Inhibition of Family II Pyrophosphatases by Analogs of Pyrophosphate and Phosphate |
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Authors: | A?B?Zyryanov R?Lahti Email author" target="_blank">A?A?BaykovEmail author |
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Institution: | (1) Belozersky Institute of Physico-Chemical Biology and Faculty of Chemistry, Lomonosov Moscow State University, 119899 Moscow, Russia;(2) Department of Biochemistry and Food Chemistry, University of Turku, Turku, FIN-20500, Finland |
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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 Ki approximately 10 microM), which is slowly hydrolyzed by these enzymes with a catalytic constant of approximately 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. |
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Keywords: | pyrophosphatase diphosphonate phosphate inhibition family II Streptococcus mutans Streptococcus gordonii |
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