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Information on EC 2.7.11.7 - myosin-heavy-chain kinase
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2.7.11.7 myosin-heavy-chain kinaseIUBMB 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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Word Map
- 2.7.11.7
- dictyostelium
- discoideum
- autophosphorylation
-
disassembly
-
p21-activated
- acanthamoeba
-
cytokinesis
- amoeba
-
actin-activated
- ca2+-calmodulin
- mg2+-atpase
-
furrow
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A-CAT
EC 2.7.1.129
-
-
formerly
-
kinase (phosphorylating), myosin heavy chain
-
-
-
-
MHCK
MIHCK
myosin heavy chain kinase
-
-
-
-
myosin I heavy-chain kinase
-
-
-
-
myosin II heavy-chain kinase
-
-
-
-
additional information
additional information
member of the p21-activated kinase family
additional information
member of the p21-activated kinase family
additional information
member of the p21-activated kinase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
catalytic domain: amino acid residues 31-259
ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
catalytic domain structure, modeling
-
ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
residues Ser627, Thr631 and Thr632 are essential for catalytic activity
-
ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
activation of the enzyme by autophosphorylation is necessary for full catalytic activity
-
ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
enzyme contains the C-terminal WD-domain, responsible for substrate binding, the catalytic domain, and the N-terminal coiled-coil translocation domain
ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
enzyme contains the C-terminal WD-domain, responsible for substrate binding, the catalytic domain, and the N-terminal coiled-coil translocation domain
ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
major phosphorylation site: Ser8
ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
catalytic domain: amino acid residues 31-259
-
-
ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
64763-54-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + AKRVSMMR
ADP + AKRVS(-phosphate)MMR
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
catalytic domain
-
-
?
ATP + chicken gizzard myosin light chain
ADP + chicken gizzard myosin light chain phosphate
ATP + GRSARVSTYA
ADP + GRSARVS(-phosphate)TYA
peptide derived from Dictyostelium myosin ID
-
?
ATP + myelin basic protein
ADP + myelin basic protein phosphate
catalytic domain
-
-
?
ATP + myosin regulatory light chain
ADP + myosin regulatory light chain phosphate
catalytic domain
-
-
?
ATP + peptide LMM58 of heavy chain
?
-
4 mol phosphate per mol, Thr-residues are phosphorylated
-
-
?
ATP + smooth muscle myosin light chain
ADP + smooth muscle myosin light chain phosphate
-
-
-
-
?
ATP + [myosin II heavy-chain]
ADP + [myosin II heavy-chain] phosphate
-
-
-
?
ATP + [protein LMM58 heavy chain]
ADP + [protein LMM58 heavy chain] phosphate
-
-
-
-
?
ATP + casein
ADP + casein phosphate
catalytic domain, low activity
-
-
?
ATP + chicken gizzard myosin light chain
ADP + chicken gizzard myosin light chain phosphate
-
poor substrate
-
-
?
ATP + chicken gizzard myosin light chain
ADP + chicken gizzard myosin light chain phosphate
-
no activity
-
-
?
ATP + GRGRSSVYS
ADP + GRGRSS(-phosphate)VYS
-
synthetic peptide with a sequence corresponding to the phosphorylation site of myosin IC
-
?
ATP + GRGRSSVYS
ADP + GRGRSS(-phosphate)VYS
-
synthetic peptide with a sequence corresponding to the phosphorylation site of myosin IC
-
?
ATP + GRGRSSVYS
ADP + GRGRSS(-phosphate)VYS
-
synthetic peptide with a sequence corresponding to the phosphorylation site of myosin IC
-
-
?
ATP + GRGRSSVYS
ADP + GRGRSS(-phosphate)VYS
synthetic peptide with a sequence corresponding to the phosphorylation site of myosin IC
-
-
?
ATP + myosin heavy chain
ADP + myosin heavy chain phosphate
-
protamine is no substrate
-
?
ATP + myosin heavy chain
ADP + myosin heavy chain phosphate
-
no activity with myosins from gizzard, cardiac or skeletal muscle, but active with the isolated 20 kDa gizzard myosin light chain
-
?
ATP + myosin heavy chain
ADP + myosin heavy chain phosphate
-
substrate: bovine brain myosin
-
?
ATP + myosin heavy chain
ADP + myosin heavy chain phosphate
-
specific for myosin heavy chains, no phosphorylation of light chains
-
?
ATP + myosin heavy chain
ADP + myosin heavy chain phosphate
-
substrate specificity
-
?
ATP + myosin heavy chain
ADP + myosin heavy chain phosphate
-
phosphorylates threonine residues
-
?
ATP + myosin heavy chain
ADP + myosin heavy chain phosphate
-
phosphorylates threonine residues
-
?
ATP + myosin heavy chain
ADP + myosin heavy chain phosphate
-
rabbit skeletal myosin heavy chains are phosphorylated
-
?
ATP + myosin heavy chain
ADP + myosin heavy chain phosphate
-
0.7 mol phosphate per mol of heavy chain
-
?
