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Information on EC 5.6.1.8 - myosin ATPase
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5.6.1.8 myosin ATPaseIUBMB Comments
Proteins of the contractile apparatus of muscle and nonmuscle cells; myosin molecule consists of two heavy chains (about 200 kDa) and two pairs of light chains (15--27 kDa). The head region of the heavy chain contains actin- and ATP-binding sites. ATP hydrolysis provides energy for actomyosin contraction.
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Word Map
- 5.6.1.8
-
contractile
- cardiac
- fiber
- cytoskeleton
-
tension
- troponin
- ventricular
- f-actin
- myocardial
- artery
- hypertrophy
- myofibrillar
- junction
- microtubule
- cardiomyopathy
-
isometric
- cardiomyocytes
- myotubes
- myocytes
- calmodulin
-
striated
- soleus
-
cytokinesis
- myoblasts
-
myogenic
- sarcomere
-
myogenesis
-
actin-binding
-
sliding
- desmin
- dictyostelium
-
muscle-specific
- sarcoplasmic
-
slide
-
stiff
- rhoa
- ventricle
-
digitorum
- lateralis
-
vastus
- extensor
-
unload
- kinesins
- myocarditis
-
rock
-
twitch
- adhesions
- longus
-
microfilaments
-
myofibers
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
=
+
+
+
+
myosin bound to actin filament at position n
=
+
+
myosin bound to actin filament at position n+1
Synonyms
myosin, actomyosin, heavy meromyosin, actomyosin atpase, nmiib, myosin-2, myosin-atpase, natural actomyosin, myosin 2, myosin ii atpase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
actomyosin
actomyosin ATPase
EC 3.6.1.32
-
-
formerly
-
EC 3.6.4.1
-
-
formerly
-
matpase
-
-
-
-
myofibril ATPase
myosin
myosin ATPase
myosin II ATPase
myosin S1 ATPase
myosin-ATPase
actomyosin
-
-
-
-
myosin S1 ATPase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + myosin bound to actin filament at position n = ADP + phosphate + myosin bound to actin filament at position n+1
ATP + H2O + myosin bound to actin filament at position n = ADP + phosphate + myosin bound to actin filament at position n+1
terminal phosphate of triphosphate is removed
-
ATP + H2O + myosin bound to actin filament at position n = ADP + phosphate + myosin bound to actin filament at position n+1
kinetics
-
ATP + H2O + myosin bound to actin filament at position n = ADP + phosphate + myosin bound to actin filament at position n+1
kinetics and mechanical behaviour
-
ATP + H2O + myosin bound to actin filament at position n = ADP + phosphate + myosin bound to actin filament at position n+1
kinetics of activtation by actin
-
ATP + H2O + myosin bound to actin filament at position n = ADP + phosphate + myosin bound to actin filament at position n+1
combined quantum/classical mechanics study and catalytic mechanism, detailed overview and analysis
ATP + H2O + myosin bound to actin filament at position n = ADP + phosphate + myosin bound to actin filament at position n+1
the actin-activated release of inorganic phosphate from the acto myosin-ADP-phosphate complex is the rate-limiting step in the steady-state actomyosin ATPase cycle
ATP + H2O + myosin bound to actin filament at position n = ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphonic ester
-
-
-
-
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (actin-translocating)
Proteins of the contractile apparatus of muscle and nonmuscle cells; myosin molecule consists of two heavy chains (about 200 kDa) and two pairs of light chains (15--27 kDa). The head region of the heavy chain contains actin- and ATP-binding sites. ATP hydrolysis provides energy for actomyosin contraction.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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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 + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
CTP + H2O + myosin bound to actin filament at position n
CDP + phosphate + myosin bound to actin filament at position n+1
GTP + H2O + myosin bound to actin filament at position n
GDP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ITP + H2O + myosin bound to actin filament at position n
IDP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
UTP + H2O + myosin bound to actin filament at position n
UDP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
nucleoside triphosphates are hydrolyzed in decreasing order: GTP, ITP, CTP, ATP, UTP
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
nucleoside triphosphates are hydrolyzed in the following order: GTP, ITP, CTP, ATP, UTP
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
ATP binding site of myosin and catalytically active conformation, modeling and analysis of crystal structure, PDB 1VOM
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
P13538; P02609; P02604
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
Delivering of F-actin to the lamella of migrating fibroblasts
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
Lethocerus griseus
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
246975, 246976, 246978, 246983, 246995, 246996, 246997, 247001, 247004, 247005, 733515, 733791, 735020, 749738, 749747, 749819, 749998, 751659
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
CTP + H2O + myosin bound to actin filament at position n
CDP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
CTP + H2O + myosin bound to actin filament at position n
CDP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
additional information
?
-
during its contraction cycle, the myosin motor catalyzes the hydrolysis of ATP
-
-
?
additional information
?
-
P13538; P02609; P02604
myosin head (myosin subfragment 1, S1) consists of two major structural domains, the motor (or catalytic) domain and the regulatory domain. Functioning of the myosin head as a molecular motor is believed to involve a rotation of the regulatory domain (lever arm) relative to the motor domain during the ATPase cycle. This rotation can be accompanied by an interaction between the motor domain and the C-terminus of the essential light chain associated with the regulatory domain. During rotation, the regulatory domain acts as a semi-rigid lever arm, which amplifies and transmits conformational changes occurring in the motor domain during ATP hydrolysis, the sliding velocity of actin filaments in the in vitro motility assay strongly depends on the length of the lever arm. The essential light chain associated with the regulatory domain may play a crucial role in the motor function of the myosin head, taking part in the overall stabilization of the S1 molecule during the ATPase cycle
-
-
?
additional information
?
-
-
contraction of free-floating-fibroblast-populated collagen lattice through elongated fibroblasts and rapid myosin ATPase, requiring tyrosine phosphorylation. The mechanism for attached-delayed-released-fibroblast-populated collagen lattice contraction is through cell contraction by sustained myosin ATPase, involving tyrosine dephosphorylation
-
-
?
additional information
?
-
-
kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates. The results are consistent with a dual rate-limitation model in which the rate of force recovery is limited by both NTP cleavage and phosphate release, with their relative contributions and apparent rate constants influenced by an intervening rapid force-generating transition
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
nucleoside triphosphates are hydrolyzed in the following order: GTP, ITP, CTP, ATP, UTP
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
P13538; P02609; P02604
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
Delivering of F-actin to the lamella of migrating fibroblasts
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
Lethocerus griseus
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
246975, 246976, 246978, 246983, 246995, 246996, 246997, 247001, 247004, 247005, 733515, 733791, 735020, 749738, 749747, 749819, 749998, 751659
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
additional information
?
-
during its contraction cycle, the myosin motor catalyzes the hydrolysis of ATP
-
-
?
additional information
?
-
P13538; P02609; P02604
myosin head (myosin subfragment 1, S1) consists of two major structural domains, the motor (or catalytic) domain and the regulatory domain. Functioning of the myosin head as a molecular motor is believed to involve a rotation of the regulatory domain (lever arm) relative to the motor domain during the ATPase cycle. This rotation can be accompanied by an interaction between the motor domain and the C-terminus of the essential light chain associated with the regulatory domain. During rotation, the regulatory domain acts as a semi-rigid lever arm, which amplifies and transmits conformational changes occurring in the motor domain during ATP hydrolysis, the sliding velocity of actin filaments in the in vitro motility assay strongly depends on the length of the lever arm. The essential light chain associated with the regulatory domain may play a crucial role in the motor function of the myosin head, taking part in the overall stabilization of the S1 molecule during the ATPase cycle
-
-
?
additional information
?
-
-
contraction of free-floating-fibroblast-populated collagen lattice through elongated fibroblasts and rapid myosin ATPase, requiring tyrosine phosphorylation. The mechanism for attached-delayed-released-fibroblast-populated collagen lattice contraction is through cell contraction by sustained myosin ATPase, involving tyrosine dephosphorylation
-
-
?
additional information
?
