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Information on EC 2.7.11.7 - myosin-heavy-chain kinase and Organism(s) Dictyostelium discoideum and UniProt Accession P34125

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IUBMB Comments
The enzyme from Dictyostelium sp. (slime moulds) brings about phosphorylation of the heavy chains of Dictyostelium myosin, inhibiting the actin-activated ATPase activity of the myosin. One threonine residue in each heavy chain acts as acceptor. While the enzyme from some species is activated by actin, in other cases Ca2+/calmodulin are required for activity.
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Dictyostelium discoideum
UNIPROT: P34125
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Word Map
The taxonomic range for the selected organisms is: Dictyostelium discoideum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mhck a, mihck, myosin heavy chain kinase, a-cat, mhck b, mihc kinase, myosin heavy chain kinase a, mhck-b, myosin ii heavy chain kinase, myosin ii heavy-chain kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A-CAT
kinase (phosphorylating), myosin heavy chain
-
-
-
-
myosin heavy chain kinase
-
-
-
-
myosin heavy chain kinase A
-
myosin heavy chain kinase B
-
myosin heavy chain kinase C
-
myosin I heavy-chain kinase
-
-
-
-
myosin II heavy chain kinase
-
-
myosin II heavy chain kinase A
-
myosin II heavy chain kinase B
-
myosin II heavy chain kinases A
-
myosin II heavy chain kinases B
-
myosin II heavy-chain kinase
-
-
-
-
myosin-II heavy chain kinase A
-
additional information
member of the p21-activated kinase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:[myosin heavy-chain] O-phosphotransferase
The enzyme from Dictyostelium sp. (slime moulds) brings about phosphorylation of the heavy chains of Dictyostelium myosin, inhibiting the actin-activated ATPase activity of the myosin. One threonine residue in each heavy chain acts as acceptor. While the enzyme from some species is activated by actin, in other cases Ca2+/calmodulin are required for activity.
CAS REGISTRY NUMBER
COMMENTARY hide
64763-54-8
-
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 heavy chain kinase
ADP + myosin heavy chain kinase phosphate
show the reaction diagram
ATP + AAYKTKKKK
?
show the reaction diagram
-
-
-
?
ATP + AKRVSMMR
ADP + AKRVS(-phosphate)MMR
show the reaction diagram
peptide derived from myosin I heavy chain kinase amino acid residues 4-11, exchange at position 4: Ser to Ala
phophorylation site is Ser8
?
ATP + caldesmon
ADP + caldesmon phosphate
show the reaction diagram
O76739, P42527, P90648
catalytic domain
-
-
?
ATP + casein
ADP + casein phosphate
show the reaction diagram
ATP + GRSARVSTYA
ADP + GRSARVS(-phosphate)TYA
show the reaction diagram
peptide derived from Dictyostelium myosin ID
-
?
ATP + histone 2A
ADP + histone 2A phosphate
show the reaction diagram
-
low activity
-
-
?
ATP + MH1 peptide
ADP + MH1 peeptide phosphate
show the reaction diagram
-
-
-
?
ATP + myelin basic protein
?
show the reaction diagram
-
-
-
?
ATP + myelin basic protein
ADP + myelin basic protein phosphate
show the reaction diagram
O76739, P42527, P90648
catalytic domain
-
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
show the reaction diagram
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
show the reaction diagram
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
show the reaction diagram
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
show the reaction diagram
ATP + myosin regulatory light chain
ADP + myosin regulatory light chain phosphate
show the reaction diagram
O76739, P42527, P90648
catalytic domain
-
-
?
ATP + peptide LMM58 of heavy chain
?
show the reaction diagram
-
4 mol phosphate per mol, Thr-residues are phosphorylated
-
-
?
ATP + phosvitin
ADP + phosvitin phosphate
show the reaction diagram
-
low activity
-
-
?