ATP + myosin heavy chain
ADP + myosin heavy chain phosphate
-
best substrate: chicken intestine brush border myosin
-
?
ATP + myosin heavy chain
ADP + myosin heavy chain phosphate
-
best substrate: chicken intestine brush border myosin
-
?
ATP + myosin heavy chain
ADP + myosin heavy chain phosphate
-
specific for myosin heavy chains, no phosphorylation of light chains
-
?
ATP + myosin heavy chain
ADP + myosin heavy chain phosphate
-
specific for myosin heavy chains, no phosphorylation of light chains
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
35 kDa trypsin fragment of the C-terminus of the maximally activated, phosphorylated enzyme is fully catalytically active and contains 2 thirds of the autophosphorylation sites of the native enzyme
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
intermolecular autophosphorylation with vesicle-bound enzyme in absence of substrates
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
leads to activation of the phosphorylation activity towards myosin I
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
leads to activation of the phosphorylation activity towards myosin I
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
enzyme incorporates 6-8 mol phosphate per mol of enzyme
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
enzyme incorporates 1 mol of phosphate per mol of enzyme
-
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
4 phosphorylation sites on each heavy chain
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
enzyme incorporates 20 mol phosphate per mol of kinase
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
enzyme incorporates 2-3 mol phosphate per mol of 130 kDa subunit
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
leads to activation of the phosphorylation activity towards myosin I
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
leads to activation of the phosphorylation activity towards myosin I
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
leads to activation of the phosphorylation activity towards myosin I
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
-
leads to activation of the phosphorylation activity towards myosin I
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
the enzyme contains a cluster of 23 serine and threonine residues at the carboxyterminal end that might be the autophosphorylation domain
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
increased activity during chemotaxis
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
enzyme incorporates 20 mol phosphate per mol of kinase
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
the enzyme contains a cluster of 23 serine and threonine residues at the carboxyterminal end that might be the autophosphorylation domain
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
increased activity during chemotaxis
-
?
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
-
-
-
?
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
role of RasGEF Q in regulating myosin II function through MHCK A, overview
-
-
?
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
phosphorylation of myosin takes place at three threonine residues in the tail region by myosin II heavy chain kinases
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
substrate: myosin IB, phosphorylation site is Ser315
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
substrate: myosin IB, phosphorylation site is Ser315
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
higher activity with membrane-bound substrate myosin I
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
myosin light chains are no substrates
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
substrate myosin IA: phosphorylation of a single threonine
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylates serine-residues
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
substrate is heavy chain of myosin IC
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
substrate is heavy chain of myosin IC
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
substrate is heavy chain of myosin IC
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
incorporation of 0.9-1.0 mol phosphate per mol of heavy chain myosin
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylates threonine residues
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
myosin I from intestinal brush border
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
35 kDa trypsin fragment of the C-terminus of the maximally activated, phosphorylated enzyme is fully catalytically active and contains 2 thirds of the autophosphorylation sites of the native enzyme
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
contains two myosin heavy chain kinases: one for myosin I and one for myosin II
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
substrate: myosin IC, phosphorylation site is Ser311
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
a basic amino acid is essential on amino-terminal side of phosphorylation site, two are preferable, and a Tyr-residue is essential two residues away on the COOH-terminal side
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
substrates are heavy chains of myosin IA and IB
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
substrates are heavy chains of myosin IA and IB
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
substrates are heavy chains of myosin IA and IB
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
myosin light chains are no substrates
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
myosin light chains are no substrates
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
4 mol phosphate per mol of myosin
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylation of residues Thr1833 and Thr2029
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylation of residues Thr1833 and Thr2029
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylates threonine residues
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylates threonine residues
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylates threonine residues
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylates threonine residues
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
1.9 mol phosphate per mol myosin
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
10 mol phosphate per mol of kinase subunit
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
20 mol phosphate per mol of kinase subunit, kinetics
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
major site of phosphorylation is Ser8
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
bovine muscle myosin is no substrate
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
no substrates are human platelet myosin, ovalbumin and smooth muscle myosin from turkey
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
6-8 mol phosphate per mol of enzyme
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
substrate: myosin ID
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
substrate: myosin ID
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
reaction in regulatory contractile activity in Dictyostelium discoideum
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
involved in regulation of myosin II filament assembly
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
involved in regulation of myosin II filament assembly
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
increased activity during chemotaxis
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylation of residues Thr1833 and Thr2029
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
phosphorylates threonine residues
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
10 mol phosphate per mol of kinase subunit
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
6-8 mol phosphate per mol of enzyme
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
myosin light chains are no substrates
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
contains two myosin heavy chain kinases: one for myosin I and one for myosin II
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
incorporation of 3 mol phosphate per mol of myosin II heavy chain, phosphorylation sites are mainly identical in vitro and in vivo
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
phosphorylates serine residues
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
phosphorylates serine residues
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
specific isozyme A for the heavy chain of myosin II
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
specific isozyme A for the heavy chain of myosin II
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
isozyme MHCK B
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
drives filament disassembly in vitro
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
drives filament disassembly in vitro
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
catalytic domain
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
phosphorylates primarly threonine residues
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
phosphorylates primarly threonine residues
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
involved in regulation of myosin II filament assembly
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
involved in regulation of myosin II filament assembly
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
key role in regulating myosin localization
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
key role in regulating myosin localization
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
the enzymes anterior localization is dynamically regulated during chemotaxis, phagocytosis, and other polarized cell motility events via direct binding to F-actin
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
specific isozyme A for the heavy chain of myosin II
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
drives filament disassembly in vitro
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
phosphorylates primarly threonine residues
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
key role in regulating myosin localization
-
?