-
-
kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates. The results are consistent with a dual rate-limitation model in which the rate of force recovery is limited by both NTP cleavage and phosphate release, with their relative contributions and apparent rate constants influenced by an intervening rapid force-generating transition
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
additional information
-
uterine myosin S1 ATPase activity does not depend on the concentration of Mg2+ in the presence of 5 mM Zn2+
Mg2+
required, Mg2+ coordination sphere, binding structure, overview
Mg2+
-
required, structure of myosin-2 complex with Mg2+-ADP-metavanadate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-dibromo-6-(3,4,5-tribromo-1-methyl-1H-pyrrol-2-yl)phenol
-
2-(3,5-dibromo-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,3-dihydro-1H-pyrrole
-
-
2-(3,5-dibromo-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,5-dihydro-1H-pyrrole
-
-
2-(3,5-dichloro-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,3-dihydro-1H-pyrrole
-
-
2-(3,5-dichloro-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,5-dihydro-1H-pyrrole
-
-
2-(3,5-difluoro-2-methoxyphenyl)-1-(4-methylbenzene-1-sulfonyl)-2,5-dihydro-1H-pyrrole
-
-
2-(3,5-difluoro-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,3-dihydro-1H-pyrrole
-
-
calponin
-
25% inhibition in the presence of actin, calmodulin abolishes inhibitory effect
-
cardiac myosin binding protein-C
-
reduces actin filament velocity in concentration-dependent manner: 200 nM cMYBP-C to around 25%, 400 nM cMYBP-C to almost 0%
-
D2O
-
about 50% inhibition of enzyme, increase in maximum isometric force P0 by about 20%
Fluorescein 5'-isothiocyanate
-
90% of enzyme activity is lost with the incorporation of 2.6 mol of reagent /mol of myosin, fluorescent label is mainly incorporated into the myosin heavy chain
heparin
-
heparins of molecular weights from 1.75 kDa to 11.6 kDa are competitive inhibitors
HgCl2
-
uncompetitive, 50 nM, 15% inhibition, 400 nM, 80% inhibition, DTT or glutathione protect, full activity is restored by 500 nM DTT or glutathione
KF
-
in the presence of fluoride Mg2+ and MgADP- form a stable S1-MgADP-MgFx complex, that traps the active site of S 1, Mg2+ may occupy the gamma-phosphate position in the ATP binding site of S 1
myosin
-
aging results in chemical changes in myosin (probably oxidation of cysteines) that have inhibitory effects on the actin-activated myosin ATPase
-
N-ethylmaleimide
-
in the absence of divalent cations and in the presence of K+ ions
N-[1-(2-methoxyphenyl)-4-(trimethylsilyl)but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dibromo-2-methoxyphenyl)-2-(trimethylsilyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dibromo-2-methoxyphenyl)-4-(trimethylsilyl)but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dibromo-2-methoxyphenyl)-but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dibromo-2-methoxyphenyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dichloro-2-methoxyphenyl)-2-(trimethylsilyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dichloro-2-methoxyphenyl)-4-(trimethylsilyl)but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dichloro-2-methoxyphenyl)-but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dichloro-2-methoxyphenyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-difluoro-2-methoxyphenyl)-2-(trimethylsilyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-difluoro-2-methoxyphenyl)-4-(trimethylsilyl)but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-difluoro-2-methoxyphenyl)-but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-difluoro-2-methoxyphenyl)buta-2,3-dien-1-yl]-4-methylbenzene-1-sulfonamide
-
-
N-[1-(methoxyphenyl)-2-(trimethylsilyl)-buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
p-mercuribenzoate
-
enzyme activity increases until 40% of SH-groups are titrated, complete inhibition when all SH-groups are titrated
p-Mercuriphenyl sulfonate
-
enzyme activity increases until 40% of SH-groups are titrated, complete inhibition when all SH-groups are titrated
Pb(CH3COO)2
-
100 micromol lead acetate reduces myosin Ca2+ ATPase activity by 25%
phenylmercuric acetate
-
enzyme activity increases until 40% of SH-groups are titrated, complete inhibition when all SH-groups are titrated
Troponin
-
troponin together with tropomyosin inhibits the actomyosin ATPase activity in vitro
-
VO43-
-
phosphate analog, binds in solution to myosin and inhibits its ATPase, forming a stable inactive myosin-ADP-VO43- complex (rate constant of ADP and orthovanadate dissociation about 0.00001 s-1)
Zn2+
-
about 60% residual activity at 5 mM Zn2+. Tetrahydroxythiacalix[4]arene-tetrasulfosphonate and tetrahydroxythiacalix[4]arene-tetraphosphonate restore myosin S1 ATPase activity to the control level in the presence of 5 mM Zn2+
2,3,4-trichloro-5-(3,5-dichloro-2-methoxyphenyl)-1H-pyrrole
-
2,4,6-Trinitrobenzene sulfonate
-
inhibition of cardiac and skeletal myosin
acetone
-
strong inhibition of cardiac myosin at alkaline pH, weak inhibition of skeletal myosin at alkaline pH
acetone
-
strong inhibition of cardiac myosin at alkaline pH, weak inhibition of skeletal myosin at alkaline pH
acetone
-
strong inhibition of cardiac myosin at alkaline pH, weak inhibition of skeletal myosin at alkaline pH
acetone
-
strong inhibition of cardiac myosin at alkaline pH, weak inhibition of skeletal myosin at alkaline pH
blebbistatin
-
100 micromol reduces appearance of new graded polarity (actomyosin) bundles within the lamella 10-fold
caldesmon
-
the mechanism of smooth muscle caldesmon-tropomyosin inhibition of the elementary steps of the actomyosin ATPase. At a physiological ratio of caldesmon to actin (1 caldesmon/7 actin monomers) actomyosin ATPase is inhibited by about 75%
caldesmon
-
caldesmon molecules are located along the thin filament and inhibit in vitro the actomyosin ATPase activity
N-benzyl-p-toluenesulfonamide
-
reduces force in muscle contraction by 84% and prevents consumption of ATP during electrically stimulated contractions
tropomyosin
-
tropomyosin together with troponin inhibits the actomyosin ATPase activity in vitro
vanadate
-
decameric, noncompetitive, without actin, 50% inhibition at 0.0125 mM, in presence of 0.001 mM actin, 50% inhibition at 0.0006 mM, one V10 binding site per monomer
additional information
-
Ca2+-dependent ATPase activity and enzyme protein content in muscle are reduced by ultrasonication for 10 min at 20 mHz with 0.5-1.8 mg/ml protein, e.g. loss of 47% Ca2+-dependent enzyme activity of chicken natural actomyosin at 0.5 mg/ml protein
-
additional information
-
a new state of myosin, the super relaxed state, with a very slow ATP turnover rate in skeletal muscle shows inhibition of the myosin ATPase activity caused by binding of the myosin head to the core of the thick filament in a structural motif identified by electron microscopy
-
additional information
-
pentahalogenated 2-arylpyrrole-type alkaloids pentabromopseudilin and pentachloropseudilin represent a class of isoform-specific allosteric inhibitors of myosin ATPase. Application of the silver(I)-catalyzed cycloisomerization of N-(homopropargyl)toluene-sulfonamides to the total syntheses of the natural products and several non-natural analogues. Inhibitory effect of pentahalogenated pseudilins on myosin ATPase activity, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
arachidonic acid
-
0.0503 mM half-maximal effective concentration, 0.0263 mM half-maximal effective concentration in the presence of actin
Caffeine
-
increase in enzyme activity by 4% for non-failing, 11% for idiopathic and 10% ischemic cardiomyopathic hearts
calponin
-
1.2fold increase in myosin ATPase activity in the absence of actin
-
filamentous actinin
-
the enzyme is inhibited by increasing amount of free Mg2+ concentration above 1mM in the presence of filamentous actin, while in the absence of filamentous actinin the inhibitory effect on the enzyme activity is not observed above 1 mM free Mg2+
-
leiomodin2
-
upon its interaction with the filaments leiomodin2 decreases the actin-activated Mg2+-ATPase activity of skeletal muscle myosin
-
MCI-154
-
increase in enzyme activity by 11% for non-failing, 19% for idiopathic and 24% ischemic cardiomyopathic hearts
phalloidin F-actin
-
up to 6.8fold, fast muscle myosin, up to 2.27fold, slow muscle myosin
-
polylysine
-
activation may be related to transition from 10 S to 6 S form of myosin ATPase conformation