ATP + RKKFGESEKTKTKEFL
?
show the reaction diagram
ATP + RKKFGESEKTKTKEFL-amide
?
show the reaction diagram
ATP + synthetic peptides
?
show the reaction diagram
ATP + YAYDTRYRR
?
show the reaction diagram
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
show the reaction diagram
ATP + [myosin II heavy-chain]
ADP + [myosin II heavy-chain] phosphate
show the reaction diagram
-
-
-
?
ATP + [myosin-heavy-chain]
ADP + [myosin-heavy-chain]phosphate
show the reaction diagram
ATP + [protein LMM58 heavy chain]
ADP + [protein LMM58 heavy 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 heavy chain kinase
ADP + myosin heavy chain kinase phosphate
show the reaction diagram
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
show the reaction diagram
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
show the reaction diagram
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
show the reaction diagram
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
show the reaction diagram
ATP + [myosin II heavy-chain]
ADP + [myosin II heavy-chain] phosphate
show the reaction diagram
-
-
-
?
ATP + [myosin-heavy-chain]
ADP + [myosin-heavy-chain]phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no activation by Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+/calmodulin
-
EGTA
-
no inhibition
Positively charged polypeptides
-
strong inhibition, e.g. poly-(D-Lys), poly-(L-Lys), poly-(L-Arg) of different molecular weights
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acidic phospholipids
-
DNA
-
autophosphorylation activity is increased 5-10fold in a Ca2+-independent manner
F-actin
-
G-actin
slight activation of MHCK A, activation is abolished by latrunculin A, which depolymerizes the actin filament
-
guanosine 5'-3-O-(thio)triphosphate-Rac1
-
heparin
-
autophosphorylation activity is increased 5-10fold in a Ca2+-independent manner
phosphatidylinositol
10fold activation of autophosphorylation and kinase activity
phosphatidylinositol 4,5-bisphosphate
10fold activation of autophosphorylation and kinase activity
phosphatidylserine
10fold activation of autophosphorylation and kinase activity
Phospholipid vesicles
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.098 - 0.116
AKRVSMMR
0.058 - 0.23
ATP
0.016 - 0.019
GRSARVSTYA
0.22
RKKFGESEKTKTKEFL
recombinant MHCK B, pH 7.0, 22°C
0.1 - 0.28
RKKFGESEKTKTKEFL-amide
0.55
YAYDTRYRR
O76739, P42527, P90648
pH 7.0, 25°C
0.015
[myosin heavy-chain]
-
pH 7.5, 22°C
0.015
[protein LMM58 heavy chain]
-
pH 7.5, 22°C
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5 - 5.4
AKRVSMMR
0.017 - 0.1
ATP
0.3 - 4.7
GRSARVSTYA
0.01 - 0.79
RKKFGESEKTKTKEFL-amide
14
YAYDTRYRR
O76739, P42527, P90648
pH 7.0, 25°C
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
inhibition by positively charged polypeptides
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.1
-
purified enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
actin binding assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
overexpresssing cells show slower growth and increased cell size
Manually annotated by BRENDA team
additional information
enzyme expression only during development
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DGKA_DICDI
887
0
99177
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
145000
x * 145000, phosphorylated MHCK A, SDS-PAGE, x * 130000, unphosphorylated MHCK A, SDS-PAGE
240000
-
gel filtration
700000
-
above, gel filtration
84000
-
x * 84000, SDS-PAGE
86000
x * 86000, DNA sequence determination
94000
-
x * 94000, phosphorylated enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
alpha-kinase domain in complex with AMP and adenosine, hanging drop vapor diffusion method, using 200 mM NaH2PO4, 20% (w/v) polyethylene glycol 8000, and 100 mM Tris-HCl, pH 7.5
