Studies on sulphatases. 13. The hydrolysis of substituted phenyl sulphates by the arylsulphatase of Alcaligenes metalcaligenes

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Abstract
The Michaelis constants and maximum velocity values were determined for a series of substituted phenyl sulfates. The affinity of enzyme for substrate and maximum velocity were enhanced by electrophilic and decreased by nucleophilic substituents. It is suggested that formation of the enzyme-substrate complex involves an electrostatic attraction between nucleophilic and electrophilic groups at the active site of the enzyme with the sulfur and ionized oxygen atom of the aryl sulphate of the substrate respectively.