additional information
-
myosin II seems to be activated by a rapid actin-linked mechanism rather than slow myosin light chain phosphorylation
-
actin
-
-
actin
-
wild-type Dictyostelium actin and L236A mutant activates rabbit skeletal myosin in the presence of tropomyosin-troponin
dioxane
-
at acidic pH weak stimulation of cardiac myosin ATPase and strong activation of skeletal myosin ATPase
dioxane
-
at acidic pH weak stimulation of cardiac myosin ATPase and strong activation of skeletal myosin ATPase
F-actin
efficiently activates the steady-state ATPase activity of wild-type enzyme about 94fold from a basal value
-
F-actin
-
myosin Mg-ATPase of molluscan muscles is slightly activated by F-actin under catch state in vitro. At low Ca2+ concentration, Mg-ATPase is activated by F-actin only in the presence of dephosphorylated twitchin, a titin/connectinrelated giant protein, regulates interactions between actin and myosin filaments at low Ca2+ concentrations. When it is dephosphorylated, actin filaments tightly bind to myosin filaments, resulting in the catch state known as the state of high passive tension with very low energy consumption. In the absence of twitchin, F-actin does not bind to myosin filaments
-
F-actin
-
up to 7.5fold, fast muscle myosin, up to 3.75fold, slow muscle myosin
-
myorod
-
myorod is expressed exclusively in molluscan catch muscle and localizes on the surface of thick filaments together with twitchin and myosin. Myorod is an alternatively spliced product of themyosin heavy-chain gene that contains the C-terminal rod part of myosin and a unique N-terminal domain. Phosphorylation at the N-terminus of myorod potentiates the actin-activated Mg2+-ATPase activity of mussel myosin, no activation by unphosphorylated myorod. Actomyosin reconstitution from rabbit F-actin and mussel myosin in presence or absence of unphosphorylated or phosphorylated myorod is prepared in two modes, overview
-
myorod
-
myorod is expressed exclusively in molluscan catch muscle and localizes on the surface of thick filaments together with twitchin and myosin. Myorod is an alternatively spliced product of themyosin heavy-chain gene that contains the C-terminal rod part of myosin and a unique N-terminal domain. Phosphorylation at the N-terminus of myorod potentiates the actin-activated Mg2+-ATPase activity of rabbit myosin, no activation by unphosphorylated myorod. Actomyosin reconstitution from rabbit F-actin and rabbit myosin in presence or absence of unphosphorylated or phosphorylated myorod is prepared in two modes, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0014
ATP
-
stimulated by myosin light-chain kinase without phosphorylation, actin activated myosin ATPase
0.02
ATP
-
chimeric myosin, Dictyostelium myosin loop 2 replaced by rabbit skeletal myosin loop 2, actin activated
0.02
ATP
-
chimeric myosin, Dictyostelium myosin loop 2 replaced by rabbit skeletal myosin loop 2, actin activated
0.02
ATP
-
heavy meromyosin, isoenzyme A1A2 heterodimer, actin activated
0.06
ATP
-
chimeric myosin, Dictyostelium myosin loop 2 replaced by chicken smooth muscle myosin loop 2, actin activated
0.06
ATP
-
chimeric myosin, Dictyostelium myosin loop 2 replaced by chicken smooth muscle myosin loop 2, actin activated
0.428
ATP
wild-type S1 fragment, pH 7.0, 30°C, in presence of F-actin
additional information
additional information
-
Ca2+-activitated enzyme of soleus and plantaris is not affected by age, but enzyme activity is 16% lower in semimambraneous myofibrils from aged animals
-
additional information
additional information
-
kinetic parameters of the actomyosin interaction and actomyosin ATPase cycle by measurement techniques using small numbers of molecules instead of single-molecule measurement techniques, kinetic modeling, overview
-
additional information
additional information
kinetics measurement by stopped-flow assays, steady-state ATPase activity, and kinetc analysis using wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics measurement by stopped-flow assays, steady-state ATPase activity, and kinetc analysis using wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state Mg-ATPase activities of purified myosin, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.033
ATP
-
various isoenzymes of subfragment 1 and heavy-meromyosin, absence of actin
1.2
ATP
-
chimeric myosin, Dictyostelium myosin loop 2 replaced by chicken smooth muscle myosin loop 2, actin activated
1.85
ATP
wild-type S1 fragment, pH 7.0, 30°C, in presence of F-actin
5.7
ATP
-
chimeric myosin, Dictyostelium myosin loop 2 replaced by rabbit skeletal myosin loop 2, actin activated
17
ATP
-
myosin IA, 100-kDa fragment resulting from digestion of myosin heavy chain with alpha-chymotrypsin shows similar activity
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0919
2,3,4-tribromo-5-(3,5-dibromo-2-methoxyphenyl)-1H-pyrrole
Dictyostelium discoideum
pH not specified in the publication, 25°C
0.2745
2,3,4-trichloro-5-(3,5-dichloro-2-methoxyphenyl)-1H-pyrrole
Dictyostelium discoideum
pH not specified in the publication, 25°C
0.1254
2,4-dibromo-6-(3,4,5-tribromo-1-methyl-1H-pyrrol-2-yl)phenol
Dictyostelium discoideum
pH not specified in the publication, 25°C
0.0244
2,4-dibromo-6-(3,4,5-tribromo-1H-pyrrol-2-yl)phenol
Dictyostelium discoideum
pH not specified in the publication, 25°C
0.0472
2,4-dichloro-6-(3,4,5-tribromo-1H-pyrrol-2-yl)phenol
Dictyostelium discoideum
pH not specified in the publication, 25°C
0.1263
2,4-dichloro-6-(3,4,5-trichloro-1H-pyrrol-2-yl)phenol
Dictyostelium discoideum
pH not specified in the publication, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.005
0.01
0.027
-
actin and light chain kinase activated, phosphorylation of myosin is Ca2+ and Calmodulin-dependent
0.04
0.08
0.09
0.11
0.2
0.34
-
80 weeks old rats, activity decreases with age, Ca2+activated ATPase
0.5
0.66
-
activity value of the semimembranous muscles from rats that are cage control, Ca2+-activated
0.67
0.78
-
activity value of the semimembranous muscles from rats that are hindlimb unloaded for 4 wk, Ca2+-activated
additional information
0.08
-
activity value of the semimembranous muscles from rats that are hindlimb unloaded for 4 wk, resting
0.09
-
activity value of the semimembranous muscles from rats that are cage control, resting
0.11
-
activity value of the semimembranous muscles from rats that are hindlimb unloaded for 2 wk, resting
0.11
-
activity value of the semimembranous muscles from rats that are hindlimb unloaded for 3 wk, resting
0.67
-
activity value of the semimembranous muscles from rats that are hindlimb unloaded for 2 wk, Ca2+-activated
0.67
-
activity value of the semimembranous muscles from rats that are hindlimb unloaded for 3 wk, Ca2+-activated
additional information
-
0.094 micromol/min/mg myofibrillar dry weight, ventricle, at 20°C and pH 7.3
additional information
-
0.251 micromol/min/mg myofibrillar dry weight, atrium, at 20°C and pH 7.3
additional information
-
0.125 micromol/min/mg myofibrillar dry weight, ventricle, at 20°C and pH 7.3
additional information
-
0.039 micromol/min/mg myofibrillar dry weight, ventricle, at 20°C and pH 7.3
additional information
-
0.072 micromol/min/mg myofibrillar dry weight, atrium, at 20°C and pH 7.3
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.3
7.5
9.5
9
-
cardiac myosin at 15°C, at 15°C maximal activity is lower at acidic pH than at alkaline pH for both cardiac- and skeletal myosin
9
-
skeletal myosin at 15°C, second (lower) optimum at pH 6, U-shaped curve of pH dependency
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
6 - 9
5 - 10
-
Mg-ATPase, acidic maximum at pH 5.0, alkaline maximum at pH 9.5, high ionic strength, 0.6 M KCl
5 - 10
-
Ca-ATPase, acidic maximum at pH 5.0, alkaline maximum (higher) at pH 9.5, high ionic strength, 0.6 M KCl
6 - 9
-
myosin B Ca2+-ATPase, U-shaped curve, minimum at pH 7, second maximum (lower) at pH 6
6 - 9
-
myosin B, EDTA-activated-ATPase, activity increases with rising pH, strong decrease above pH 9
6 - 9
-
myosin B, Mg2+-ATPase, little activity increase until pH 7, decrease above pH 9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 37
-
cardiac myosin activity increases steadily at acidic pH, at alkaline pH activity increases between 0 and 10°C and declines between 20 and 37°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATPase activity of myosin I is stimulated 30 - 40fold by F-actin, when a single serine residue of its heavy chain is phosphorylated