alpha-kinase domain of myosin-II heavy chain kinase A, hanging drop vapor diffusion method, using 5% PEG (w/v) 8000, 20% (w/v) PEG 300, 10% (v/v) glycerol and 0.1 M Tris-HCl, pH 9.0
MHCK A in complex with ATP and a peptide substrate, and MHCK A alpha kinase domain in individual complexes with AMP, ADP, and beta,gamma-methyleneadenosine 5'-triphosphate, X-ray diffraction structcure determination and analysis
purified recombinant wild-type and truncation mutant enzymes, hanging drop vapor diffusion method, mixing of 0.001 ml protein solution with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 0.2 M NaH2PO4, and 18% w/v PEG 8000, 4°C, 10 days, X-ray diffraction structure determination and analysis at 1.9 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C800A
catalytic domain mutation, no remaining activity when expressed as full length enzyme or as catalytic domain only in a deficient Dictyostelium discoideum cell line
D663A
D766A
site-directed mutagenesis of the central active site residue, inactive mutant
D766E
site-directed mutagenesis of the central active site residue, inactive mutant
D766S
E713A
the mutant shows about 10% activity compared to the wild type enzyme
E713D
the mutant shows about 3% activity compared to the wild type enzyme
K645A
site-directed mutagenesis of an alpha-kinase domain residue, the mutant shows 98.5% reduced activity compared to the wild-type enzyme
K645R
the mutant shows about 3% activity compared to the wild type enzyme
K722N
the mutant shows about 20% activity compared to the wild type enzyme
L716S
the mutant shows about 1% activity compared to the wild type enzyme
Q758A
the mutant shows about 3% activity compared to the wild type enzyme
Q768A
the mutant shows about 70% activity compared to the wild type enzyme
Q822R/Q823R/T825S
site-directed mutagenesis
R592A
site-directed mutagenesis of an alpha-kinase domain residue, the mutant shows 92% reduced activity compared to the wild-type enzyme
R592L
the mutant shows about 30% activity compared to the wild type enzyme
T825A
site-directed mutagenesis
T825E
site-directed mutagenesis
T825S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
and above, unstable
640776
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
1-2 h, stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loses about 25% of activity for every freeze-thaw cycle
-
phosphorylated enzyme is somewhat less stable than unphosphorylated enzyme
-
very unstable if exposed to low salt, i.e. 50 mM KCl or less, in the absence of sucrose
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 25 mM HEPES buffer, pH 7.5, 1 mM DTT, 1 mM EDTA, 50 mM NaCl, 10% glycerol, or 20% sucrose, stable for 3 months
-
-20°C, in 50% sucrose or glycerol, t1/2: 2 weeks
-
0°C, highly purified preparation of unphosphorylated enzyme, 25% loss of activity per day
-
0°C, in 10 mM imidazole, pH 7, 100 mM KCl, 2 mM DTT, 60% sucrose, several weeks
-
0°C, partially purified preparation of unphosphorylated enzyme, several days
-
indefinitely stable upon storage in liquid nitrogen, recovery of 60-70% activity after thawing
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
14000fold to near homogeneity
-
DE53 column chromatography and SP-Sepharose column chromatography
isolation of highly phosphorylated and unphosphorylated myosin II heavy chain kinase A
-
MHCK B, recombinant from Dictyostelium discoideum cells as FLAG-tagged protein
recombinant GST-fusion catalytic domain of MHCK B, expressed in Escherichia coli
O76739, P42527, P90648
recombinant GST-tagged wild-type full-length and MHCKB truncation mutants by glutathione affinity chromatography
recombinant His-tagged catalytic domain of MHCK A, expressed in Escherichia coli
O76739, P42527, P90648
recombinant His-tagged catalytic domain of MHCK C, expressed in Escherichia coli
O76739, P42527, P90648