ATP + RKKFGESEKTKTKEFL-amide
?
low activity
-
-
?
ATP + RKKFGESEKTKTKEFL-amide
?
catalytic domain
-
-
?
ATP + RKKFGESEKTKTKEFL-amide
?
-
isozyme myosin II heavy chain kinase A
-
-
?
ATP + RKKFGESEKTKTKEFL-amide
?
synthetic peptide MH-3
-
-
?
ATP + synthetic peptides
?
-
variations in length, and number, location and kind of basic residues of the basic sequence of peptide GRGRSSVYS, overview
-
-
?
ATP + synthetic peptides
?
-
peptide MH-3, corresponding to myosin II heavy chain from residues 2020 to 2035 except that Ser-2026 and Thr-2031 have been replaced by alanine
-
-
?
ATP + YAYDTRYRR
?
catalytic domain of the enzyme
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
phosphorylation of sites within the MHC alpha-helical, coiled-coil tail by MHCK A
-
-
?
ATP + [myosin-heavy-chain]
ADP + [myosin-heavy-chain]phosphate
-
-
-
?
ATP + [myosin-heavy-chain]
ADP + [myosin-heavy-chain]phosphate
-
-
-
-
?
additional information
?
-
enzyme contains several SH3-binding domains
-
-
?
additional information
?
-
-
the Mg2+-ATPase activity of the substrate myosin I is increased by its phosphorylation and the binding of F-actin
-
-
?
additional information
?
-
-
the Mg2+-ATPase activity of the substrate myosin I is increased by its phosphorylation and the binding of F-actin
-
-
?
additional information
?
-
-
the Mg2+-ATPase activity of the substrate myosin I is increased by its phosphorylation and the binding of F-actin
-
-
?
additional information
?
-
enzyme possesses binding domains for the Ras-related GTP-binding proteins Cdc42 and Rac
-
-
?
additional information
?
-
-
the Mg2+-ATPase activity of the substrate myosin II is inhibited in vitro by its phosphorylation
-
-
?
additional information
?
-
-
localization of autophosphorylation sites
-
-
?
additional information
?
-
enzyme possesses binding domains for the Ras-related GTP-binding proteins Cdc42 and Rac
-
-
?
additional information
?
-
the Mg2+-ATPase activity of the substrate myosin II is inhibited in vitro by its phosphorylation
-
-
?
additional information
?
-
-
the Mg2+-ATPase activity of the substrate myosin II is inhibited in vitro by its phosphorylation
-
-
?
additional information
?
-
O76739
localization of autophosphorylation sites
-
-
?
additional information
?
-
localization of autophosphorylation sites
-
-
?
additional information
?
-
localization of autophosphorylation sites
-
-
?
additional information
?
-
biochemical mechanism for the spatial regulation of myosin II filament disassembly acts via MHCK A activation by actin
-
-
?
additional information
?
-
-
biochemical mechanism for the spatial regulation of myosin II filament disassembly acts via MHCK A activation by actin
-
-
?
additional information
?
-
C-terminal phosphorylation of myosin heavy chain is required for regulation of myosin II filament assembly, regulation mechanism
-
-
?
additional information
?
-
-
C-terminal phosphorylation of myosin heavy chain is required for regulation of myosin II filament assembly, the 3 isozymes MHCK A, MHCK B, and MHCK C show differential localization patterns in living cells
-
-
?
additional information
?
-
MHCK A performs autophosphorylation
-
-
?
additional information
?
-
-
MHCK A performs autophosphorylation
-
-
?
additional information
?
-
MHCK A contains active RasB, and is the predominant exchange factor for RasB. RasGEF Q can bind to F-actin and has the potential to form complexes with MHCK A, overview
-
-
?
additional information
?
-
-
MHCK A contains active RasB, and is the predominant exchange factor for RasB. RasGEF Q can bind to F-actin and has the potential to form complexes with MHCK A, overview
-
-
?
additional information
?
-
substrate specificity of the MHCK A catalytic domain: a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by MHCK A. Phosphorylation by MHCK A is enhanced 2 to 4fold by basic residues in the P+2, P+3 and P+4 positions, with a strong preference for threonine as the phosphoacceptor amino acid, overview
-
-
?
additional information
?
