Purification and Characterization of a Novel Thermostable Extracellular Protein Tyrosine Phosphatase from Metarhizium anisopliae Strain CQMa102
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An extracellular phosphatase was purified to homogeneity from the entomopathogenic fungus <I>Metarhizium anisopliae</I> with a 41.0% yield. The molecular mass and isoelectric point of the purified enzyme were about 82.5 kDa and 9.5 respectively. The optimum pH and temperature were about 5.5 and 75 °C when using <I>O</I>-phospho-<small>L</small>-tyrosine as substrate. The protein displayed high stability in a pH range 3.0–9.5 at 30 °C and was remarkably thermostable at 70 °C. The purified enzyme showed high activity on <I>O</I>-phospho-<small>L</small>-tyrosine and protein tyrosine phosphatase substrate monophosphate (a specific substrate of protein tyrosine phosphatase). Although one peptide of the phosphatase shared identity with one alkaline phosphatase of <I>Neurospora crassa</I>, its substrate specificity and inhibitor sensitivity indicate that the enzyme is a protein tyrosine phosphatase.
- Agricultural and Biological Chemistry
Agricultural and Biological Chemistry 70(8), 1961-1968, 2006-08-23
Japan Society for Bioscience, Biotechnology, and Agrochemistry