recombinant His-tagged full-length isozyme MHCK A and truncation mutant DELTAcoil-MHCK A from Dictyostelium discoideum to homogeneity by affinity chromatography, recombinant GST-fusion coiled-coil domain and catalytic domain from Escherichia coli to near homogeneity by affinity chromatography
recombinant His-tagged full-length isozyme MHCK A from Dictyostelium discoideum by affinity chromatography, recombinant GST-fusion truncation mutant DELTAcoil-MHCK A from Escherichia coli by affinity chromatography, the GST-tag is cleaved off by thrombin treatment
recombinant His-tagged or GFP-fusion proteins from Dictyostelium discoideum
recombinant His-tagged wild-type and mutant MHCK A alpha-kinase domains from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant MHCK A GST-tagged catalytic domain by glutathione affinity chromatography
recombinant MHCK B GST-tagged catalytic domain by glutathione affinity chromatography
solubilized by high-salt extraction, affinity chromatography, 4600fold, to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, gene MHCK possesses all of the domains characteristic of members of the protein kinase C family
cells overexpressing GFP-GEF have both unphosphorylated and autophosphorylated MHCK A
construction of His-tagged or GFP fusion proteins with the full length enzyme or enzyme fragments, expression in Dictyostelium discoideum cells
DNA sequence determination and analysis
expressed in Escherichia coli BL21(DE3) cells
expression of FLAG-tagged T825A and T825E enzyme mutants in Dictyostelium discoideum cells, expression of His-tagged wild-type and mutant MHCK A alpha-kinase domains in Escherichia coli strain BL21(DE3)
expression of GFP-tagged isozyme MHCK A in a Dictyostelium discoideum strain lacking endogenous MHCK A, expression of a truncation mutant DELTAcoil-MHCK A comprising residues 1-498 in Escherichia coli as GST-fused protein
expression of MHCK A, comprising residues 527-887, i.e. A-CAT, as a GST-fusion protein, phylogenetic analysis
expression of MHCK B, comprising residues 13-459, i.e. B-CAT, as a GST-fusion protein, phylogenetic analysis
expression of the 3 isozymes MHCK A, MHCK B, and MHCK C as GFP-fusion proteins
-
expression of the catalytic domain of MHCK B as a GST-fusion protein in Escherichia coli BL21(DE3)
O76739, P42527, P90648
expression of the His-tagged catalytic domain of MHCK A in Escherichia coli BL21(DE3)
O76739, P42527, P90648
expression of the His-tagged catalytic domain of MHCK C in Escherichia coli BL21(DE3)
O76739, P42527, P90648
gene mhck A, construction of overexpressing cell line by transfection of an expression plasmid into the deficient mhck A- cell line
-
MHCK B, overexpression as FLAG-tagged protein in AX2 cells or 3xALA cells of Dictyostelium discoideum
overexpression of FLAG-tagged full-length MHCK-B in Dictyostelium cells, in AX2, mhkB-null, and mhkA/B/C-null cell lines. Expression of GST-tagged wild-type full-length and MHCKB truncation mutants
overexpression of His-tagged full-length isozyme MHCK A and truncation mutant DELTAcoil-MHCK A comprising residues 1-498 in Dictyostelium discoideum, overexpression of isolated coiled-coil domain and of the catalytic domain in Escherichia coli as GST-fused proteins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Dictyostelium discoideum (P34125), Dictyostelium discoideum (P42527), Dictyostelium discoideum (P90648)
Manually annotated by BRENDA team
Ct, G.P.; Bukiejko, U.
Purification and characterization of a myosin heavy chain kinase from Dictyostelium discoideum
J. Biol. Chem.
262
1065-1072
1987
Dictyostelium discoideum
Manually annotated by BRENDA team
Medley, Q.W.; Bagshaw, W.L.; Truong, T.; Cote, G.P.
Dictyostelium myosin II heavy-chain kinase A is activated by heparin, DNA and acidic phospholipids and inhibited by polylysine, polyarginine and histones
Biochim. Biophys. Acta
1175
7-12
1992
Dictyostelium discoideum
Manually annotated by BRENDA team
Ravid, S.; Spudich, J.A.