-
substrate specificity of the MHCK A catalytic domain: a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by MHCK A. Phosphorylation by MHCK A is enhanced 2 to 4fold by basic residues in the P+2, P+3 and P+4 positions, with a strong preference for threonine as the phosphoacceptor amino acid, overview
-
-
?
additional information
?
-
-
substrate specificity of the MHCK A catalytic domain: a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by MHCK A. Phosphorylation by MHCK A is enhanced 2 to 4fold by basic residues in the P+2, P+3 and P+4 positions, with a strong preference for threonine as the phosphoacceptor amino acid, overview
-
-
?
additional information
?
-
substrate specificity of the MHCK B catalytic domain: a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by MHCK B. Phosphorylation by MHCK B is further enhanced 8fold by a basic residue in the P+2 position, strong preference for threonine as the phosphoacceptor amino acid, overview
-
-
?
additional information
?
-
substrate specificity of the MHCK B catalytic domain: a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by MHCK B. Phosphorylation by MHCK B is further enhanced 8fold by a basic residue in the P+2 position, strong preference for threonine as the phosphoacceptor amino acid, overview
-
-
?
additional information
?
-
-
substrate specificity of the MHCK B catalytic domain: a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by MHCK B. Phosphorylation by MHCK B is further enhanced 8fold by a basic residue in the P+2 position, strong preference for threonine as the phosphoacceptor amino acid, overview
-
-
?
additional information
?
-
the enzyme also exhibits ATPase and unspecific Ser/Thr protein kinase activities
-
-
?
additional information
?
-
-
the enzyme also exhibits ATPase and unspecific Ser/Thr protein kinase activities
-
-
?
additional information
?
-
the enzyme performs autophosphorylation at Thr825
-
-
?
additional information
?
-
-
the enzyme performs autophosphorylation at Thr825
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [myosin II heavy-chain]
ADP + [myosin II heavy-chain] phosphate
-
-
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
increased activity during chemotaxis
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
intramolecular autophosphorylation
-
?
ATP + myosin heavy chain kinase
ADP + myosin heavy chain kinase phosphate
increased activity during chemotaxis
-
?
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
-
-
-
?
ATP + myosin heavy-chain
ADP + myosin heavy chain phosphate
role of RasGEF Q in regulating myosin II function through MHCK A, overview
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
reaction in regulatory contractile activity in Dictyostelium discoideum
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
involved in regulation of myosin II filament assembly
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
involved in regulation of myosin II filament assembly
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
increased activity during chemotaxis
-
?
ATP + myosin I heavy chain
ADP + myosin I heavy chain phosphate
-
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
involved in regulation of myosin II filament assembly
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
involved in regulation of myosin II filament assembly
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
key role in regulating myosin localization
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
key role in regulating myosin localization
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
the enzymes anterior localization is dynamically regulated during chemotaxis, phagocytosis, and other polarized cell motility events via direct binding to F-actin
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
-
?
ATP + myosin II heavy chain
ADP + myosin II heavy chain phosphate
-
key role in regulating myosin localization
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
?
ATP + [myosin heavy-chain]
ADP + [myosin heavy-chain] phosphate
-
-
-
?
ATP + [myosin-heavy-chain]
ADP + [myosin-heavy-chain]phosphate
-
-
-
?
ATP + [myosin-heavy-chain]
ADP + [myosin-heavy-chain]phosphate
-
-
-
-
?
additional information
?
-
biochemical mechanism for the spatial regulation of myosin II filament disassembly acts via MHCK A activation by actin
-
-
?
additional information
?
-
-
biochemical mechanism for the spatial regulation of myosin II filament disassembly acts via MHCK A activation by actin
-
-
?
additional information
?
-
C-terminal phosphorylation of myosin heavy chain is required for regulation of myosin II filament assembly, regulation mechanism
-
-
?
additional information
?
-
-
C-terminal phosphorylation of myosin heavy chain is required for regulation of myosin II filament assembly, the 3 isozymes MHCK A, MHCK B, and MHCK C show differential localization patterns in living cells
-
-
?
additional information
?
-
MHCK A contains active RasB, and is the predominant exchange factor for RasB. RasGEF Q can bind to F-actin and has the potential to form complexes with MHCK A, overview
-
-
?
additional information
?
