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Inhibition of Family II Pyrophosphatases by Analogs of Pyrophosphate and Phosphate

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Abstract

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 K i ≈ 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 (K i = 1–6 mM). The value of K i 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.

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Correspondence to A. A. Baykov.

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Translated from Biokhimiya, Vol. 70, No. 8, 2005, pp. 1099–1103.

Original Russian Text Copyright © 2005 by Zyryanov, Lahti, Baykov.

Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM04-329, March 27, 2005.

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Zyryanov, A.B., Lahti, R. & Baykov, A.A. Inhibition of Family II Pyrophosphatases by Analogs of Pyrophosphate and Phosphate. Biochemistry (Moscow) 70, 908–912 (2005). https://doi.org/10.1007/s10541-005-0201-5

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  • DOI: https://doi.org/10.1007/s10541-005-0201-5

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