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. 1979;24(1):67-71.

Isatin-enzyme interactions. VII. Mechanism of inhibition of rat kidney alkaline phosphatase

B Singh, R Sharma, J P Nagpaul, R C Bansal, P Kumar
  • PMID: 436809

Isatin-enzyme interactions. VII. Mechanism of inhibition of rat kidney alkaline phosphatase

B Singh et al. Enzyme. 1979.

Abstract

Isatin has been found to inhibit rat kidney alkaline phosphatase (EC 3.1.3.1). The inhibition is dependent on isatin concentration and is of un-competitive type. The hydrolysis of disodium phenyl phosphate by the enzyme at different temperatures (17--37 degrees C) obeys the Arrhenius equation. Energy of activation in the absence and presence of isatin has been found to be 9.84 and 10.24 kCal/mol. The hyperbolic profile of isatin inhibition; the lowering of both Km and Vmax in the presence of isatin, and, small changes in enthalpy, free energy and entropy in the presence of isatin suggest a non-allosteric un-competitive inhibition of the enzyme.

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