-
-
brenda
His-tagged motor domain construct comprising amino acids 1-761
UniProt
brenda
-
-
-
brenda
non-muscle myosin IIb, recombinant protein expressed in baculovirus expression system
-
-
brenda
-
246976, 246978, 246983, 246995, 246996, 246997, 247001, 247004, 247005, 654753, 654823, 654882, 654976, 669474, 670007, 684827, 685073, 685318, 719098, 719099, 733515, 733791, 735020, 749738, 749747, 749819, 749998, 751659
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
2 mol of ATP and 2 mol of actin monomer bind to 1 mol of arterial myosin
brenda
-
myosin ATPase isoenzymes show different temperature sensivities
brenda
-
myosin-VIIa, exclusively expressed by pigmented epithelial cells
brenda
-
permeabilized fibers of soleus, plantaris, and semimembraneous muscle
brenda
-
-
246975, 246996, 246997, 247005, 669474, 685073, 719098, 719099, 733515, 733791, 735020, 749819, 749998, 751659
brenda
-
2 mol of ATP and 2 mol of actin monomer bind to 1 mol of skeletal muscle myosin
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
-
in drebrin A (DA-actin) from dendritic spines, DA-actin exodus is blocked by myosin II ATPase inhibitor, but is not blocked by myosin light chain kinase or Rho-associated kinase inhibitors, indicating that myosin II mediates the interaction between NMDA receptor activation and DA-actin exodus in long-term potentiation induction. Glutamate-induced DA-actin exodus is also dependent on myosin II ATPase activity. Myosin II seems to be activated by a rapid actin-linked mechanism rather than slow myosin light chain phosphorylation. The myosin-II mediated DA-actin exodus might be an initial event in LTP induction, triggering actin polymerization and spine enlargement
physiological function
myosin is a linear motor that utilizes the free energy obtained from ATP hydrolysis to drive the coordinated motion of its protein domains during muscle contraction. During its contraction cycle, the myosin motor catalyzes the hydrolysis of ATP, molecular mechanism involving residue Glu459, overview
physiological function
-
myosin Mg-ATPase of molluscan muscles is slightly activated by F-actin under catch state in vitro. At low Ca2+ concentration, Mg-ATPase is activated by F-actin only in the presence of dephosphorylated twitchin, a titin/connectinrelated giant protein, regulates interactions between actin and myosin filaments at low Ca2+ concentrations. When it is dephosphorylated, actin filaments tightly bind to myosin filaments, resulting in the catch state known as the state of high passive tension with very low energy consumption. When twitchin is phosphorylated actin filaments detach from the myosin filaments, resulting in relaxation of the catch. In the absence of F-actin, twitchin and its phosphorylation state do not affect Mg-ATPase activities in any of the conditions tested. Determination of a molecular mechanism for the catch, where twitchin alone does not interact with the myosin catalytic motor domain but its complex with F-actin does, forming the bridge between actin and myosin filaments and the myosin slowly hydrolyzes Mg-ATP in the catch state. Regulation mechanism, overview
physiological function
-
the actomyosin interaction plays a key role in a number of cellular functions. Mechanism of the actomyosin contractile system
physiological function
P13538; P02609; P02604
the molecular mechanism of muscle contraction and many other events of biological motility is based on cyclic interaction of myosin heads with actin filaments coupled to myosin-catalyzed ATP hydrolysis. The myosin head or myosin subfragment 1 consists of two major structural domains, the N-terminal globular motor (or catalytic) domain and the C-terminal regulatory domain. The motor domain is responsible for ATP hydrolysis and actin binding, modeling, overview
physiological function
-
in drebrin A (DA-actin) from dendritic spines, DA-actin exodus is blocked by myosin II ATPase inhibitor, but is not blocked by myosin light chain kinase or Rho-associated kinase inhibitors, indicating that myosin II mediates the interaction between NMDA receptor activation and DA-actin exodus in long-term potentiation induction. Glutamate-induced DA-actin exodus is also dependent on myosin II ATPase activity. Myosin II seems to be activated by a rapid actin-linked mechanism rather than slow myosin light chain phosphorylation. The myosin-II mediated DA-actin exodus might be an initial event in LTP induction, triggering actin polymerization and spine enlargement
-
additional information
-
actomyosin reconstitution from rabbit F-actin and mussel myosin in presence or absence of unphosphorylated or phosphorylated myorod is prepared in two modes, overview
additional information
-
actomyosin reconstitution from rabbit F-actin and rabbit myosin in presence or absence of unphosphorylated or phosphorylated myorod is prepared in two modes, overview
additional information
-
Ca2+-dependent ATPase activity and enzyme protein content in muscle are reduced by ultrasonication for 10 min at 20 mHz with 0.5-1.8 mg/ml protein, e.g. loss of 47% Ca2+-dependent enzyme activity of chicken natural actomyosin at 0.5 mg/ml protein. Unlike myofibrils, actomyosin is a model where interactions and substructural changes of constituent polypeptides can be investigated without interference of endogenous muscle proteases
additional information
combined quantum/classical mechanics study and catalytic mechanism overview
additional information
P13538; P02609; P02604
formation of the ternary complexes S1-ADP-AlF4 - and S1-ADP-BeFx that mimic S1 ATPase intermediate states S1-ADP-Pi and S1-ATP, respectively, and analysis of the changes in thermal unfolding and the domain structure. Local conformational changes in the myosin ATPase site spread to the entire motor domain, resulting in global structural changes in the motor domain. destabilizing of the regulatory domain by removal of essential light chain or regulatory light chain (and especially of both) markedly reduces the sliding velocity of actin filaments without a significant loss in actin-activated ATPase activity of myosin. the essential light chain associated with the regulatory domain may play a crucial role in the motor function of the myosin head, taking part in the overall stabilization of the S1 molecule during the ATPase cycle. Proposed interactions between the C-terminal half of essential light chain and the motor domain of the myosin head
additional information
loop-2 of the catalytic motor domain of the heavy chain of Acanthamoeba castellanii myosin-2
additional information
-
loop-2 of the catalytic motor domain of the heavy chain of Acanthamoeba castellanii myosin-2
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A222DYD0_9HEMI
1956
0
222926
TrEMBL
other Location (Reliability: 1)
A0A2P6QBD6_ROSCH
740
0
82451
TrEMBL
Chloroplast (Reliability: 3)
A0A2P6RKH5_ROSCH
1529
0
172496
TrEMBL
other Location (Reliability: 2)
A0A2G9HVQ0_9LAMI
1010
0
115813
TrEMBL
other Location (Reliability: 3)
B6H0B1_PENRW
Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255)
1120
1
125994
TrEMBL
Secretory Pathway (Reliability: 1)
A0A396JUT8_MEDTR
1108
0
125635
TrEMBL
other Location (Reliability: 4)
A0A396HCB9_MEDTR
1014
0
115639
TrEMBL
other Location (Reliability: 4)
A0A221IRA2_9HEMI
1956
0
223294
TrEMBL
other Location (Reliability: 1)
A0A072US24_MEDTR
1530
0
172638
TrEMBL
other Location (Reliability: 4)
A0A2P6QRS9_ROSCH
1539
0
173586
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6SDY6_ROSCH
137
0
15053
TrEMBL
other Location (Reliability: 2)
A3GHA0_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
1306
0
149242
TrEMBL
other Location (Reliability: 2)
A2R349_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
1129
1
126917
TrEMBL
Secretory Pathway (Reliability: 1)
A0A221IQX6_9HEMI
1971
0
224881
TrEMBL
other Location (Reliability: 1)
A0A221IRA3_9HEMI
1956
0
222778
TrEMBL
other Location (Reliability: 1)
G7KZI6_MEDTR
1510
0
170807
TrEMBL
other Location (Reliability: 3)
A0A0B2QDU3_GLYSO
506
0
56753
TrEMBL
other Location (Reliability: 2)
A0A2P6R4S5_ROSCH
1177
0
132888
TrEMBL
Chloroplast (Reliability: 3)
A0A2P6PVH0_ROSCH
1173
0
132188
TrEMBL
other Location (Reliability: 5)
A0A2G9GVA3_9LAMI
195
0
21753
TrEMBL
other Location (Reliability: 3)
A0A2G9G9B4_9LAMI
515
0
58102
TrEMBL
other Location (Reliability: 3)
A7ASN6_BABBO
1473
0
165191
TrEMBL
other Location (Reliability: 4)
