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Information on EC 2.7.11.18 - myosin-light-chain kinase and Organism(s) Oryctolagus cuniculus and UniProt Accession P07313

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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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Oryctolagus cuniculus
UNIPROT: P07313
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The taxonomic range for the selected organisms is: Oryctolagus cuniculus
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
DNA-dependent protein kinase catalytic subunit
-
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 kinase, smooth muscle
-
myosin light chain protein kinase
-
-
-
-
myosin light-chain kinase
-
-
-
-
non-muscle myosin light chain kinase
-
-
short myosin light chain kinase
-
-
smooth-muscle-myosin-light-chain kinase
-
-
-
-
additional information
-
cf. EC 2.7.11.17
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 + phosphorylated myosin light chain
show the reaction diagram
ATP + BpaKKRAARATSNVFA
ADP + ?
show the reaction diagram
-
Bpa is the photoreactive amino acid p-benzoylphenylalanine
-
-
?
ATP + KKRAARATSNVFA
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 light chain
ADP + phosphorylated myosin light chain
show the reaction diagram
-
-
-
?
ATP + myosin regulatory light chain
?
show the reaction diagram
-
-
-
-
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
show the reaction diagram
ATP + [rabbit white skeletal muscle myosin P-light chain]
ADP + [rabbit white skeletal muscle myosin P-light chain] phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme binds to thin filaments with high affinity, myofilament binding by Ig-like modules is blocked by disassembling of the filaments, overview
-
-
?
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
ATP + myosin light chain
ADP + myosin light chain phosphate
show the reaction diagram
ATP + myosin light chain
ADP + phosphorylated myosin light chain
show the reaction diagram
-
-
-
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
show the reaction diagram
additional information
?
-
-
the enzyme binds to thin filaments with high affinity, myofilament binding by Ig-like modules is blocked by disassembling of the filaments, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
free form, strong, not in the presence of excess Mg2+
Increasing ionic strength
-
up to 0.4 M NaCl, weak
-
naphthalene sulfonamide derivatives
-
-
-
phosphate
-
up to 0.1 M, weak
phosphorylation
-
Trifluoperazine
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
-
a calmodulin-sensitive MLCK isozyme
F-actin
-
binding via the DFRXXL motifs in the N-terminal region of isozymes S-MLCK and L-MLCK, the latter also uses the six Ig-like modules in its N-terminal extension for binding, the first two of which are minimally required for microfilament binding, overview
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0075
BpaKKRAARATSNVFA
-
25°C, pH 7, Bpa is the photoreactive amino acid p-benzoylphenylalanine
0.05 - 0.063
isolated myosin light chain
-
25°C, pH 7.6
0.0084
KKRAARATSNVFA
-
25°C, pH 7
0.005 - 0.019
myosin light chain
0.0067 - 0.014
myosin regulatory light chain
-
0.1 - 0.2
[rabbit white skeletal muscle myosin P-light chain]
-
27°C, pH 7.6
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16 - 88
myosin light chain
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13
-
BpaKKRAARATSNVFA as substrate
19.9
-
KKRAARATSNVFA as substrate
24
-
skeletal muscle
additional information
-
1280 pmol/min/pmol
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 8.2
-
about half-maximal activity at pH 5.7 and 8.2, with a small shoulder of 77% of maximal activity at 7-7.5
6.3 - 9.2
-
about half-maximal activity at pH 6.3 and 9.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
isoelectric focusing, pH 3-10, 4% polyacrylamide gel or flat bed isoelectric focusing with Sephadex G-200
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
polymorphonuclear and alveolar
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
peripherally in hepatocytes, rarely in cytoplasm
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MYLK2_RABIT
608
0
65468
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
103000
-
sedimentation equilibrium method
108000 - 125000
-
short myosin light chain kinase
125700
calculated from sequence of DNA
152000
x * 152000, SDS-PAGE, recombinant enzyme
77000
-
gel filtration
92000
-
x * 92000, SDS-PAGE
94000
-
1 * 94000, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
diffential phosphorylation by Aurora B on serine residues during interphase and mitosis has regulatory function, phosphorylation sites for Aurora B on the enzyme, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isolution structure of a calmodulin-target peptide complex by multidimensional NMR
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A983P
-
dramatic increase in Ca2+ required for half-maximal activity
A986P
-
significantly increase in Ca2+ required for half-maximal activity, slightly decreased KM for regulatory light chain
M968P
-
10% Ca2+/calmodulin independent activity of total activity, decreased KM for regulatory light chain
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
rapid inactivation below
640614, 640615
6.3 - 8
-
stable in 10% sucrose
640614
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freeze-thawing decreases activity
-
unstable upon lyophilization
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 5% w/v sucrose, several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on calmodulin-Sepharose
-
recombinant His-tagged wild-type and mutant isozymes from Escherichia coli strain Bl21(DE3) by nickel affinity chromatograpyh
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA, expressed in COS cells
expression in A7r5 rat thoracic aorta smooth muscle cells as GFP-fusion protein
-
expression in COS cells
expression in COS-7 african green monkey kidney cells
-
expression in COS-cells
expression in Sf9 insect cells
-
expression in transgenic mice, expression in COS cells
-
expression of the long isozyme L-MLCK in murine NIH3T3 cells, expression of GFP-tagged wild-type and mutant isozymes in COS-7 cells and as His-tagged proteins in Escherichia coli strain BL21(DE3)
-
telokin, the carboxyl terminus of the smooth muscle myosin light chain kinase which is expressed as an independent protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Davis, J.S.; Hassanzadeh, S.; Winitsky, S.; Lin, H.; Satorius, C.; Vemuri, R.; Aletras, A.H.; Wen, H.; Epstein, N.D.
