Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search General Information

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 11 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.8more actomyosin reconstitution from rabbit F-actin and mussel myosin in presence or absence of unphosphorylated or phosphorylated myorod is prepared in two modes, overview 735020
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.8more actomyosin reconstitution from rabbit F-actin and rabbit myosin in presence or absence of unphosphorylated or phosphorylated myorod is prepared in two modes, overview 735020
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.8more 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 733053
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.8more combined quantum/classical mechanics study and catalytic mechanism overview 733689
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.8more 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 735033
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.8more loop-2 of the catalytic motor domain of the heavy chain of Acanthamoeba castellanii myosin-2 734229
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.8physiological 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 -, 735134
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.8physiological 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 733689
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.8physiological 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 734515
Display the word mapDisplay the reaction diagram Show all sequences 5.6.1.8physiological function the actomyosin interaction plays a key role in a number of cellular functions. Mechanism of the actomyosin contractile system 733515
Results 1 - 10 of 11 > >>