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Kinetics of Inhibition of Green Crab (Scylla Serrata) Alkaline Phosphatase by Sodium (2,2′-bipyridine) Oxodiperoxovanadate

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Abstract

Green crab (Scylla serrata) alkaline phosphatase (EC 3.1.3.1) is a metalloenzyme, which catalyzes the nonspecific hydrolysis of phosphate monoesters. The kinetics of inhibition of the enzyme by sodium (2, 2′-bipyridine) oxodiperoxovanadate, pV(bipy), has been studied. The time course of the hydrolysis of p-nitrophenyl-phosphate catalyzed by the enzyme in the presence of different pV(bipy) concentrations showed that at each pV(bipy) concentration, the rate decreased with increasing time until a straight line was approached, the straight line slopes are the same for all concentrations. The results suggest that the inhibition of the enzyme by pV(bipy) is a slow, reversible reaction with fractional remaining activity. The microscopic rate constants are determined for the reaction of inhibitor with the enzyme.

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Authors and Affiliations

  1. Department of Biology, Xiamen University, Xiamen, 361005, P. R. China

    Xing-Wang Zhou, Zong-Lai Zhuang & Qing-Xi Chen

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  1. Xing-Wang Zhou
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  2. Zong-Lai Zhuang
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  3. Qing-Xi Chen
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Correspondence to Qing-Xi Chen.

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Zhou, XW., Zhuang, ZL. & Chen, QX. Kinetics of Inhibition of Green Crab (Scylla Serrata) Alkaline Phosphatase by Sodium (2,2′-bipyridine) Oxodiperoxovanadate. J Protein Chem 18, 735–740 (1999). https://doi.org/10.1023/A:1020621332377

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  • DOI: https://doi.org/10.1023/A:1020621332377

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