A0A2G9GFS9_9LAMI
760
0
86921
TrEMBL
other Location (Reliability: 2)
A0A2G9H0R5_9LAMI
992
0
112931
TrEMBL
other Location (Reliability: 3)
A0A396JGY7_MEDTR
1582
0
180858
TrEMBL
other Location (Reliability: 3)
A0A221IQU7_9HEMI
1971
0
225003
TrEMBL
other Location (Reliability: 1)
A0A2G9I9S7_9LAMI
1534
0
174940
TrEMBL
other Location (Reliability: 4)
A0A396JLG2_MEDTR
1516
0
173273
TrEMBL
other Location (Reliability: 4)
A0A396JP85_MEDTR
979
1
111459
TrEMBL
other Location (Reliability: 4)
A0A2G9HAZ0_9LAMI
1221
0
137109
TrEMBL
other Location (Reliability: 2)
A0A2P6QBC6_ROSCH
380
0
43702
TrEMBL
other Location (Reliability: 3)
U6MF83_9EIME
330
0
35517
TrEMBL
other Location (Reliability: 2)
B6HG04_PENRW
Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255)
1567
0
179199
TrEMBL
other Location (Reliability: 1)
A7AWK3_BABBO
837
0
93562
TrEMBL
other Location (Reliability: 2)
A0A2G9I6B0_9LAMI
1513
0
172595
TrEMBL
other Location (Reliability: 5)
A0A221IR91_9HEMI
668
0
76290
TrEMBL
other Location (Reliability: 1)
A0A396JJC6_MEDTR
104
0
11779
TrEMBL
other Location (Reliability: 2)
G7I6V3_MEDTR
1072
0
122783
TrEMBL
other Location (Reliability: 3)
A0A2G9HQ29_9LAMI
476
0
54558
TrEMBL
other Location (Reliability: 5)
A0A396JZN0_MEDTR
1176
0
133007
TrEMBL
Chloroplast (Reliability: 4)
A2R9R1_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
1572
0
179690
TrEMBL
other Location (Reliability: 1)
A0A2P6Q1L6_ROSCH
1522
0
173568
TrEMBL
other Location (Reliability: 3)
A0A2G9GJ57_9LAMI
1502
0
168843
TrEMBL
other Location (Reliability: 3)
A0A2G9HRU7_9LAMI
1524
0
173541
TrEMBL
other Location (Reliability: 2)
A0A221IRF8_9HEMI
1971
0
225151
TrEMBL
other Location (Reliability: 1)
A0A221IRH5_9HEMI
1971
0
224867
TrEMBL
other Location (Reliability: 1)
G7IR58_MEDTR
1203
0
136058
TrEMBL
Chloroplast (Reliability: 3)
A0A396JUH3_MEDTR
288
0
32592
TrEMBL
other Location (Reliability: 5)
A0A2P6R5Q6_ROSCH
1555
0
176374
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9HQP8_9LAMI
1061
0
120427
TrEMBL
other Location (Reliability: 2)
A0A221IRH6_9HEMI
699
0
80025
TrEMBL
other Location (Reliability: 1)
A0A8J8W6W4_9EURO
2395
0
276451
TrEMBL
Mitochondrion (Reliability: 2)
A7ASD9_BABBO
1651
0
186706
TrEMBL
other Location (Reliability: 3)
A0A221IR99_9HEMI
409
0
45965
TrEMBL
Mitochondrion (Reliability: 5)
A3GI45_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
1571
0
180188
TrEMBL
other Location (Reliability: 1)
A0A221IRA8_9HEMI
1956
0
222762
TrEMBL
other Location (Reliability: 1)
A0A396JQ47_MEDTR
1027
0
118589
TrEMBL
other Location (Reliability: 5)
A0A0F4YYL7_TALEM
2407
0
277654
TrEMBL
Mitochondrion (Reliability: 3)
A3LSE0_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
1063
0
121511
TrEMBL
other Location (Reliability: 1)
A0A222DXQ8_9HEMI
1956
0
222792
TrEMBL
other Location (Reliability: 1)
A0A396JJI1_MEDTR
1170
0
132347
TrEMBL
other Location (Reliability: 4)
A0A396JNU0_MEDTR
1513
0
172073
TrEMBL
other Location (Reliability: 3)
A0A0F4YUE0_TALEM
1571
0
179375
TrEMBL
other Location (Reliability: 1)
A2QN88_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
2406
0
277202
TrEMBL
Mitochondrion (Reliability: 3)
A0A2P6PUP5_ROSCH
1515
0
172214
TrEMBL
other Location (Reliability: 4)
A0A396J293_MEDTR
1169
1
134095
TrEMBL
other Location (Reliability: 4)
A0A072TQA3_MEDTR
1178
0
133649
TrEMBL
Chloroplast (Reliability: 5)
A0A061IJ24_CRIGR
2280
0
261171
TrEMBL
other Location (Reliability: 1)
A0A061IFH1_CRIGR
2043
0
234215
TrEMBL
other Location (Reliability: 2)
A0A2G9HJM6_9LAMI
1509
0
170960
TrEMBL
other Location (Reliability: 5)
A0A2G9HVQ3_9LAMI
88
0
10723
TrEMBL
other Location (Reliability: 2)
A0A2G9HD57_9LAMI
140
0
16351
TrEMBL
Secretory Pathway (Reliability: 4)
A0A396HDD1_MEDTR
58
0
6901
TrEMBL
Mitochondrion (Reliability: 2)
MYOE_DICDI
1005
0
114795
Swiss-Prot
other Location (Reliability: 2)
MYS2_DICDI
2116
0
243786
Swiss-Prot
other Location (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
125000
-
alpha,beta,gamma, 1 * 125000 + 1 * 27000 + 1 * 14000, myosin IB, one heavy chain and two light chains, ATP catalytic-, actin binding- and phosphorylation site are located on heavy chain, SDS-PAGE
130000
-
alpha,beta,gamma, 1 * 130000 + 1 * 17000 + 1 * 14000, myosin IA, one heavy chain and two light chains, SDS-PAGE
14000
150000
-
myosin IA and IB, sucrose density gradient and eqilibrium centrifugation
16500
-
alpha,beta 1,beta 2, 1 * 20000 + 2 * 16500, at least three species of light chains, SDS-PAGE
17000
170000
-
alpha2,beta2,gamma2, 2 * 170000 + 2 * 17500 + 2 * 17000, two heavy chains and four light chains, SDS-PAGE
17500
-
alpha2,beta2,gamma2, 2 * 170000 + 2 * 17500 + 2 * 17000, two heavy chains and four light chains, SDS-PAGE
20000
-
alpha,beta 1,beta 2, 1 * 20000 + 2 * 16500, at least three species of light chains, SDS-PAGE
27000
-
alpha,beta,gamma, 1 * 125000 + 1 * 27000 + 1 * 14000, myosin IB, one heavy chain and two light chains, ATP catalytic-, actin binding- and phosphorylation site are located on heavy chain, SDS-PAGE
400000
-
myosin II, sucrose density gradient and eqilibrium centrifugation
14000
-
alpha,beta,gamma, 1 * 130000 + 1 * 17000 + 1 * 14000, myosin IA, one heavy chain and two light chains, SDS-PAGE
14000
-
alpha,beta,gamma, 1 * 125000 + 1 * 27000 + 1 * 14000, myosin IB, one heavy chain and two light chains, ATP catalytic-, actin binding- and phosphorylation site are located on heavy chain, SDS-PAGE
17000
-
alpha,beta,gamma, 1 * 130000 + 1 * 17000 + 1 * 14000, myosin IA, one heavy chain and two light chains, SDS-PAGE
17000
-
alpha2,beta2,gamma2, 2 * 170000 + 2 * 17500 + 2 * 17000, two heavy chains and four light chains, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heteromer
-
alpha,beta 1,beta 2, 1 * 20000 + 2 * 16500, at least three species of light chains, SDS-PAGE
hexamer
-
alpha2,beta2,gamma2, 2 * 170000 + 2 * 17500 + 2 * 17000, two heavy chains and four light chains, SDS-PAGE
trimer
additional information
P13538; P02609; P02604
domain structure of myosin head or myosin subfragment 1, S1
trimer
-
alpha,beta,gamma, 1 * 130000 + 1 * 17000 + 1 * 14000, myosin IA, one heavy chain and two light chains, SDS-PAGE
trimer
-
alpha,beta,gamma, 1 * 125000 + 1 * 27000 + 1 * 14000, myosin IB, one heavy chain and two light chains, ATP catalytic-, actin binding- and phosphorylation site are located on heavy chain, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphorylation of Ser-639 in loop-2 of myosin-2 affects the processive behavior of myosin-2 filaments
side-chain modification
side-chain modification
-
increasing levels of myosin light chain phosphorylation in cold stressed rats, 1.9 mol of P/mol of myosin, heavy chain of myosin IA and IB can be phosphorylated to the extent of 1 mol of P per mol of heavy chain
side-chain modification
-
increasing levels of myosin light chain phosphorylation in cold stressed rats, 1.9 mol of P/mol of myosin, heavy chain of myosin IA and IB can be phosphorylated to the extent of 1 mol of P per mol of heavy chain
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis, in which myosin II from Dictyostelium discoideum is complexed with Mg2-ADP-vanadate, a transition state analogue, PDB ID 1VOM
analysis of structures of nucleotide-free chicken skeletal S1 (PDB entry 2MYS) and chicken gizzard S1 in the S1-ADP-BeFx complex (PDB entry 1BR4)
P13538; P02609; P02604
X-ray crystallographic analysis of the Dictyostelium discoideum myosin-2 motor domain complexes with magnesium(II)-ADP-metavanadate and the three pseudilin inhibitors pentabromopseudilin, pentachloropseudilin, and tribromodichloropseudilin, PDB IDs 2JJ9, 1VOM, and 2XO8
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S639D
site-directed mutagenesis, a phosphomimetic mutation that affects the processive behavior of myosin-2 filaments
I499C
-
plus cysteine-light mutations C49S, C312Y, C470I, C599L, C678Y, rescues growth of cells in suspension similarly to wild type, minimal implications on actin binding, ATP-induced actin release, actin-activated ATPase activity
I499C/R738C
-
plus cysteine-light mutations C49S, C312Y, C470I, C599L, C678Y, rescues growth of cells in suspension similarly to wild type, even after disulfide-induced crosslinking of mutated residues just minimal implications on actin binding, ATP-induced actin release, actin-activated ATPase activity
R738C
-
plus cysteine-light mutations C49S, C312Y, C470I, C599L, C678Y, rescues growth of cells in suspension similarly to wild type, minimal implications on actin binding, ATP-induced actin release, actin-activated ATPase activity
