EC Number   |
Natural Substrates |
|---|
   5.6.1.8 | ATP + H2O + myosin bound to actin filament at position n |
- |
| 5.6.1.8 | ATP + H2O + myosin bound to actin filament at position n |
nucleoside triphosphates are hydrolyzed in the following order: GTP, ITP, CTP, ATP, UTP |
| 5.6.1.8 | ATP + H2O + myosin bound to actin filament at position n |
Delivering of F-actin to the lamella of migrating fibroblasts |
| 5.6.1.8 | more |
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 |
| 5.6.1.8 | more |
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 |
| 5.6.1.8 | more |
during its contraction cycle, the myosin motor catalyzes the hydrolysis of ATP |
| 5.6.1.8 | more |
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 |