Myosin heavy chain kinase from developed Dictyostelium cells. Purification and characterization
J. Biol. Chem.
264
15144-15150
1989
Dictyostelium discoideum
Manually annotated by BRENDA team
Medley, Q.W.; Lee, S.F.; Cote, G.P.
Purification and characterization of myosin II heavy chain kinase A from Dictyostelium
Methods Enzymol.
196
23-34
1991
Dictyostelium discoideum, Dictyostelium discoideum Ax-3
Manually annotated by BRENDA team
Nagasaki, A.; Itoh, G.; Yumura, S.; Uyeda, T.Q.
Novel myosin heavy chain kinase involved in disassembly of myosin II filaments and efficient cleavage in mitotic dictyostelium cells
Mol. Biol. Cell
13
4333-4342
2002
Dictyostelium discoideum, Dictyostelium discoideum (Q8MY12), Dictyostelium discoideum AX2 (Q8MY12)
Manually annotated by BRENDA team
Rico, M.; Egelhoff, T.T.
Myosin heavy chain kinase B participates in the regulation of myosin assembly into the cytoskeleton
J. Cell. Biochem.
88
521-532
2003
Dictyostelium discoideum (P90648), Dictyostelium discoideum
Manually annotated by BRENDA team
Ravid, S.; Spudich, J.A.
Membrane-bound Dictyostelium myosin heavy chain kinase: a developmentally regulated substrate-specific member of the protein kinase C family
Proc. Natl. Acad. Sci. USA
89
5877-5881
1992
Dictyostelium discoideum (P34125), Dictyostelium discoideum AX3 (P34125)
Manually annotated by BRENDA team
Kolman, M.F.; Futey, L.M.; Egelhoff, T.T.
Dictyostelium myosin heavy chain kinase A regulates myosin localization during growth and development
J. Cell. Biol.
132
101-109
1996
Dictyostelium discoideum, Dictyostelium discoideum JH10
Manually annotated by BRENDA team
Lee, S.F.; Egelhoff, T.T.; Mahasneh, A.; Cote, G.P.
Cloning and characterization of a Dictyostelium myosin I heavy chain kinase activated by Cdc42 and Rac
J. Biol. Chem.
271
27044-27048
1996
Dictyostelium discoideum (Q869N2)
Manually annotated by BRENDA team
Lee, S.F.; Mahasneh, A.; de la Roche, M.; Cote, G.P.
Regulation of the p21-activated kinase-related Dictyostelium myosin I heavy chain kinase by autophosphorylation, acidic phospholipids, and Ca2+-calmodulin
J. Biol. Chem.
273
27911-27917
1998
Dictyostelium discoideum (Q869N2)
Manually annotated by BRENDA team
Luo, X.; Crawley, S.W.; Steimle, P.A.; Egelhoff, T.T.; Cote, G.P.
Specific phosphorylation of threonine by the Dictyostelium myosin II heavy chain kinase family
J. Biol. Chem.
276
17836-17843
2001
Dictyostelium discoideum (O76739), Dictyostelium discoideum (P42527), Dictyostelium discoideum (P90648)
Manually annotated by BRENDA team
Steimle, P.A.; Licate, L.; Cote, G.P.; Egelhoff, T.T.
Lamellipodial localization of Dictyostelium myosin heavy chain kinase A is mediated via F-actin binding by the coiled-coil domain
FEBS Lett.
516
58-62
2002
Dictyostelium discoideum (P42527), Dictyostelium discoideum
Manually annotated by BRENDA team
Russ, M.; Croft, D.; Ali, O.; Martinez, R.; Steimle, P.A.
Myosin heavy chain kinase A from Dictyostelium possesses a novel actin binding domain that cross-links actin filaments
Biochem. J.
395
373-383
2005
Dictyostelium discoideum (P42527)
Manually annotated by BRENDA team
Egelhoff, T.T.; Croft, D.; Steimle, P.A.
