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应用
氨酰基tRNA合成酶可用于蛋白质合成和调节的研究。
生化/生理作用
氨酰基tRNA合成酶能够将氨基酸连接到其相应的tRNA上，这对于蛋白质合成至关重要。两类氨酰基tRNA合成酶都是多结构域蛋白。
其他说明
氨基酸活化酶的混合物
EC连接酶亚类6.1.1
质量
粗品
单位定义
一个酶活性单位是指在pH 7.6、37°C条件下，在10分钟内激活并将 1.0 皮摩尔（10-12 摩尔）标记氨基酸连接至tRNA（使用的氨基酸：L-精氨酸）上所需的酶量。
外形
溶于50%甘油中含有10 mM Tris HCl, pH 7.2, 10 mM MgCl2、30 mM 2-巯基乙醇和10 mM KCl
分析说明
通过缩二脲法测定的蛋白质。
警示用语：
Warning
危险声明
危险分类
Skin Sens. 1
储存分类代码
10 - Combustible liquids
WGK
WGK 2
法规信息
常规特殊物品
Irem Avcilar-Kucukgoze et al.
Cell chemical biology, 27(7), 839-849 (2020-06-20)
Arginyltransferase ATE1 mediates posttranslational arginylation and plays key roles in multiple physiological processes. ATE1 utilizes arginyl (Arg)-tRNAArg as the donor of Arg, putting this reaction into a direct competition with the protein synthesis machinery. Here, we address the question of
C L Harris
Journal of bacteriology, 169(6), 2718-2723 (1987-06-01)
Aminoacyl-tRNA synthetases from several strains of Escherichia coli are shown to elute as a high-molecular-weight complex on 6% agarose columns (Bio-Gel A-5M). In contrast, very little synthetase activity was observed in such complexes on Sephadex G-200 columns, suggesting that these
C R Woese et al.
Microbiology and molecular biology reviews : MMBR, 64(1), 202-236 (2000-03-08)
The aminoacyl-tRNA synthetases (AARSs) and their relationship to the genetic code are examined from the evolutionary perspective. Despite a loose correlation between codon assignments and AARS evolutionary relationships, the code is far too highly structured to have been ordered merely
Ziwei Liu et al.
PLoS genetics, 17(7), e1009675-e1009675 (2021-07-30)
Emerging evidence indicates that tRNA-derived small RNAs (tsRNAs) are involved in fine-tuning gene expression and become dysregulated in various cancers. We recently showed that the 22nt LeuCAG3´tsRNA from the 3´ end of tRNALeu is required for efficient translation of a
Lance W Rider et al.
The Journal of biological chemistry, 284(16), 10324-10333 (2009-01-14)
Dihydrouridine synthases (DUSs) are flavin-dependent enzymes that catalyze site-specific reduction of uracils in tRNAs. The mechanism of DUS 2 from Saccharomyces cerevisiae was studied. Previously published turnover rates for this DUS were very low. Our studies show that the catalytic
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