5.6.1.8: myosin ATPase
This is an abbreviated version!
For detailed information about myosin ATPase, go to the full flat file.
Word Map on EC 5.6.1.8
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5.6.1.8
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contractile
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cardiac
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fiber
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cytoskeleton
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tension
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troponin
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ventricular
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f-actin
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myocardial
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artery
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hypertrophy
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myofibrillar
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junction
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microtubule
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cardiomyopathy
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isometric
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cardiomyocytes
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myotubes
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myocytes
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calmodulin
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striated
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soleus
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cytokinesis
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myoblasts
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myogenic
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sarcomere
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myogenesis
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actin-binding
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sliding
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desmin
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dictyostelium
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muscle-specific
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sarcoplasmic
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slide
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stiff
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rhoa
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ventricle
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digitorum
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lateralis
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vastus
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extensor
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unload
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kinesins
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myocarditis
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rock
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twitch
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adhesions
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longus
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microfilaments
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myofibers
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medicine
- 5.6.1.8
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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
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myogenesis
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actin-binding
-
sliding
- desmin
- dictyostelium
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muscle-specific
- sarcoplasmic
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slide
-
stiff
- rhoa
- ventricle
-
digitorum
- lateralis
-
vastus
- extensor
-
unload
- kinesins
- myocarditis
-
rock
-
twitch
- adhesions
- longus
-
microfilaments
-
myofibers
- medicine
Reaction
Synonyms
actin activated myosin ATPase, actin-stimulated myosin ATPase, actomyosin, actomyosin 1b ATPase, actomyosin ATPase, actomyosin-ATPase, EC 3.6.1.32, EC 3.6.4.1, heavy meromyosin, heavy meromyosin ATPase, HMM, HMM ATPase, matpase, myofibril ATPase, myosin, myosin 2, myosin 2 motor domain, myosin ATPase, myosin II ATPase, myosin II S1, myosin Mg-ATPase, myosin MgATPase, myosin S1 ATPase, myosin-2, myosin-2 ATPase, myosin-ATPase, natural actomyosin, NMIIB, S1-myosin ATPase
ECTree
5.6.1.8 myosin ATPaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 5.6.1.8 - myosin ATPase
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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
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-
?
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
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-
-
?
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
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-
?
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
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-
-
?
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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-
-
?
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
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-
246975, 246976, 246978, 246983, 246995, 246996, 246997, 247001, 247004, 247005, 733515, 733791, 735020, 749738, 749747, 749819, 749998, 751659
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-
?
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
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-
?
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
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-
?
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
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-
?
additional information
?
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-
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
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-
?
