chain kinase, smmlck, nmmlck, myosin kinase, cmlck, skmlck, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
myosin light chain kinase, smooth muscle
-
myosin light-chain kinase
-
calcium/calmodulin-dependent myosin light chain kinase
-
-
-
-
kinase, myosin light-chain (phosphorylating)
-
-
-
-
myosin kinase
-
-
-
-
myosin light chain kinase
-
-
myosin light chain protein kinase
-
-
-
-
myosin light-chain kinase
smooth-muscle-myosin-light-chain kinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:[myosin light chain] O-phosphotransferase
Requires Ca2+ and calmodulin for activity. The 20-kDa light chain from smooth muscle myosin is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
51845-53-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + myosin light chain
ADP + myosin light chain phosphate
show the reaction diagram
20 kDa regulatory light chain of smooth muscle
-
-
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
show the reaction diagram
-
-
-
?
ATP + kemptamide
ADP + ?
show the reaction diagram
-
-
-
-
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
show the reaction diagram
ATP + myosin light chain
ADP + myosin light chain phosphate
show the reaction diagram
ATP + myosin-II regulatory light chain
ADP + myosin-II regulatory light chain phosphate
show the reaction diagram
-
-
-
-
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + myosin light chain
ADP + phosphorylated myosin light chain
show the reaction diagram
-
-
-
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
show the reaction diagram
-
causes endothelial contraction
-
-
?
ATP + myosin light chain
ADP + myosin light chain phosphate
show the reaction diagram
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
show the reaction diagram
-
the multifunctional regulatory enzyme stimulates smooth muscle myosin ATPase activity by binding to the myosin heads without phosphorylating the myosin light chain, kinetics, overview
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
-
Calmodulin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
at higher free concentrations, 0.4-3 mM, independent of Mg2+ or pH-value
Calmodulin-binding protein from bovine cardiac muscle
-
-
-
cAMP-dependent protein kinase
-
phosphorylates light chain myosin kinase leading to decreased affinity from calmodulin
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Increasing ionic strength
-
-
-
kaempferol
-
i.e. 3,5,7-trihydroxy-2-(4-hydroxyphenyl)-1-benzopyran-4-one, IC50: 0.00045 mM
ML-7
-
-
naphthalene sulfonamide derivatives
-
-
-
phosphorylation
-
Trifluoperazine
-
-
additional information
-
non-kinase, inhibitory activity of N-terminal, actin-binding domain of MLCK
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
phosphorylation
-
activation, smooth muscle enzyme, not bovine cardiac enzyme
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.075 - 0.22
ATP
0.000002
Calmodulin
-
30°C, pH 6.8
0.11
kemptamide
-
30°C, pH 6.8
0.005 - 0.02
myosin light chain
0.02 - 0.027
turkey gizzard myosin light chain
additional information
additional information
-
kinetic constants for enzymes from various sources with different myosin light chains as substrates
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00045
kaempferol
Bos taurus
-
i.e. 3,5,7-trihydroxy-2-(4-hydroxyphenyl)-1-benzopyran-4-one, IC50: 0.00045 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18.5
-
-
2.51
-
myosin light chain, in native myosin
8.1 - 8.9
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.1
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8.8
-
about half-maximal activity at pH 6.8 and about 75% of maximal activity at pH 8.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
a SV40-infected endothelial cell line
Manually annotated by BRENDA team
-
not rat
Manually annotated by BRENDA team
-
not rat
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
-
myosin light chain kinases in smooth muscle and non-muscle tissues are the same protein
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
F-actin-associated along cellular stress fibres
Manually annotated by BRENDA team
-
associated
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
myosin light chain kinase mediates transcellular intravasation of breast cancer cells through the underlying endothelial cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MYLK_BOVIN
1176
0
128825
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
127000
-
sucrose density gradient centrifugation
150000
-
gel filtration and sedimentation studies
152000
-
x * 152000, SDS-PAGE
155000
160000
-
x * 160000, SDS-PAGE
214000
-
x * 214000, SDS-PAGE, from endothelium
85000
-
gel filtration
94000
-
x * 94000, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
30-60 min, about 50% loss of activity
640621
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol and Tween 40 stabilize
-
protease inhibitors with broad specificity and glycerol stabilize during initial purification, unstable to further purification
-
repeated freeze-thawing decreases activity
-
unstable upon lyophilization
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
calmodulin-Sepharose column chromatography, DEAE 650M Toyopearl column chromatography, and Superose 6 gel filtration
purified to homogeneity from a number of vertebrate muscles and partially purified from non-muscle tissues
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recombinant GST-tagged C-terminal enzyme fragment by glutathione affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
isolation of cDNA
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
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expression of wild-type full-length MLCK and of several enzyme fragments in Escherichia coli with the use of a cold-shock promoter
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
breast cancer cells transiently activate endothelial MLCK at tumor invasion sites
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gallagher, P.J.; Herring, B.P.; Griffin, S.A.; Stull, J.T.
Molecular characterization of a mammalian smooth muscle myosin light chain kinase [published erratum appears in J Biol Chem 1992 May 5;267(13):9450]
J. Biol. Chem.
266
23936-23944
1991
Bos taurus, Gallus gallus, Oryctolagus cuniculus, Oryctolagus cuniculus (P29294), Rattus norvegicus
Manually annotated by BRENDA team
Garcia, J.G.N.; Lazar, V.; Gilbert-McClain, L.I.; Gallagher, P.J.; Verin, A.D.
