Burns G R, Galanopoulou E, Wynn C H
Biochem J. 1977 Oct 1;167(1):223-7. doi: 10.1042/bj1670223.
Arylsulphatase II of Aspergillus oryzae exhibits both hydrolytic and sulphotransferase activities. The kinetic data suggest the formation of an intermediate covalent enzyme-sulphate complex with transfer of sulphate from donor to acceptor proceeding via a Ping Pong mechanism. The unusual kinetic behaviour when 2-hydroxy-5-nitrophenyl sulphate is the substrate is also consistent with this mechanism.
米曲霉的芳基硫酸酯酶 II 具有水解和磺基转移酶活性。动力学数据表明,通过乒乓机制,从供体到受体的硫酸盐转移过程中会形成一种中间共价酶 - 硫酸盐复合物。当以 2 - 羟基 - 5 - 硝基苯硫酸酯为底物时的异常动力学行为也与该机制一致。