异亮氨酰 - tRNA合成酶失活与来自大肠杆菌的tRNAIle的氨酰化程度
Isoleucyl-tRNA synthetase inactivation and the extent of aminoacylation of tRNAIle from Escherichia coli.
作者信息
Marashi F, Harris C L
出版信息
Biochim Biophys Acta. 1977 Jul 5;477(1):84-8. doi: 10.1016/0005-2787(77)90162-9.
PMID:328047
Abstract
A difference in isoleucine acceptance between normal and sulfur-deficient tRNA from Escherichia coli C6 (rel-, met-, cys-) was eliminated when more isoleucyl-tRNA synthetase was added at the reaction plateau. Enzymatic deacylation was similar for both tRNAs. These results suggest that enzyme inactivation caused a premature reaction plateau which was not predicted by the rates of acylation and deacylation.
摘要
当在反应平稳期添加更多异亮氨酰 - tRNA合成酶时，来自大肠杆菌C6（rel - ，met - ，cys - ）的正常tRNA和缺硫tRNA之间异亮氨酸接受能力的差异消除了。两种tRNA的酶促脱酰基作用相似。这些结果表明，酶失活导致了一个过早出现的反应平稳期，这是酰化和脱酰化速率无法预测的。
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