Actin activation of myosin heavy chain kinase A in Dictyostelium: a biochemical mechanism for the spatial regulation of myosin II filament disassembly
J. Biol. Chem.
280
2879-2887
2005
Dictyostelium discoideum (P42527), Dictyostelium discoideum
Manually annotated by BRENDA team
Yumura, S.; Yoshida, M.; Betapudi, V.; Licate, L.S.; Iwadate, Y.; Nagasaki, A.; Uyeda, T.Q.; Egelhoff, T.T.
Multiple myosin II heavy chain kinases: roles in filament assembly control and proper cytokinesis in Dictyostelium
Mol. Biol. Cell
16
4256-4266
2005
Dictyostelium discoideum
Manually annotated by BRENDA team
Crawley, S.W.; Cote, G.P.
Determinants for substrate phosphorylation by Dictyostelium myosin II heavy chain kinases A and B and eukaryotic elongation factor-2 kinase
Biochim. Biophys. Acta
1784
908-915
2008
Dictyostelium discoideum (P42527), Dictyostelium discoideum (P90648), Dictyostelium discoideum
Manually annotated by BRENDA team
Mondal, S.; Bakthavatsalam, D.; Steimle, P.; Gassen, B.; Rivero, F.; Noegel, A.A.
Linking Ras to myosin function: RasGEF Q, a Dictyostelium exchange factor for RasB, affects myosin II functions
J. Cell Biol.
181
747-760
2008
Dictyostelium discoideum (P42527), Dictyostelium discoideum
Manually annotated by BRENDA team
Franklin, A.; Hyatt, L.; Chowdhury, A.; Steimle, P.A.
The WD-repeat domain of Dictyostelium myosin heavy chain kinase C functions in both substrate targeting and cellular localization
Eukaryot. Cell
9
344-349
2010
Dictyostelium discoideum (Q8MY12), Dictyostelium discoideum
Manually annotated by BRENDA team
Underwood, J.; Greene, J.; Steimle, P.A.
Identification of a new mechanism for targeting myosin II heavy chain phosphorylation by Dictyostelium myosin heavy chain kinase B
BMC Res. Notes
3
56
2010
Dictyostelium discoideum (P90648)
Manually annotated by BRENDA team
Crawley, S.W.; Gharaei, M.S.; Ye, Q.; Yang, Y.; Raveh, B.; London, N.; Schueler-Furman, O.; Jia, Z.; Cote, G.P.
Autophosphorylation activates Dictyostelium myosin II heavy chain kinase A by providing a ligand for an allosteric binding site in the alpha-kinase domain
J. Biol. Chem.
286
2607-2616
2011
Dictyostelium discoideum (P42527), Dictyostelium discoideum
Manually annotated by BRENDA team
Ye, Q.; Crawley, S.W.; Yang, Y.; Cote, G.P.; Jia, Z.
Crystal structure of the alpha-kinase domain of Dictyostelium myosin heavy chain kinase A
Sci. Signal.
3
ra17
2010
Dictyostelium discoideum (P42527), Dictyostelium discoideum
Manually annotated by BRENDA team
Yang, Y.; Ye, Q.; Jia, Z.; Cote, G.P.
Characterization of the catalytic and nucleotide binding properties of the alpha-kinase domain of Dictyostelium myosin-II heavy chain kinase A
J. Biol. Chem.
290
23935-23946
2015
Dictyostelium discoideum (P42527)
Manually annotated by BRENDA team
Ye, Q.; Yang, Y.; van Staalduinen, L.; Crawley, S.W.; Liu, L.; Brennan, S.; Cote, G.P.; Jia, Z.
Structure of the Dictyostelium myosin-II heavy chain kinase A (MHCK-A) alpha-kinase domain apoenzyme reveals a novel autoinhibited conformation
Sci. Rep.
6
26634
2016
Dictyostelium discoideum (P42527)
Manually annotated by BRENDA team