Kinetic characterization of the ATPase and actin-activated ATPase activities of Acanthamoeba castellanii myosin-2.

@article{Heissler2013KineticCO,
  title={Kinetic characterization of the ATPase and actin-activated ATPase activities of Acanthamoeba castellanii myosin-2.},
  author={Sarah M. Heissler and Xiong Liu and Edward D. Korn and James R Sellers},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 37},
  pages={26709-20}
}
Phosphorylation of Ser-639 in loop-2 of the catalytic motor domain of the heavy chain of Acanthamoeba castellanii myosin-2 and the phosphomimetic mutation S639D have been shown previously to down-regulate the actin-activated ATPase activity of both the full-length myosin and single-headed subfragment-1 (Liu, X., Lee, D. Y., Cai, S., Yu, S., Shu, S., Levine… CONTINUE READING