Inhibition of Family II Pyrophosphatases by Analogs of Pyrophosphate and Phosphate
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Imidodiphosphate (the pyrophosphate analog containing a nitrogen atom in the bridge position instead of oxygen) is a potent inhibitor of family II pyrophosphatases from Streptococcus mutans and Streptococcus gordonii (inhibition constant Ki ≈ 10 µM), which is slowly hydrolyzed by these enzymes with a catalytic constant of ≈1 min−1. Diphosphonates with different substituents at the bridge carbon atom are much less effective (Ki = 1–6 mM). The value of Ki for sulfate (a phosphate analog) is only 12 mM. The inhibitory effect of the pyrophosphate analogs exhibits only a weak dependence on the nature of the metal ion (Mn, Mg, or Co) bound in the active site.
Key wordspyrophosphatase diphosphonate phosphate inhibition family II Streptococcus mutans Streptococcus gordonii
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