-
-
MHCK A contains active RasB, and is the predominant exchange factor for RasB. RasGEF Q can bind to F-actin and has the potential to form complexes with MHCK A, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
additional information
Mg2+
required, Mg2+ is coordinated in an octahedral arrangement by the side chains of Asp766 and Gln768, the main-chain carbonyl group of Pro767, and three water molecules
Mg2+
required, the Mg2 binding sites are regulatory, because millimolar concentrations of Mg2+, in excess of that required to bind to ATP, are required for A-CAT to exhibit maximal catalytic activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Positively charged polypeptides
-
strong inhibition, e.g. poly-(D-Lys), poly-(L-Lys), poly-(L-Arg) of different molecular weights
-
Ca2+/calmodulin
calmodulin-binding site: amino acid residues 51-80; competes with phospholipids
-
Ca2+/calmodulin
binds to the enzyme and inhibits its activation by acidic phospholipids but not by guanosine 5'-3-O-(thio)triphosphate-Rac1
-
KCl
-
strong, 90% inhibition at 60 mM, complete inhibition at 100 mM
additional information
-
strong inhibition of phosphorylation activity by increasing ionic strength
-
additional information
autoinhibitory domains, overview, autoinhibition is reversed by Rac
-
additional information
-
no inhibition by Ca2+; no inhibition by cAMP or cGMP
-
additional information
-
ionic strength has no effect on autophosphorylation activity; strong inhibition of phosphorylation activity by increasing ionic strength
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DNA
-
autophosphorylation activity is increased 5-10fold in a Ca2+-independent manner
G-actin
slight activation of MHCK A, activation is abolished by latrunculin A, which depolymerizes the actin filament
-
heparin
-
autophosphorylation activity is increased 5-10fold in a Ca2+-independent manner
phosphatidylinositol 4,5-bisphosphate
10fold activation of autophosphorylation and kinase activity
acidic phospholipids
-
enhance the activation of the enzyme by autophosphorylation
-
acidic phospholipids
functions cooperatively with acidic phospholipids to associate the enzyme with membranes
-
acidic phospholipids
enhance the activation of the enzyme by autophosphorylation
-
F-actin
about 40fold activation of myosin heavy chain kinase A, structure and mechanism, stimulation via enzyme autophosphorylation
-
F-actin
i.e. filamentous actin, from rabbit muscle, about 40fold activation, coiled-coil domain binding structure and mechanism, overview, the enzyme's coiled-coil structure mediates its oligomerization, cellular localization, and actin-binding activity of the MHCK A
-
guanosine 5'-3-O-(thio)triphosphate-Rac1
functions cooperatively with acidic phospholipids to associate the enzyme with membranes
-
guanosine 5'-3-O-(thio)triphosphate-Rac1
i.e. GTPgammaS-Rac1
-
guanosine 5'-3-O-(thio)triphosphate-Rac1
10fold activation of autophosphorylation and kinase activity
-
phosphatidylinositol
10fold activation of autophosphorylation and kinase activity
phosphatidylserine
-
stimulation only of the autophosphorylated enzyme
phosphatidylserine
-
stimulates the enzymes autophosphorylation activity
phosphatidylserine
10fold activation of autophosphorylation and kinase activity
Phospholipid vesicles
-
autophosphorylation activity is increased 5-10fold in a Ca2+-independent manner
-
Phospholipid vesicles
-
composed of phosphatidylserine or phosphatidylinositol, not phosphatidylcholine
-
Phospholipid vesicles
-
autophosphorylation activity is increased 5-10fold in a Ca2+-independent manner
-
Phospholipid vesicles
-
composed of phosphatidylserine or phosphatidylinositol, not phosphatidylcholine
-
Rac
activation of autophosphorylation and kinase activity only in presence of phosphatidylserine, activates only the fully phosphorylated enzyme
-
additional information
no activation by phosphatidylcholine and phosphatidylethanolamine
-
additional information
-
enzyme is stimulated by its autophosphorylation
-
additional information
-
enzyme is stimulated by its autophosphorylation
-
additional information
-
enzyme is stimulated by its autophosphorylation
-
additional information
-
enzyme is stimulated by its autophosphorylation
-
additional information
enzyme is stimulated by its autophosphorylation
-
additional information
no activation by phosphatidylcholine and sphingosine
-
additional information
association with the actin cytoskeleton causes a drastic increase in the autophosphorylation activity of MHCK A, which is then activated
-
additional information
-
association with the actin cytoskeleton causes a drastic increase in the autophosphorylation activity of MHCK A, which is then activated
-
additional information
autophosphorylation at Thr825 activates MHCK A at least 50fold, dephosphorylation of the residue reduces the activity
-
additional information
-
autophosphorylation at Thr825 activates MHCK A at least 50fold, dephosphorylation of the residue reduces the activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.098
AKRVSMMR
in presence of guanosine 5'-3-O-(thio)triphosphate-Rac1, pH 7.0
0.064
GRGRSSVYS
-
phospholipid-bound, unphosphorylated enzyme, pH 7.0, 30°C
0.15
GRGRSSVYS
-
recombinant wild-type catalytic domain, pH 7.0, 30°C
0.2
GRGRSSVYS
-
recombinant T632A mutant catalytic domain, pH 7.0, 30°C
0.017
GRSARVSTYA
in presence of guanosine 5'-3-O-(thio)triphosphate-Rac1, pH 7.0
0.0007
myosin IA
-
phospholipid-bound, unphosphorylated enzyme, pH 7.0, 30°C
-
0.0005
myosin IB
-
phospholipid-bound, unphosphorylated enzyme, pH 7.0, 30°C
-
additional information
additional information
-
catalytic domain mutants
-
additional information
additional information
-
Km values for derivatives of peptide GRGRSSVYS
-
additional information
additional information