F547A
-
mutation in loop 1, a hydrophobic triplet of residues, involved in actin binding
P548A
-
mutation in loop 1, a hydrophobic triplet of residues, involved in actin binding
W546A
-
mutation in loop 1, a hydrophobic triplet of residues, involved in actin binding
Myo1b-GAGEGA
-
Myo1b in which wild-type loop 4 is replaced with loop 4 of Dictyostelium myosin II, GAGEGA
Myo1b1IQ-GAGEGA
-
Myo1b1IQ in which wild-type loop 4 is replaced with loop 4 of Dictyostelium myosin II, GAGEGA
Myo1b1IQ-WT
-
wild-type Myo1b truncated after the first IQ domain at amino acid 728 containing the wild-type loop 4 sequence, RMNGLDES
additional information
additional information
-
enzyme deletion mutant, no growth of cells in suspension
additional information
-
myosin loop 2 replaced by rabbit skeletal or smooth muscle loop 2
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
-
after 1 h at pH 9.0 isoenzyme V1 shows 2-12% loss of activity compared with 45% for isoenzyme V3
247002
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 30
25 - 37
-
100% inhibition after incubation at pH 9.0 and 37°C for 2 min, 10% at 25°C
additional information
P13538; P02609; P02604
thermal unfolding of myosin head or myosin subfragment 1, S1, thermally induced dissociation of leight chain 1 from the S1 heavy chain, overview
25 - 30
-
activity of skeletal myosin decreases about 50% after preincubation for 20 min at 30°C and pH 5.7, very slow decrease at pH 8.6, activity of cardiac myosin decreases about 90% after preincubation at 25°C and pH 8.6, very slow decrease at pH 5.7
25 - 30
-
activity of skeletal myosin decreases about 50% after preincubation for 20 min at 30°C and pH 5.7, very slow decrease at pH 8.6, activity of cardiac myosin decreases about 90% after preincubation at 25°C and pH 8.6, very slow decrease at pH 5.7
25 - 30
-
activity of skeletal myosin decreases about 50% after preincubation for 20 min at 30°C and pH 5.7, very slow decrease at pH 8.6, activity of cardiac myosin decreases about 90% after preincubation at 25°C and pH 8.6, very slow decrease at pH 5.7
25 - 30
-
activity of skeletal myosin decreases about 50% after preincubation for 20 min at 30°C and pH 5.7, very slow decrease at pH 8.6, activity of cardiac myosin decreases about 90% after preincubation at 25°C and pH 8.6, very slow decrease at pH 5.7
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, ADP-agarose, hydroxyapatite, BioGel adsorption, myosin Ia and IB
-
myofibrils are isolated from heart tissue
myosin with unphosphorylated regulatory light chain (20000 Da) from smooth muscle of gizzard; recombinant His-tagged myosin head: immobilized metal ion affinity chromatography (Ni2+)
-
native myosin and myorod from posterior adductor by ammonium sulfate fractionation, dialysis, and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged motor domain construct comprising amino acids 1-761
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
phosphorylation of Ser639 in loop-2 of the catalytic motor domain of the heavy chain of Acanthamoeba castellanii myosin-2 and the phosphomimetic mutation S639D downregulate the actin-activated ATPase activity of both the full-length myosin and single-headed subfragment-1
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
Ca2+-activated myosin ATPase activity is reduced with age in semimembraneous muscle, one mechanism that contributes to age-related slowing of contraction in that muscle
medicine
-
decrease of enzyme activity in hearts of idiopathic and ischemic cardiomyopathic individuals, MCI-154 and caffeine increased enzyme activity
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saeiki, K.; Yasunaga, T.; Matsuura, Y.; Wakabayashi, T.
Role of residues 230 and 236 of actin in myosin-ATPase activation by actin-tropomyosin
Biochem. Biophys. Res. Commun.
275
428-433
2000
Oryctolagus cuniculus
brenda
Murphy, C.T.; Spudich, J.A.
The sequence of the myosin 50-20K loop affects myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity
Biochemistry
38
3785-3792
1999
Gallus gallus, Oryctolagus cuniculus, Dictyostelium sp.
brenda
Katoch, S.S.; Soni, A.
Changes in myosin ATPase activity in skeletal muscles of rat during cold stress
Indian J. Biochem. Biophys.
36
204-206
1999
Rattus norvegicus
brenda
Park, S.; Ajtai, K.; Burghardt, T.P.
Inhibition of myosin ATPase by metal fluoride complexes
Biochim. Biophys. Acta
1430
127-140
1999
Oryctolagus cuniculus
brenda
Ye, L-H.; Kishi, H.; Nakamura, A.; Okagaki, T.; Tanaka, T.; Oiwa, K.; Kohama, K.
Myosin light-chain kinase of smooth muscle stimulates myosin ATPase activity without phosphorylating myosin light chain
Proc. Natl. Acad. Sci. USA
96
6666-6671
1999
Gallus gallus
brenda
Degan, P.; Gesser, H.
Ca2+ activated myosin-ATPase in cardiac myofibrils of rainbow trout, freshwater turtle and rat
J. Exp. Zool.
278
381-390
1997
Oncorhynchus mykiss, Trachemys scripta, Rattus norvegicus
brenda
Rayment, I.
The structural basis of the myosin ATPase activity
J. Biol. Chem.
271
15850-15853
1996
Dictyostelium sp.
brenda
Hasson, T.; Mooseker, M.S.
Vertebrate unconventional myosins
J. Biol. Chem.
271
16431-16434
1996
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Wank, V.; Bauer, R.; Punkt, K.; Ziegan, J.
Enzyme activity patterns of myosin ATPase, alpha-glycerophosphate dehydrogenase and succinate dehydrogenase within different muscle fibre types
Acta Histochem.
96
213-218
1994
Oryctolagus cuniculus
brenda
Szymanski, P.T.; Ferguson, D.G.; Paul, R.J.
Polylysine activates smooth muscle myosin ATPase activity via induction of a 10S to 6S transition
Am. J. Physiol.
265
379-386
1993
Gallus gallus
brenda
Lin, Y.; Ye, L.H.; Ishikawa, R.; Fujita, K.; Kohama, K.
Stimulatory effect of calponin on myosin ATPase activity
J. Biochem.
113
643-645
1993
Gallus gallus
brenda
Bolognani, L.; Buttafoco, P.; Ferrari, R.; Venturelli, T.; Volpi, N.
Effects of monocarboxylic and dicarboxylic acids on myosin ATPase activity tested by luminometric procedure
Biochem. Int.
26
231-239
1992
Bos taurus
brenda
Volpi, N.; Bianchini, P.; Bolognani, L.
Competitive inhibition of myosin ATPase activity by different molecular weight heparins
Biochem. Int.
24
243-253
1991
Bos taurus
brenda
Tuxen, A.
Effect of varying the preincubation and incubation temperature on the reaction pattern for myosin ATPase in rat skeletal muscle
Acta Anat. (Basel)
139
161-163
1990
Rattus norvegicus
brenda
Abe, M.; Takahashi, K.; Hiwada, K.
Effect of calponin on actin-activated myosin ATPase activity
J. Biochem.
108
835-838
1990
Gallus gallus
brenda
Srivastava, S.; Sasser, G.; Peterson, D.L.; Driska, S.P.
Characterization of the fluorescein isothiocyanate-reactive site of gizzard myosin ATPase
Biochim. Biophys. Acta
912
230-238
1987
Meleagris gallopavo
brenda
White, D.C.S.; Ricigliano, W.; Webb, M.R.
Analysis of the ATPase mechanism of myosin subfragment 1 from insect fibrillar flight muscle in the presence and absence of actin, using phosphate-water oxygen exchange measurements
J. Muscle Res. Cell Motil.
8
537-540
1987
Lethocerus griseus, Lethocerus indicus
brenda
Lynch, T.J.; Albanesi, J.P.; Korn, E.D.; Robinson, E.A.; Bowerst, B.; Fujisaki, H.
ATPase activities and actin-binding properties of subfragments of Acanthamoeba myosin IA
J. Biol. Chem.
261
17156-17162
1986
Acanthamoeba castellanii
brenda
Kanda, K.; Sobue, K.; Kakiuchi, S.
Phosphorylation of myosin light chain and the actin-activated ATPase activity of adrenal medullary myosin
J. Biochem.
97
961-964
1985
Bos taurus
brenda
Tamura, Y.; Kudo, T.; Sako, H.; Miyakama, S.; Nishimoto, T.; Saijo, Y.; Orino, S.; Mori, H.
Enzymatic properties of myosin ATPase from the conduction system of bovine heart
Tokushima J. Exp. Med.
32
1-8
1985
Bos taurus
brenda
Tanii, I.; Osafune, M.; Arata, T.; Inoue, A.
ATPase characterisics of myosin from nematode Caenorhabditis elegans purified by an improved method. Formation of myosin-phosphate-ADP complex and ATP-induced fluorescence enhancement
J. Biochem.
98
1201-1209
1985
Caenorhabditis elegans, Oryctolagus cuniculus
brenda
Kameyama, S.; Ichikawa, H.; Sunaga, Y.; Nakata, S.; Saito, Y.; Eiki, T.; Watanabe, S.
Biochemical characteristics of cardiac myosin: the pH dependence of Ca-ATPase activity, and that of the absorption spectrum of 2,4,6-trinitrophenyl groups attached to myosin
J. Biochem.
97
625-632
1985
Bos taurus, Gallus gallus, Oryctolagus cuniculus, Sus scrofa
brenda
Bechet, J.J.; Bachouchi, N.; Janmot, C.; d'Albis, A.