The overall pattern of cardiac contraction depends on a spatial gradient of myosin regulatory light chain phosphorylation
Cell
107
631-641
2001
Oryctolagus cuniculus (P07313), Homo sapiens (Q9H1R3), Homo sapiens
Manually annotated by BRENDA team
Herring, B.P.; Stull, J.T.; Gallagher, P.J.
Domain characterization of rabbit skeletal muscle myosin light chain kinase
J. Biol. Chem.
265
1724-1730
1990
Oryctolagus cuniculus (P07313), Oryctolagus cuniculus
Manually annotated by BRENDA team
Ikura, M.; Clore, G.M.; Gronenborn, A.M.; Zhu, G.; Klee, C.B.; Bax, A.
Solution structure of a calmodulin-target peptide complex by multidimensional NMR
Science
256
632-638
1992
Oryctolagus cuniculus (P07313)
Manually annotated by BRENDA team
Takio, K.; Blumenthal, D.K.; Edelman, A.M.; Walsh, K.A.; Krebs, E.G.; Titani, K.
Amino acid sequence of an active fragment of rabbit skeletal muscle myosin light chain kinase
Biochemistry
24
6028-6037
1985
Oryctolagus cuniculus (P07313), Oryctolagus cuniculus
Manually annotated by BRENDA team
Takio, K.; Blumenthal, D.K.; Walsh, K.A.; Titani, K.; Krebs, E.G.
Amino acid sequence of rabbit skeletal muscle myosin light chain kinase
Biochemistry
25
8049-8057
1986
Oryctolagus cuniculus (P07313), Oryctolagus cuniculus
Manually annotated by BRENDA team
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
Gallagher, P.J.; Herring, B.P.
The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin
J. Biol. Chem.
266
23945-23952
1991
Oryctolagus cuniculus (P29294)
Manually annotated by BRENDA team
Pires, E.; Perry, S.V.; Thomas, M.A.W.
Myosin light-chain kinase, a new enzyme from striated muscle
FEBS Lett.
41
292-296
1974
Oryctolagus cuniculus
Manually annotated by BRENDA team
Pires, E.M.V.; Perry, S.V.
Purification and properties of myosin light-chain kinase from fast skeletal muscle
Biochem. J.
167
137-146
1977
Oryctolagus cuniculus
Manually annotated by BRENDA team
Nagamoto, H.; Yagi, K.
Properties of myosin light chain kinase prepared from rabbit skeletal muscle by an improved method
J. Biochem.
95
1119-1130
1984
Oryctolagus cuniculus
Manually annotated by BRENDA team
Yang, H.H.; Boxer, L.A.
Purification of myosin light chain kinase from rabbit polymorphonuclear leukocytes
Pediatr. Res.
15
229-234
1981
Oryctolagus cuniculus
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
Nunnally, M.H.; Rybicki, S.B.; Stull, J.T.
Characterization of chicken skeletal muscle myosin light chain kinase. Evidence for muscle-specific isozymes
J. Biol. Chem.
260
1020-1026
1985
Gallus gallus, Oryctolagus cuniculus
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
Gao, Z.H.; Zhi, G.; Herring, B.P.; Moomaw, C.; Deogny, L.; Slaughter, C.A.; Stull, J.T.
Photoaffinity labeling of a peptide substrate to myosin light chain kinase
J. Biol. Chem.
270
10125-10135
1995
Oryctolagus cuniculus
Manually annotated by BRENDA team
Lin, P.; Luby-Phelps, K.; Stull, J.T.
Properties of filament-bound myosin light chain kinase
J. Biol. Chem.
274
5987-5994
1999
Oryctolagus cuniculus
Manually annotated by BRENDA team
Padre, R.C.; Stull, J.T.
Conformational requirements for Ca2+/calmodulin binding and activation of myosin light chain kinase
FEBS Lett.
472
148-152
2000
Oryctolagus cuniculus
Manually annotated by BRENDA team
Dulyaninova, N.G.; Bresnick, A.R.
The long myosin light chain kinase is differentially phosphorylated during interphase and mitosis
Exp. Cell Res.
299
303-314
2004
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Zhu, H.Q.; Wang, Y.; Hu, R.L.; Ren, B.; Zhou, Q.; Jiang, Z.K.; Gui, S.Y.
Distribution and expression of non-muscle myosin light chain kinase in rabbit livers
World J. Gastroenterol.
9
2715-2719
2003
Homo sapiens, Oryctolagus cuniculus
Manually annotated by BRENDA team
Yang, C.X.; Chen, H.Q.; Chen, C.; Yu, W.P.; Zhang, W.C.; Peng, Y.J.; He, W.Q.; Wei, D.M.; Gao, X.; Zhu, M.S.
Microfilament-binding properties of N-terminal extension of the isoform of smooth muscle long myosin light chain kinase
Cell Res.
16
367-376
2006
Oryctolagus cuniculus
Manually annotated by BRENDA team
Ryder, J.W.; Lau, K.S.; Kamm, K.E.; Stull, J.T.
Enhanced skeletal muscle contraction with myosin light chain phosphorylation by a calmodulin-sensing kinase
J. Biol. Chem.
282
20447-20454
2007
Oryctolagus cuniculus
Manually annotated by BRENDA team