Acid phosphatase purified from Mycoplasma fermentans has protein tyrosine phosphatase-like activity.
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.
Shibata
K
K
Department of Oral Bacteriology, Hokkaido University School of Dentistry, Sapporo, Japan.
Noda
M
M
Sawa
Y
Y
Watanabe
T
T
D000135:Acid Phosphatase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D009174:Mycoplasma / Q000201:enzymology; D016858:Mycoplasma fermentans / Q000201:enzymology*; D019000:Phosphotyrosine; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism; D014443:Tyrosine / Q000031:analogs & derivatives / Q000378:metabolism
D019000:Phosphotyrosine; D014443:Tyrosine; D000135:Acid Phosphatase; D017027:Protein Tyrosine Phosphatases