The N-terminus of A1-type myosin essential light chains binds actin and modulates myosin motor function.

@article{Timson1998TheNO,
  title={The N-terminus of A1-type myosin essential light chains binds actin and modulates myosin motor function.},
  author={David J. Timson and Hylary R. Trayer and Ian P. Trayer},
  journal={European journal of biochemistry},
  year={1998},
  volume={255 3},
  pages={654-62}
}
There are two isoforms (A1 and A2) of the myosin essential light chain (ELC) and consequently two isoenzymes of myosin subfragment 1 (S1), S1(A1) and S1(A2). The two isoenzymes differ in their kinetic properties with S1(A1) having a lower apparent Km for actin and a slower turnover of MgATP (k(cat)) than S1(A2). The two forms of the ELC differ only at their N-termini where A1 has an additional 40-odd amino acids that are not present in A2. The human atrial ELC (an A1-type ELC) was overexpressed… CONTINUE READING

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