F-actin binding kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5
AKRVSMMR
in presence of guanosine 5'-3-O-(thio)triphosphate-Rac1, pH 7.0
105
GRGRSSVYS
-
recombinant T632A mutant catalytic domain, pH 7.0, 30°C
4.6
GRSARVSTYA
in presence of guanosine 5'-3-O-(thio)triphosphate-Rac1, pH 7.0
additional information
additional information
O76739
catalytic domain, several substrates
-
additional information
additional information
catalytic domain, several substrates
-
additional information
additional information
catalytic domain, several substrates
-
additional information
additional information
-
catalytic domain mutants
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition by positively charged polypeptides
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.98
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.5
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
6 - 9
-
about half-maximal activity at pH 6.0, about 90% of maximal activity at pH 7.0 and pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
22
25
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
myosin I heavy chain kinase
-
-
brenda
gene MHKA or MHCKA, myosin heavy chain kinase A
SwissProt
brenda
gene MHKB or MHCKB, myosin heavy chain kinase B
SwissProt
brenda
two heavy chain kinases: one in growth-phase cells and one in starved, developing cells
-
-
brenda
the Ca2+/calmodulin dependent heavy chain kinase has several properties in common with the family of type II calmodulin-dependent protein kinases
-
-
brenda
two myosin heavy-chain kinases: a Ca2+/calmodulin dependent and a Ca2+/calmodulin independent enzyme
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
starved-developing cells contain enzyme form MHCK B
brenda
-
overexpresssing cells show slower growth and increased cell size
brenda
-
overexpresssing cells show slower growth and increased cell size
-
brenda
additional information
enzyme expression only during development
brenda
additional information
-
enzyme expression only during development
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
MHCK A associates with the cytoskeleton and localizes to the cell cortex
brenda
-
binding to the plasma membrane enhances the activity of unphosphorylated enzyme 20fold, substrate myosin I
brenda
association of the enzyme to membranes enhances the activity
brenda
additional information
translocation of the enzyme within the cell responding to outer signals
-
brenda
additional information
-
translocation of the enzyme within the cell responding to outer signals
-
brenda
additional information
-
MHCK A is localized to actin-rich regions in mitotic cells
-
brenda
additional information
MHCK A is localized to actin-rich regions in mitotic cells
-
brenda
additional information
-
the 3 isozymes MHCK A, MHCK B, and MHCK C show differential localization patterns in living cells, overview
-
brenda
additional information
the enzyme's coiled-coil structure mediates its oligomerization, cellular localization, and actin-binding activity of the MHCK A
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
alpha-kinases transfer the gamma-phosphate of ATP to protein substrates through an aspartylphosphate intermediate
evolution
myosin II heavy chain kinase A is a member of the atypical alpha-kinase family
malfunction
removal of the N-rich region severely compromises MHC phosphorylation by the catalytic domain. Removal of both the N-rich and WD-repeat domains renders the catalytic domain barely able to phosphorylate MHC above detectable levels, whereas the truncation containing the N-rich region can still use MHC as a substrate, albeit at about 30% of that displayed by the full-length kinase. But the innate kinase activity of the catalytic domain is not lost upon removal of the N-rich region and/or the WD-repeat domain of MHCK-B since all three versions of MHCK-B phosphorylated MH-1 peptide to the same level
malfunction
the catalytic activity of A-CAT, the alpha-kinase domain of MHCKA comprising residues 552-841, is severely inhibited by the removal of a disordered C-terminal tail residues 806-841
physiological function
heavy chain phosphorylation plays a central role in regulating myosin II bipolar filament assembly in Dictyostelium
physiological function
myosin II heavy chain kinase A, MHCK A, disrupts the assembly and cellular activity of bipolar filaments of myosin II by phosphorylating sites within its alpha-helical, coiled-coil tail
physiological function
the enzyme phosphorylates sites in the myosin II tail that block filament assembly
additional information
ADP is bound at the active site and invariant Asp766 at the active site is phosphorylated in the crysstallized MHCK A. The aspartylphosphate group is exposed to the solvent within an active-site pocket that might function as a docking site for substrates. Access to the aspartylphosphate is regulated by a conformational switch in a loop that binds to a Mg2+ ion, providing a mechanism that allows alpha-kinases to sense and respond to local changes in Mg2+ concentration. Access to the active-site pocket was regulated by a C-terminal glycine-rich loop that bound to Mg2+ and switched between two distinct conformations. The invariant Asp766 residue is located at the center rear of the active site where it interacted with phosphate, the alpha-phosphate of AMP, and Mg2+ in the active-site pocket
additional information
-
ADP is bound at the active site and invariant Asp766 at the active site is phosphorylated in the crysstallized MHCK A. The aspartylphosphate group is exposed to the solvent within an active-site pocket that might function as a docking site for substrates. Access to the aspartylphosphate is regulated by a conformational switch in a loop that binds to a Mg2+ ion, providing a mechanism that allows alpha-kinases to sense and respond to local changes in Mg2+ concentration. Access to the active-site pocket was regulated by a C-terminal glycine-rich loop that bound to Mg2+ and switched between two distinct conformations. The invariant Asp766 residue is located at the center rear of the active site where it interacted with phosphate, the alpha-phosphate of AMP, and Mg2+ in the active-site pocket
