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Acid Metallophosphatase from the Ameba Amoeba proteus

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Abstract

Tartrate-resistant acid phosphatase (TR-AcPh) from the ameba Amoeba proteus is represented by 3 bands (electromorphs) revealed after disk-electrophoresis in PAAG, using 2-naphthylphosphate as substrate. The presence of 50 mmol/l MgCl2 or CaCl2 in the incubation mixture increases activities of all electromorphs of TR-AcPh, while of ZnCl2, of two of them. The activity of the TR-AcPh electromorphs also rose after the 30-min incubation of the gels in MgCl2, CaCl2 or ZnCl2 (10 and 100 mM) before gel staining. However, 1 M ZnCl2, unlike 1 M CaCl2 or 1 M MgCl2, partly inactivated two out of three TR-AcPh electromorphs. The TR-AcPh electromorphs were inhibited by 1,10-phenanthroline (1,10-Ph), EDTA, and EGTA (all at a concentration of 5 mM) faster than by H2O2 (10 mM). The inactivation of the TR-AcPh electromorphs by the chelating agents did not depend (EGTA) or nearly did not depend (EDTA, 1,10-Ph) on their concentration (0.05, 0.5, and 5 mM). Out of 5 tested ions (Mg2+, Ca2+, Fe2+, Fe3+, and Zn2+), only Zn ions reactivated the TR-AcPh electromorphs inactivated by 1,10-Ph, EDTA or EGTA. The TR-AcPh electromorphs were reactivated worse after inactivation by EGTA than by EDTA or 1,10-Ph. It is suggested that the active site of TR-AcPh contains the zinc ion essential for catalytic activity of this enzyme, i.e., TR-AcPh of A. proteus is a metallophosphatase performing the phosphomonoesterase activity in acidic medium.

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  1. Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia

    V. A. Sopina

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Sopina, V.A. Acid Metallophosphatase from the Ameba Amoeba proteus . Journal of Evolutionary Biochemistry and Physiology 40, 28–36 (2004). https://doi.org/10.1023/B:JOEY.0000031002.56892.d6

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