Mechanistic studies of the hydrolysis of p-nitrophenyl sulfate catalyzed by arylsulfatase from Helix pomatia.

The kinetics of the hydrolysis of small aryl substrate p-nitrophenyl sulfate (p-NPS) catalyzed by arylsulfatase from Helix pomatia was studied at a wide range of temperatures as well as at ambient and elevated pressures. The employed kinetic assay techniques allow for the determination of activation entropy ( [image omitted]), activation enthalpy ( [image omitted]), as well as activation volume ( [image omitted]) which suggested associative interchange character of the sulfate ester hydrolysis. The pH dependence obtained for catalytic parameters suggests that two protonation/deprotonation reactions can occur and the optimum pH for the catalytic activity was also detected. [ABSTRACT FROM AUTHOR]