additional information
mechanism for targeting myosin II heavy chain phosphorylation by myosin heavy chain kinase B, overview. An intrinsically unstructured, and asparagine-rich, region of a MHCK-B can mediate specific targeting of the kinase to phosphorylate myosin II heavy chain involving a direct binding interaction with myosin II filaments, while the the WD repeat domain is not absolutely required in MHCK-B substrate targeting, in contrast to isozyme MHCK-A. The N-rich region facilitates phosphorylation of MHC by binding directly to myosin II filaments
additional information
the phosphate-pocket functions as a positive allosteric binding site, the phosphorylated Thr825 activates alpha-kinase domain by providing a covalently tethered ligand for the phosphate-pocket, mechanism modeling
additional information
-
the phosphate-pocket functions as a positive allosteric binding site, the phosphorylated Thr825 activates alpha-kinase domain by providing a covalently tethered ligand for the phosphate-pocket, mechanism modeling
Show AA Sequence and Transmembrane Helices (243 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
107000
130000
145000
x * 145000, phosphorylated MHCK A, SDS-PAGE, x * 130000, unphosphorylated MHCK A, SDS-PAGE
50000
-
10 * 50000, SDS-PAGE, asymmetric complex with an axial ratio calculated for prolate ellipsoid of 6.1
79300
x * 79300, determined from amino acid sequence, difference to MW of 97 kDa determined by SDS-PAGE is due to high proline content
130000
x * 145000, phosphorylated MHCK A, SDS-PAGE, x * 130000, unphosphorylated MHCK A, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
-
10 * 50000, SDS-PAGE, asymmetric complex with an axial ratio calculated for prolate ellipsoid of 6.1
monomer
additional information
?
x * 79300, determined from amino acid sequence, difference to MW of 97 kDa determined by SDS-PAGE is due to high proline content
?
x * 145000, phosphorylated MHCK A, SDS-PAGE, x * 130000, unphosphorylated MHCK A, SDS-PAGE
additional information
the enzyme's coiled-coil structure mediates its oligomerization, cellular localization, and actin-binding activity of the MHCK A
additional information
MHCK A protein consists of an N-terminal coiled-coil domain, a central kinase domain, and a C-terminal WD-repeat domain, domain structures comparisons of the catalytic alpha-kinase domain to the one from Mus musculus, overview
additional information
-
MHCK A protein consists of an N-terminal coiled-coil domain, a central kinase domain, and a C-terminal WD-repeat domain, domain structures comparisons of the catalytic alpha-kinase domain to the one from Mus musculus, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
MHCK A performs autophosphorylation, facilitated by F-actin requiring the coiled coil domain of the enzyme
phosphoprotein
association with the actin cytoskeleton causes a drastic increase in the autophosphorylation activity of MHCK A, which is then activated
phosphoprotein
15 to 20 autophosphorylation sites in MHCK-B reside in the N-rich region of the kinase. Autophosphorylation of full-length MHCK-B has no effect on the kinase activity of the enzyme
phosphoprotein
autophosphorylation at Thr825 activates MHCK A at least 50fold, dephosphorylation of the residue reduces the activity. The phosphorylated Thr825 docks intramolecularly into the phosphate-pocket. Allosteric activation is predicted to involve a conformational change in Arg734, which bridges the bound phosphate to Asp762 in a key active site loop
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S627A
-
catalytic domain mutant, mutation of potential phosphorylation site, no phosphorylation of the mutant, reduced activity, increased Km values for the substrates, but higher activity than the unphosphorylated wild-type enzyme
S627D
-
catalytic domain mutant, mutation of potential phosphorylation site, no phosphorylation of the mutant, reduced activity, increased Km values for the substrates, the acidic residue cannot substitute for phospho-Ser
S627E
-
catalytic domain mutant, mutation of potential phosphorylation site, no phosphorylation of the mutant, reduced activity, increased Km values for the substrates, the acidic residue cannot substitute for phospho-Ser
T631A
-
catalytic domain mutant, mutation of a conserved Thr residue, full phosphorylation of the mutant, reduced activity, increased Km values for the substrates
T631D
-
catalytic domain mutant, mutation of a conserved Thr residue, 95% phosphorylation of the mutant, highly reduced activity, increased Km values for the substrates
T631E
-
catalytic domain mutant, mutation of a conserved Thr residue, no phosphorylation of the mutant, highly reduced activity, highly increased Km values for the substrates
T632A
-
catalytic domain mutant, mutation of a nonconserved Thr residue, full phosphorylation of the mutant, increased activity, only slightly increased Km values for the substrates
T632D
-
catalytic domain mutant, mutation of a nonconserved Thr residue, 80% phosphorylation of the mutant, reduced activity, increased Km values for the substrates
T632E
-
catalytic domain mutant, mutation of a nonconserved Thr residue, full phosphorylation of the mutant, reduced activity, increased Km values for the substrates
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
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
T825S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
D663A
