Acid phosphatase purified from Mycoplasma fermentans has protein tyrosine phosphatase-like activity.

@article{Shibata1994AcidPP,
  title={Acid phosphatase purified from Mycoplasma fermentans has protein tyrosine phosphatase-like activity.},
  author={Kenichiro Shibata and Masatoshi Noda and Yoshihisa Sawa and Toru Watanabe},
  journal={Infection and immunity},
  year={1994},
  volume={62 1},
  pages={313-5}
}
Acid phosphatase purified from Mycoplasma fermentans dephosphorylated phosphotyrosine-containing lysozyme and Raytide, a peptide substrate for protein tyrosine phosphatases. The optimum pH for Raytide was about 5.5. Raytide phosphatase activity was inhibited by potassium fluoride, sodium molybdate, and sodium orthovanadate and was found to exist in some mycoplasmas.