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
-
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
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
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General Information
General Information on EC 5.6.1.8 - myosin ATPase
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physiological function
additional information
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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
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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
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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
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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
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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
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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
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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
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loop-2 of the catalytic motor domain of the heavy chain of Acanthamoeba castellanii myosin-2