来自大肠杆菌的甲硫氨酰 - tRNA合成酶的作用机制。1. 作为配体、离子和pH函数的tRNAMet结合的荧光研究。 - Suppr

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超能文献

The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. 1. Fluorescence studies on tRNAMet binding as a function of ligands, ions and pH.

作者信息

Blanquet S, Iwatsubo M, Waller J P

出版信息

Eur J Biochem. 1973 Jul 2;36(1):213-26. doi: 10.1111/j.1432-1033.1973.tb02903.x.

DOI:10.1111/j.1432-1033.1973.tb02903.x

PMID:4581817

Abstract

摘要

相似文献

The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. 1. Fluorescence studies on tRNAMet binding as a function of ligands, ions and pH.来自大肠杆菌的甲硫氨酰 - tRNA合成酶的作用机制。1. 作为配体、离子和pH函数的tRNAMet结合的荧光研究。

Eur J Biochem. 1973 Jul 2;36(1):213-26. doi: 10.1111/j.1432-1033.1973.tb02903.x.

The mechanism of action of methionyl-tRNA synthetase. 3. Ion requirements and kinetic parameters of the ATP-PPi exchange and methionine-transfer reactions catalyzed by the native and trypsin-modified enzymes.甲硫氨酰 - tRNA合成酶的作用机制。3. 天然酶和胰蛋白酶修饰酶催化的ATP - 焦磷酸交换反应以及甲硫氨酸转移反应的离子需求和动力学参数。

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The mechanism of action of methionyl-tRNA synthetase. 2. Interaction of the enzyme with specific and unspecific tRNAs.

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Antico-operative binding of bacterial and mammalian initiator tRNAMet to methionyl-tRNA synthetase from escherichia coli.细菌和哺乳动物起始甲硫氨酸转运核糖核酸（tRNAMet）与大肠杆菌甲硫氨酰-tRNA合成酶的抗协同结合

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Enzymatic deacylation of methionyl-tRNAfMet catalysed by methionyl, isoleucyl and phenylalanyl-tRNA synthetases.

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The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. Equilibrium-dialysis studies on the binding of methionine, ATP and ATP-Mg2+ by the native and trypsin-modified enzymes.来自大肠杆菌的甲硫氨酰 - tRNA合成酶的作用机制。关于天然酶和胰蛋白酶修饰酶对甲硫氨酸、ATP和ATP - Mg2+结合的平衡透析研究。

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The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. Mechanism of the amino-acid activation reaction catalyzed by the native and the trypsin-modified enzymes.来自大肠杆菌的甲硫氨酰 - tRNA合成酶的作用机制。天然酶和胰蛋白酶修饰酶催化的氨基酸活化反应机制。

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The aminoacylation of transfer ribonucleic acid. Recognition of methionine by Escherichia coli methionyl-transfer ribonucleic acid synthetase.转移核糖核酸的氨酰化作用。大肠杆菌甲硫氨酰转移核糖核酸合成酶对甲硫氨酸的识别。

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Isoleucyl transfer ribonucleic acid synthetase of Escherichia coli B. Effects of magnesium and spermine on the amino acid activation reaction.大肠杆菌B的异亮氨酰转移核糖核酸合成酶。镁和精胺对氨基酸活化反应的影响。

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Neutron-scattering studies of the binding of initiator tRNAMet to escherichia coli trypsin modified methionyl-tRNA synthetase.起始tRNA甲硫氨酸与经大肠杆菌胰蛋白酶修饰的甲硫氨酰-tRNA合成酶结合的中子散射研究

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A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation.附加在植物甲硫氨酰 - tRNA合成酶上的一个重复通用RNA结合结构域作为氨酰化的顺式作用辅因子。

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Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase.结晶态大肠杆菌甲硫氨酰 - tRNA(f)Met甲酰基转移酶的结构：与甘氨酰胺核糖核苷酸甲酰基转移酶的比较。

EMBO J. 1996 Sep 2;15(17):4749-58.

E. coli initiator tRNA analogs with different nucleotides in the discriminator base position.在鉴别碱基位置具有不同核苷酸的大肠杆菌起始tRNA类似物。

Nucleic Acids Res. 1982 Oct 25;10(20):6531-9. doi: 10.1093/nar/10.20.6531.

The role of the anticodon in the interaction between methionyl-tRNA synthetase and bacterial initiator tRNA.反密码子在甲硫氨酰 - tRNA合成酶与细菌起始tRNA相互作用中的作用。

Nucleic Acids Res. 1974 Feb;1(2):217-21. doi: 10.1093/nar/1.2.217.

Fast purification of a functional elongator tRNAmet expressed from a synthetic gene in vivo.体内从合成基因表达的功能性延伸因子tRNAmet的快速纯化。

Nucleic Acids Res. 1988 Aug 25;16(16):8095-6. doi: 10.1093/nar/16.16.8095.

Peptides at the tRNA binding site of the crystallizable monomeric form of E. coli methionyl-tRNA synthetase.大肠杆菌甲硫氨酰 - tRNA合成酶可结晶单体形式的tRNA结合位点处的肽段。

Nucleic Acids Res. 1987 Dec 23;15(24):10523-30. doi: 10.1093/nar/15.24.10523.

Selection of suppressor methionyl-tRNA synthetases: mapping the tRNA anticodon binding site.抑制性甲硫氨酰 - tRNA合成酶的选择：绘制tRNA反密码子结合位点图谱。

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Involvement of the size and sequence of the anticodon loop in tRNA recognition by mammalian and E. coli methionyl-tRNA synthetases.反密码子环的大小和序列在哺乳动物和大肠杆菌甲硫氨酰 - tRNA合成酶识别tRNA中的作用。

Nucleic Acids Res. 1992 Sep 25;20(18):4741-6. doi: 10.1093/nar/20.18.4741.

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