焦磷酸在酵母苯丙氨酰 - tRNA合成酶对大肠杆菌tRNA（Phe）进行氨酰化反应中的关键作用。
Crucial role of pyrophosphate in the aminoacylation of E. coli tRNA(Phe) by yeast phenylalanyl-tRNA synthetase.
作者信息
Khvorova A M, Wolfson A D
机构信息
A.N. Bakh Institute of Biochemistry, Moscow, Russia.
出版信息
FEBS Lett. 1992 Oct 19;311(2):139-42. doi: 10.1016/0014-5793(92)81385-y.
Rapid inactivation of the yeast phenylalanyl-tRNA synthetase in the course of aminoacylation of the heterologous E. coli tRNA(Phe) is observed. This inactivation occurs due to the formation of the tight complex of the enzyme with the pyrophosphate formed during the aminoacylation reaction. This complex is shown to be the normal intermediate of the reaction. Possible inactivation mechanism and correlation between structural differences of yeast and E. coli tRNAs(Phe) with the changes in the enzymatic mechanism of aminoacylation are discussed.
观察到在异源大肠杆菌苯丙氨酰 - tRNA（Phe）氨酰化过程中酵母苯丙氨酰 - tRNA合成酶的快速失活。这种失活是由于酶与氨酰化反应过程中形成的焦磷酸形成紧密复合物所致。该复合物被证明是反应的正常中间体。讨论了可能的失活机制以及酵母和大肠杆菌苯丙氨酰 - tRNA（Phe）的结构差异与氨酰化酶促机制变化之间的相关性。
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