Lorentz K, Assel K
Enzyme. 1975;20(4):248-56. doi: 10.1159/000458945.
Acid phosphatases from human tissues were investigated with respect to the cleavage of six different aryl phosphates. The enzymes, except the prostatic one, showed increasing Km values with increasing substrate concentrations at a constant pH. Electrophilic substitution of the aromatic ring lowered the reaction velocity, but apparently did not change the Km. The optimum hydrolysis was at pH 3.0--6.0 without any regular pattern, which could depend on the substrate configuration.
针对六种不同芳基磷酸酯的裂解情况，对来自人体组织的酸性磷酸酶进行了研究。除前列腺酸性磷酸酶外，在恒定pH条件下，随着底物浓度的增加，这些酶的米氏常数（Km）值也增加。芳环的亲电取代降低了反应速度，但显然并未改变米氏常数。最佳水解pH值在3.0至6.0之间，无任何规律模式，这可能取决于底物构型。
