Roy A B
Ciba Found Symp. 1979(72):177-90. doi: 10.1002/9780470720554.ch11.
Sulphatase A was first described as an arylsulphatase but was subsequently shown to have cerebroside sulphatase activity, bydrolysing galactose 3-sulphate residues in certain lipids. A characteristic feature of the arylsulphatase activity is the substrate-induced inactivation of the enzyme which occurs during the catalytic reaction. Present views of the course of this modification are considered. A similar modification of the enzyme does not occur during the cerebroside sulphatase reaction and the fall in velocity noted during most such assays can be explained by disappearance of substrate and accumulation of sulphate. Possible reasons for the difference between the two types of activity are considered. Sulphatase A also hydrolyses hexose sulphates at rates comparable to those of aryl sulphates. The specificity of sulphatase A towards its natural substrates, sulpholipids, is considered in the light of these findings.
硫酸酯酶A最初被描述为一种芳基硫酸酯酶,但随后被证明具有脑苷脂硫酸酯酶活性,可水解某些脂质中的半乳糖3-硫酸酯残基。芳基硫酸酯酶活性的一个特征是在催化反应过程中底物诱导的酶失活。文中考虑了对此修饰过程的当前观点。在脑苷脂硫酸酯酶反应过程中不会发生类似的酶修饰,并且在大多数此类测定中观察到的速度下降可以通过底物消失和硫酸盐积累来解释。文中考虑了两种活性类型之间差异的可能原因。硫酸酯酶A还以与芳基硫酸盐相当的速率水解己糖硫酸盐。根据这些发现,讨论了硫酸酯酶A对其天然底物硫脂的特异性。