Myosin light chain kinase in endothelium: molecular cloning and regulation
Am. J. Respir. Cell Mol. Biol.
16
489-494
1997
Bos taurus, Homo sapiens, Homo sapiens (Q15746)
Manually annotated by BRENDA team
Kobayashi, H.; Inoue, A.; Mikawa, T.; Kuwayama, H.; Hotta, Y.; Masaki, T.; Ebashi, S.
Isolation of cDNA for bovine stomach 155 kDa protein exhibiting myosin light chain kinase activity
J. Biochem.
112
786-791
1992
Bos taurus (Q28824), Bos taurus
Manually annotated by BRENDA team
Serventi, I.M.; Coffee, C.J.
Characterization of myosin light-chain kinase from bovine adrenal medulla
Arch. Biochem. Biophys.
245
379-388
1986
Bos taurus
Manually annotated by BRENDA team
Walsh, M.P.; Hinkins, S.; Flink, I.L.; Hartshorne, D.J.
Bovine stomach myosin light chain kinase: purification, characterization, and comparison with the turkey gizzard enzyme
Biochemistry
21
6890-6896
1982
Bos taurus, Gallus gallus, Meleagris gallopavo
Manually annotated by BRENDA team
Walsh, M.P.; Vallet, B.; Autric, F.; Demaille, J.G.
Purification and characterization of bovine cardiac calmodulin-dependent myosin light chain kinase
J. Biol. Chem.
254
12136-12144
1979
Bos taurus
Manually annotated by BRENDA team
Wolf, H.; Hofmann, F.
Purification of myosin light chain kinase from bovine cardiac muscle
Proc. Natl. Acad. Sci. USA
77
5852-5855
1980
Bos taurus
Manually annotated by BRENDA team
Bartelt, D.C.; Moroney, S.; Wolff, D.J.
Purification, characterization and substrate specificity of calmodulin-dependent myosin light-chain kinase from bovine brain
Biochem. J.
247
747-756
1987
Bos taurus
Manually annotated by BRENDA team
Yamazaki, K.; Itoh, K.; Sobue, K.; Mori, T.; Shibata, N.
Purification of caldesmon and myosin light chain (MLC) kinase from arterial smooth muscle: comparisons with gizzard caldesmon and MLC kinase
J. Biochem.
101
1-9
1987
Bos taurus, Gallus gallus
Manually annotated by BRENDA team
Rogers, J.C.; Williams, D.L.
Kaempferol inhibits myosin light chain kinase
Biochem. Biophys. Res. Commun.
164
419-425
1989
Bos taurus
Manually annotated by BRENDA team
Conti, M.A.; Adelstein, R.S.
Purification and properties of myosin light chain kinases
Methods Enzymol.
196
34-47
1991
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Meleagris gallopavo, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Bailin, G.
Structure and function of a calmodulin-dependent smooth muscle myosin light chain kinase
Experientia
40
1185-1188
1984
Bos taurus, Gallus gallus, Oryctolagus cuniculus, Meleagris gallopavo
Manually annotated by BRENDA team
Stull, J.T.; Nunnally, M.H.; Michnoff, C.H in
Calmoduline-dependent protein kinases
The Enzymes, 3rd. Ed. (Boyer, P. D. , Krebs, E. G. , eds. )
17
113-166
1986
Bos taurus, Canis lupus familiaris, Cavia porcellus, Gallus gallus, Homo sapiens, Meleagris gallopavo, Rattus norvegicus
-
Manually annotated by BRENDA team
Verin, A.D.; Gilbert-McClain, L.I.; Patterson, C.E.; Garcia, J.G.N.
Biochemical regulation of the nonmuscle myosin light chain kinase isoform in bovine endothelium
Am. J. Respir. Cell Mol. Biol.
19
767-776
1998
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
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
Biochem. Biophys. Res. Commun.
305
16-21
2003
Bos taurus
Manually annotated by BRENDA team
Behling-Kelly, E.; McClenahan, D.; Kim, K.S.; Czuprynski, C.J.
Viable "Haemophilus somnus" induces myosin light-chain kinase-dependent decrease in brain endothelial cell monolayer resistance
Infect. Immun.
75
4572-4581
2007
Bos taurus
Manually annotated by BRENDA team
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
Biochem. Biophys. Res. Commun.
369
135-143
2008
Bos taurus, Gallus gallus
Manually annotated by BRENDA team
Xie, C.; Zhang, Y.; Wang, H.H.; Matsumoto, A.; Nakamura, A.; Ishikawa, R.; Yoshiyama, S.; Hayakawa, K.; Kohama, K.; Gao, Y.
Calcium regulation of non-kinase and kinase activities of recombinant myosin light-chain kinase and its mutants
IUBMB Life
61
1092-1098
2009
Gallus gallus, Bos taurus (Q28824)
Manually annotated by BRENDA team
Khuon, S.; Liang, L.; Dettman, R.W.; Sporn, P.H.; Wysolmerski, R.B.; Chew, T.L.
Myosin light chain kinase mediates transcellular intravasation of breast cancer cells through the underlying endothelial cells: a three-dimensional FRET study
J. Cell Sci.
123
431-440
2010
Bos taurus
Manually annotated by BRENDA team