Isoenzymes of myosin subfragments. Chromatographic fractionation on carboxymethylcellulose and actin-activated ATPase activity as a function of temperature
Biochim. Biophys. Acta
703
54-61
1982
Oryctolagus cuniculus
brenda
Srivastava, S.; Kanungo, M.S.
Aging modulates some properties of skeletal myosin ATPase of rat
Biochem. Med.
28
266-272
1982
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Korn, E.D.; Collins, J.H.; Maruta, H.
Myosins from Acanthamoeba castellanii
Methods Enzymol.
85
357-363
1982
Acanthamoeba castellanii
brenda
Yamashita, T.; Tanaka, Y.; Matsuzawa, H.
Cytoplasmic and plasma membrane adenosine triphosphatase of polymorphonuclear neutrophils, comparison of their enzymatic properties and attempt for a direct determination of myosin ATPase activity using polymorphonuclear neutrophil extract
Biochim. Biophys. Acta
599
246-253
1980
Cavia porcellus
brenda
Takeuchi, K.
Comparison of kinetic properties of the ATPase reaction of arterial smooth muscle myosin with skeletal muscle myosin
J. Biochem.
88
1693-1702
1980
Bos taurus, Oryctolagus cuniculus
brenda
Pope, B.; Hoh, J.F.Y.; Weeds, A.
The ATPase activities of rat cardiac myosin isoenzymes
FEBS Lett.
118
205-209
1980
Rattus norvegicus
brenda
Shimizu, T.
Bovine platelet myosin. Properties of Mg- and Ca-ATPase
J. Biochem.
84
607-616
1978
Bos taurus
brenda
Trentham, D.R.
The adenosine triphosphatase reactions of myosin and actomyosin and their relation to energy transduction in muscle
Biochem. Soc. Trans.
5
5-22
1977
Oryctolagus cuniculus
brenda
Kielley, W.W.
Myosin adenosine triphosphatase
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
5
159-168
1961
Canis lupus familiaris, Oryctolagus cuniculus
-
brenda
Tiago, T.; Aureliano, M.; Gutierrez-Merino, C.
Decavanadate binding to a high affinity site near the myosin catalytic centre inhibits F-actin-stimulated myosin ATPase activity
Biochemistry
43
5551-5561
2004
Oryctolagus cuniculus
brenda
Trombetta, G.; Adami, R.; Cintio, O.; Grazi, E.
Differential response of fast and slow myosin ATPase from skeletal muscle to F-actin and to phalloidin F-actin
Biochim. Biophys. Acta
1569
135-138
2002
Oryctolagus cuniculus
brenda
Kobayashi, T.; Saeki, Y.; Chaen, S.; Shirakawa, I.; Sugi, H.
Effect of deuterium oxide on contraction characteristics and ATPase activity in glycerinated single rabbit skeletal muscle fibers
Biochim. Biophys. Acta
1659
46-51
2004
Oryctolagus cuniculus
brenda
Amitani, I.; Sakamoto, T.; Ando, T.
Link between the enzymatic kinetics and mechanical behavior in an actomyosin motor
Biophys. J.
80
379-397
2001
Oryctolagus cuniculus
brenda
Moreira, C.M.; Oliveira, E.M.; Bonan, C.D.; Sarkis, J.J.; Vassallo, D.V.
Effects of mercury on myosin ATPase in the ventricular myocardium of the rat
Comp. Biochem. Physiol. C
135C
269-275
2003
Rattus norvegicus
brenda
Shih, W.M.; Spudich, J.A.
The myosin relay helix to converter interface remains intact throughout the actomyosin ATPase cycle
J. Biol. Chem.
276
19491-19494
2001
Dictyostelium discoideum
brenda
Wang, F.; Kovacs, M.; Hu, A.; Limouze, J.; Harvey, E.V.; Sellers, J.R.
Kinetic mechanism of non-muscle myosin IIB: Functional adaptations for tension generation and maintenance
J. Biol. Chem.
278
27439-27448
2003
Homo sapiens
brenda
Lowe, D.A.; Husom, A.D.; Ferrington, D.A.; Thompson, L.V.
Myofibrillar myosin ATPase activity in hindlimb muscles from young and aged rats
Mech. Ageing Dev.
125
619-627
2004
Rattus norvegicus
brenda
Okafor, C.; Liao, R.; Perreault-Micale, C.; Li, X.; Ito, T.; Stepanek, A.; Doye, A.; de Tombe, P.; Gwathmey, J.K.
Mg-ATPase and Ca+ activated myosin AtPase activity in ventricular myofibrils from non-failing and diseased human hearts--effects of calcium sensitizing agents MCI-154, DPI 201-106, and caffeine
Mol. Cell. Biochem.
245
77-89
2003
Homo sapiens
brenda
Alahyan, M.; Webb, M.R.; Marston, S.B.; El-Mezgueldi, M.
The mechanism of smooth muscle caldesmon-tropomyosin inhibition of the elementary steps of the actomyosin ATPase
J. Biol. Chem.
281
19433-19448
2006
Oryctolagus cuniculus
brenda
Prochniewicz, E.; Thomas, D.D.; Thompson, L.V.
Age-related decline in actomyosin function
J. Gerontol.
A
425-431
2005
Rattus norvegicus
brenda
Burton, K.; White, H.; Sleep, J.
Kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates
J. Physiol.
563
689-711
2005
Oryctolagus cuniculus
brenda
Borlak, J.; Zwadlo, C.
The myosin ATPase inhibitor 2,3-butanedione monoxime dictates transcriptional activation of ion channels and Ca(2+)-handling proteins
Mol. Pharmacol.
66
708-717
2004
Rattus norvegicus
brenda
Paul Ehrlich, H.; Sun, B.; Kainth, K.S.; Kromah, F.
Elucidating the mechanism of wound contraction: rapid versus sustained myosin ATPase activity in attached-delayed-released compared with free-floating fibroblast-populated collagen lattices
Wound Repair Regen.
14
625-632
2006
Homo sapiens
brenda
Zhong, S.; Thompson, L.V.
The roles of myosin ATPase activity and myosin light chain relative content in the slowing of type IIB fibers with hindlimb unweighting in rats
Am. J. Physiol.
293
C723-C728
2007
Rattus norvegicus
brenda
Kulikova, N.; Pronina, O.E.; Dabrowska, R.; Borovikov, Y.S.
Caldesmon restricts the movement of both C- and N-termini of tropomyosin on F-actin in ghost fibers during the actomyosin ATPase cycle
Biochem. Biophys. Res. Commun.
345
280-286
2006
Oryctolagus cuniculus
brenda
Tiago, T.; Simao, S.; Aureliano, M.; Martin-Romero, F.J.; Gutierrez-Merino, C.
Inhibition of skeletal muscle S1-myosin ATPase by peroxynitrite
Biochemistry
45
3794-3804
2006
Oryctolagus cuniculus
brenda
Lieto-Trivedi, A.; Dash, S.; Coluccio, L.M.
Myosin surface loop 4 modulates inhibition of actomyosin 1b ATPase activity by tropomyosin
Biochemistry
46
2779-2786
2007
Mammalia
brenda
Borovikov, Y.S.; Kulikova, N.; Pronina, O.E.; Khaimina, S.S.; Wrzosek, A.; Dabrowska, R.
Caldesmon freezes the structure of actin filaments during the actomyosin ATPase cycle
Biochim. Biophys. Acta
1764
1054-1062
2006
Oryctolagus cuniculus
brenda
Tiago, T.; Martel, P.; Gutierrez-Merino, C.; Aureliano, M.
Binding modes of decavanadate to myosin and inhibition of the actomyosin ATPase activity
Biochim. Biophys. Acta
1774
474-480
2007
Dictyostelium discoideum
brenda
Padilha, A.S.; Moreira, C.M.; Meira, E.F.; Siman, F.D.; Stefanon, I.; Vassallo, D.V.
Chronic ouabain treatment enhances cardiac myosin ATPase activity in rats
Clin. Exp. Pharmacol. Physiol.
35
801-806
2008
Rattus norvegicus
brenda
Haagensen, L.; Jensen, D.H.; Gesser, H.
Dependence of myosin-ATPase on structure bound creatine kinase in cardiac myfibrils from rainbow trout and freshwater turtle
Comp. Biochem. Physiol. A
150
404-409
2008
Oncorhynchus mykiss, Trachemys scripta
brenda
Onishi, H.; Mikhailenko, S.V.; Morales, M.F.
Toward understanding actin activation of myosin ATPase: the role of myosin surface loops
Proc. Natl. Acad. Sci. USA
103
6136-6141
2006
Gallus gallus
brenda
Blair, D.R.; Funai, K.; Schweitzer, G.G.; Cartee, G.D.
A myosin II ATPase inhibitor reduces force production, glucose transport, and phosphorylation of AMPK and TBC1D1 in electrically stimulated rat skeletal muscle
Am. J. Physiol. Endocrinol. Metab.
