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从大鼠肝脏中分离出的均一精氨酰 - 赖氨酰 - tRNA合成酶复合物的特性。赖氨酰 - tRNA合成酶的动力学机制。

Characterization of a homogeneous arginyl- and lysyl-tRNA synthetase complex isolated from rat liver. Kinetic mechanism for lysyl-tRNA synthetase.

作者信息

Hilderman R H, Zimmerman J K, Dang C V, Grothusen J R

出版信息

J Biol Chem. 1983 Nov 25;258(22):13592-6.

PMID:6315704
Abstract

Bisubstrate kinetics and end product and dead end inhibition studies were performed on lysyl-tRNA synthetase isolated from rat liver. The kinetic patterns obtained are consistent with a sequential ordered mechanism of substrate addition, tRNA bound first, followed by lysine, and then by ATP. Pyrophosphate and AMP are released in a random fashion with aminoacylated tRNA the last product to dissociate from the enzyme. This is the first report of a kinetic mechanism for lysyl-tRNA synthetase.

摘要

对从大鼠肝脏中分离出的赖氨酰 - tRNA合成酶进行了双底物动力学以及终产物和无效抑制研究。所获得的动力学模式与底物添加的有序序列机制一致，即tRNA首先结合，随后是赖氨酸，然后是ATP。焦磷酸和AMP以随机方式释放，氨酰化tRNA是最后从酶上解离的产物。这是关于赖氨酰 - tRNA合成酶动力学机制的首次报道。

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