Abstract
Phosphate analogs have been known to inhibit competitively various phosphatases and phospholipase C and D. We found for the first time that only beryllium fluoride (BeF x ) among the phosphate analogs studied inhibits Bacillus cereus sphingomyelinase (SMase) activity. The active inhibitory species proved to be not BeF 3 − but BeF 2 by the measurement of SMase activity and of 19F NMR spectroscopy in the presence of a fixed concentration of BeCl 2 and different concentrations of NaF, although both the species have been reported for other kinds of enzymes. The result of kinetic experiment also indicated that the BeF x binds in the vicinity of the essential binding site for the substrate and that the Mg 2+ binding to SMase is essential for the binding of BeF x to the enzyme.
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