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A random sequential mechanism for arginyl transfer ribonucleic acid synthetase of Escherichia coli.

作者信息

Papas T S, Peterkofsky A

出版信息

Biochemistry. 1972 Nov 21;11(24):4602-8. doi: 10.1021/bi00774a029.

DOI:10.1021/bi00774a029
PMID:4347387
Abstract
摘要

相似文献

1
A random sequential mechanism for arginyl transfer ribonucleic acid synthetase of Escherichia coli.大肠杆菌精氨酰转移核糖核酸合成酶的随机顺序机制
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Phenylalanyl transfer ribonucleic acid synthetase from Escherichia coli. Reaction parameters and order of substrate addition.
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Interactions of tyrosyl transfer ribonucleic acid synthetase from Escherichia coli with its substrates. Inhibition by transfer ribonucleic acid.来自大肠杆菌的酪氨酰转移核糖核酸合成酶与其底物的相互作用。被转移核糖核酸抑制。
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Histidine regulation in Salmonella typhimurium. 13. Nucleotide sequence of histidine transfer ribonucleic acid.鼠伤寒沙门氏菌中的组氨酸调控。13. 组氨酸转移核糖核酸的核苷酸序列。
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Effect of transfer ribonucleic acid on the rate law and mechanism of the adenosine triphosphate--pyrophosphate isotope exchange reaction of an aminoacyl transfer ribonucleic acid synthetase.转移核糖核酸对氨酰转移核糖核酸合成酶的三磷酸腺苷-焦磷酸同位素交换反应的速率定律及机制的影响。
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Phenylalanyl transfer ribonucleic acid synthetase from Escherichia coli. Analysis of the adenosine triphosphate binding site.
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Transfer ribonucleic acid synthetase catalyzed deacylation of aminoacyl transfer ribonucleic acid in the absence of adenosine monophosphate and pyrophosphate.在没有一磷酸腺苷和焦磷酸的情况下，转移核糖核酸合成酶催化氨酰基转移核糖核酸的去酰化作用。
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Rapid deacylation by isoleucyl transfer ribonucleic acid synthetase of isoleucine-specific transfer ribonucleic acid aminoacylated with valine.异亮氨酰转移核糖核酸合成酶对用缬氨酸氨酰化的异亮氨酸特异性转移核糖核酸的快速去酰化作用。
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Control of arginine biosynthesis in Escherichia coli: characterization of arginyl-transfer ribonucleic acid synthetase mutants.大肠杆菌中精氨酸生物合成的调控：精氨酰转移核糖核酸合成酶突变体的特性分析
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On the active site topography of isoleucyl transfer ribonucleic acid synthetase of Escherichia coli B.关于大肠杆菌B异亮氨酰转移核糖核酸合成酶的活性位点拓扑结构
Biochemistry. 1973 Mar 13;12(6):1150-9. doi: 10.1021/bi00730a021.

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Structure-function relationship of arginyl-tRNA synthetase from Escherichia coli: isolation and characterization of the argS mutation MA5002.
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