Franks D J, Tunnicliff G, Ngo T T
Biochim Biophys Acta. 1980 Feb 14;611(2):358-62. doi: 10.1016/0005-2744(80)90072-8.
Rat brain adenylate cyclase (ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1) activity was markedly reduced when the enzyme was preincubated at 23 degrees C for periods up to 30 min with phenylglyoxyal (2.5-20 mM), an agent that binds specifically to arinyl residues. The kinetics indicated the interaction of phenylgloxal with one arginyl residue was responsible for the inactivation. Protection of inactivation of the enzyme by phenylglyoxal was attained in the presence of ATP and to a lesser extent by ADP and 5'-AMP but not by cyclic-AMP or Mg2+. In addition, 2,3-butanedione and 1,2-hexanedione, compounds that also react with arginyl residues, each inactivated adenylate cyclase to varying degrees. Furthermore, this inactivation was enhanced in the presence of borate ions. These observations strongly suggest that brain adenylate cyclase possesses essential arginyl residues.
当大鼠脑腺苷酸环化酶（ATP 焦磷酸裂解酶（环化），EC 4.6.1.1）与苯乙二醛（2.5 - 20 mM）在23℃预孵育长达30分钟时，其活性显著降低，苯乙二醛是一种特异性结合芳基残基的试剂。动力学表明苯乙二醛与一个精氨酰残基的相互作用导致了失活。在ATP存在的情况下可实现对苯乙二醛使该酶失活的保护，ADP和5'-AMP在较小程度上也有保护作用，但环磷酸腺苷或Mg2+则无此作用。此外，2,3 - 丁二酮和1,2 - 己二酮这两种也与精氨酰残基反应的化合物，各自都不同程度地使腺苷酸环化酶失活。此外，在硼酸根离子存在的情况下这种失活作用增强。这些观察结果有力地表明脑腺苷酸环化酶含有必需的精氨酰残基。
