Inhibition of alkaline phosphatase by surfactin, a natural chelating lipopeptide from Bacillus subtilis
Surfactin, an acidic lipopeptide of Bacillus subtilis, at 70 μM non-competitively inhibited alkaline phosphatase without its glycosyl-phosphatidylinositol anchor by 50%. Enzyme activity was restored by adding 50 μM ZnCl 2 and 1 mM MgCl2 confirming the chelating action of the free carboxyl groups of the Asp and Glu residues in the peptide moiety of surfactin.
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