296
E993-E1002
2009
Rattus norvegicus
brenda
Vassallo, D.V.; Lebarch, E.C.; Moreira, C.M.; Wiggers, G.A.; Stefanon, I.
Lead reduces tension development and the myosin ATPase activity of the rat right ventricular myocardium
Braz. J. Med. Biol. Res.
41
789-795
2008
Rattus norvegicus
brenda
Kronert, W.A.; Dambacher, C.M.; Knowles, A.F.; Swank, D.M.; Bernstein, S.I.
Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function
J. Mol. Biol.
379
443-456
2008
Drosophila melanogaster
brenda
Saber, W.; Begin, K.J.; Warshaw, D.M.; VanBuren, P.
Cardiac myosin binding protein-C modulates actomyosin binding and kinetics in the in vitro motility assay
J. Mol. Cell. Cardiol.
44
1053-1061
2008
Gallus gallus
brenda
Joubert, F.; Wilding, J.R.; Fortin, D.; Domergue-Dupont, V.; Novotova, M.; Ventura-Clapier, R.; Veksler, V.
Local energetic regulation of sarcoplasmic and myosin ATPase is differently impaired in rats with heart failure
J. Physiol.
586
5181-5192
2008
Rattus norvegicus
brenda
Anderson, T.W.; Vaughan, A.N.; Cramer, L.P.
Retrograde flow and myosin II activity within the leading cell edge deliver F-actin to the lamella to seed the formation of graded polarity actomyosin II filament bundles in migrating fibroblasts
Mol. Biol. Cell
19
5006-5018
2008
Gallus gallus
brenda
Katayama, T.; Watanabe, M.; Tanaka, H.; Hino, M.; Miyakawa, T.; Ohki, T.; Ye, L.; Xie, C.; Yoshiyama, S.; Nakamura, A.; Ishikawa, R.; Tanokura, M.; Oiwa, K.; Kohama, K.
Stimulatory effects of arachidonic acid on myosin ATPase activity and contraction of smooth muscle via myosin motor domain
Am. J. Physiol. Heart Circ. Physiol.
298
H505-H514
2010
Gallus gallus
brenda
Caremani, M.; Lehman, S.; Lombardi, V.; Linari, M.
Orthovanadate and orthophosphate inhibit muscle force via two different pathways of the myosin ATPase cycle
Biophys. J.
100
665-674
2011
Oryctolagus cuniculus
brenda
Cooke, R.
The role of the myosin ATPase activity in adaptive thermogenesis by skeletal muscle
Biophys. Rev.
3
33-45
2011
Oryctolagus cuniculus
brenda
Preller, M.; Chinthalapudi, K.; Martin, R.; Knolker, H.J.; Manstein, D.J.
Inhibition of myosin ATPase activity by halogenated pseudilins: a structure-activity study
J. Med. Chem.
54
3675-3685
2011
Dictyostelium discoideum (P08799)
brenda
Ahmad, R.; Hasnain, A.
Ultrasonication of chicken natural actomyosin: effect on ATPase activity, turbidity and SDS-PAGE profiles at different protein concentrations
Am. J. Biochem. Mol. Biol.
3
240-247
2013
Gallus gallus
-
brenda
Sato, M.K.; Ishihara, T.; Tanaka, H.; Ishijima, A.; Inoue, Y.
Velocity-dependent actomyosin ATPase cycle revealed by in vitro motility assay with kinetic analysis
Biophys. J.
103
711-718
2012
Oryctolagus cuniculus
brenda
Kiani, F.A.; Fischer, S.
Advances in quantum simulations of ATPase catalysis in the myosin motor
Curr. Opin. Struct. Biol.
31
115-123
2015
Dictyostelium discoideum (P08799)
brenda
Martin, R.; Risacher, C.; Barthel, A.; Jaeger, A.; Schmidt, A.; Richter, S.; Boehl, M.; Preller, M.; Chinthalapudi, K.; Manstein, D.; Gutzeit, H.; Knoelker, H.
Silver(I)-catalyzed route to pyrroles: synthesis of halogenated pseudilins as allosteric inhibitors for myosin ATPase and x-ray crystal structures of the protein-inhibitor complexes
Eur. J. Org. Chem.
2014
4487-4505
2014
Oryctolagus cuniculus
-
brenda
Heissler, S.M.; Liu, X.; Korn, E.D.; Sellers, J.R.
Kinetic characterization of the ATPase and actin-activated ATPase activities of Acanthamoeba castellanii myosin-2
J. Biol. Chem.
288
26709-26720
2013
Acanthamoeba castellanii (P05659), Acanthamoeba castellanii
brenda
Yamada, A.; Yoshio, M.; Oiwa, K.
Myosin Mg-ATPase of molluscan muscles is slightly activated by F-actin under catch state in vitro
J. Muscle Res. Cell Motil.
34
115-123
2013
Mytilus galloprovincialis
brenda
Matusovsky, O.S.; Shevchenko, U.V.; Matusovskaya, G.G.; Sobieszek, A.; Dobrzhanskaya, A.V.; Sheludko, N.S.
Catch muscle myorod modulates ATPase activity of myosin in a phosphorylation-dependent way
PLoS ONE
10
e0125379
2015
Oryctolagus cuniculus, Crenomytilus grayanus
brenda
Logvinova, D.S.; Markov, D.I.; Nikolaeva, O.P.; Sluchanko, N.N.; Ushakov, D.S.; Levitsky, D.I.
Does interaction between the motor and regulatory domains of the myosin head occur during ATPase cycle? Evidence from thermal unfolding studies on myosin subfragment 1
PLoS ONE
10
e0137517
2015
Gallus gallus (P13538 and P02609 and P02604)
brenda
Mizui, T.; Sekino, Y.; Yamazaki, H.; Ishizuka, Y.; Takahashi, H.; Kojima, N.; Kojima, M.; Shirao, T.
Myosin II ATPase activity mediates the long-term potentiation-induced exodus of stable F-actin bound by drebrin A from dendritic spines
PLoS ONE
9
e85367
2014
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Borovikov, Y.S.; Avrova, S.V.; Rysev, N.A.; Sirenko, V.V.; Simonyan, A.O.; Chernev, A.A.; Karpicheva, O.E.; Piers, A.; Redwood, C.S.
Aberrant movement of beta-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle
Arch. Biochem. Biophys.
577-578
11-23
2015
Oryctolagus cuniculus
brenda
Kobayashi, M.; Ramirez, B.E.; Warren, C.M.
Interplay of actin, ADP and Mg2+ interactions with striated muscle myosin Implications of their roles in ATPase
Arch. Biochem. Biophys.
662
101-110
2019
Oryctolagus cuniculus
brenda
Borovikov, Y.; Simonyan, A.; Karpicheva, O.; Avrova, S.; Rysev, N.; Sirenko, V.; Piers, A.; Redwood, C.
The reason for a high Ca2+-sensitivity associated with Arg91Gly substitution in TPM2 gene is the abnormal behavior and high flexibility of tropomyosin during the ATPase cycle
Biochem. Biophys. Res. Commun.
494
681-686
2017
Oryctolagus cuniculus
brenda
Ghashghaee, N.; Li, K.; Dong, W.
Direct interaction between troponin and myosin enhances the ATPase activity of heavy meromyosin
Biologia (Poland)
72
702-708
2017
Oryctolagus cuniculus
-
brenda
Kiani, F.; Fischer, S.
ATP-dependent interplay between local and global conformational changes in the myosin motor
Cytoskeleton (Hoboken)
73
643-651
2016
Homo sapiens
brenda
Li, J.; Lu, Z.; He, J.; Chen, Q.; Wang, X.; Kang, L.; Li, X.D.
Alternative exon-encoding regions of Locusta migratoria muscle myosin modulate the pH dependence of ATPase activity
Insect Mol. Biol.
25
689-700
2016
Locusta migratoria
brenda
Labyntseva, R.; Yavorovska, V.; Bevza, O.; Drapaylo, A.; Kalchenko, V.; Kosterin, S.
Thiacalix[4]arenes remove the inhibitory effects of Zn cations on the myosin ATPase activity
Nanoscale Res. Lett.
13
224
2018
Sus scrofa
brenda
Fujii, T.; Namba, K.
Structure of actomyosin rigour complex at 5.2 A resolution and insights into the ATPase cycle mechanism
Nat. Commun.
8
13969
2017
Oryctolagus cuniculus
brenda
Chung, C.S.; Mechas, C.; Campbell, K.S.
Myocyte contractility can be maintained by storing cells with the myosin ATPase inhibitor 2,3 butanedione monoxime
Physiol. Rep.
3
e12445
2015
Rattus norvegicus
brenda
Szatmari, D.; Bugyi, B.; Ujfalusi, Z.; Grama, L.; Dudas, R.; Nyitrai, M.
Cardiac leiomodin2 binds to the sides of actin filaments and regulates the ATPase activity of myosin
PLoS ONE
12
e0186288
2017
Rattus norvegicus
brenda
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