the mutant shows about 3% activity compared to the wild type enzyme
D766S
site-directed mutagenesis of the central active site residue, inactive mutant
additional information
-
construction of single, double, and triple MHCK knockout cell lines concerning the 3 isozymes MHCK A, MHCK B, and MHCK C, the mutant cells defects in cytokinesis and myosin II overassembly increasing with the number of mutations, overview
additional information
the truncation mutant DELTAcoil-MHCK A comprising residues 1-498 is not affected in its autophosphorylation rate by F-actin
additional information
the truncation mutant DELTAcoil-MHCK A comprising residues 1-498 is not affected in its autophosphorylation rate by F-actin
additional information
-
the truncation mutant DELTAcoil-MHCK A comprising residues 1-498 is not affected in its autophosphorylation rate by F-actin
additional information
overexpression of the RasGEF Q GEF domain activates RasB, causes enhanced recruitment of MHCK A to the cortex, and leads to cytokinesis defects in suspension phenocopying cells expressing constitutively active RasB, and myosin-null mutants, phenotype, overview. Cells overexpressing the GEF domain show at least 2fold higher levels of MHCK A associated with the cytoskeletal fractions
additional information
-
overexpression of the RasGEF Q GEF domain activates RasB, causes enhanced recruitment of MHCK A to the cortex, and leads to cytokinesis defects in suspension phenocopying cells expressing constitutively active RasB, and myosin-null mutants, phenotype, overview. Cells overexpressing the GEF domain show at least 2fold higher levels of MHCK A associated with the cytoskeletal fractions
additional information
version with deleted WD repeat domain: unable to phosphorylate myosin heavy chain to a significant level, phosphorylates MH-1 peptide
additional information
-
version with deleted WD repeat domain: unable to phosphorylate myosin heavy chain to a significant level, phosphorylates MH-1 peptide
additional information
generation of a DELTA809 truncation mutant, phosphothreonine and the QQG(p)TMVMPD peptide restore the phosphorylation and also the ATPase activity of the mutant alpha-kinade domain, but mutations R734A and D762A abolish the ability of phosphothreonine to activate mutant alpha-kinase domain DELTA809
additional information
-
generation of a DELTA809 truncation mutant, phosphothreonine and the QQG(p)TMVMPD peptide restore the phosphorylation and also the ATPase activity of the mutant alpha-kinade domain, but mutations R734A and D762A abolish the ability of phosphothreonine to activate mutant alpha-kinase domain DELTA809
additional information
generation of the MHCKB truncation lacking only the WD-repeat domain and of a mutant lacking the N-rich region. Cells overexpressing the MHCK mutant lacking only the WD-repeat domain exhibit cytokinesis defects and decreased myosin II assembly
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
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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% glycerol, 3 months stable and less than 20% loss of activity within 6 months
-
0°C, further purified Ca2+/calmodulin-dependent isozyme, complete loss of activity within 1 day
-
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
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
recombinant His-tagged catalytic domain of MHCK C, expressed in Escherichia coli
recombinant His-tagged catalytic domains, wild-type and mutants, from Sf9 insect cells
-
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
recombinant peptides of the enzymes N-terminus from Escherichia coli, His- or FLAG-tagged, and recombinant enzyme from Sf9 insect cells
solubilized by high-salt extraction, affinity chromatography, 4600fold, to homogeneity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cells overexpressing GFP-GEF have both unphosphorylated and autophosphorylated MHCK A
cloning of wild-type and mutants of the catalytic domain of myosin I heavy chain kinase as His-tagged proteins and expression in Spodoptera frugiperda Sf9 cells via baculovirus infection system
-
construction of His-tagged or FLAG-tagged N-terminal enzyme peptides by site directed mutagenesis for introduction of start and stop codons, expression in Escherichia coli BL21(DE3)
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
DNA sequence determination and analysis, gene MHCK possesses all of the domains characteristic of members of the protein kinase C family
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)
expression of the His-tagged catalytic domain of MHCK A in Escherichia coli BL21(DE3)
expression of the His-tagged catalytic domain of MHCK C in Escherichia coli BL21(DE3)
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
subcloning and expression in Escherichia coli, expression in Spodoptera frugiperda Sf9 cells via baculovirus infection system
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REF.
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Acanthamoeba castellanii
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Acanthamoeba castellanii
brenda
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Gallus gallus
brenda
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Bos taurus
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brenda
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Identification of a new mechanism for targeting myosin II heavy chain phosphorylation by Dictyostelium myosin heavy chain kinase B
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Dictyostelium discoideum (P90648)
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Dictyostelium discoideum (P42527)
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Dictyostelium discoideum (P42527)
brenda
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