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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase
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The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

机译:组氨酸-tRNA合成酶在原子水平上进行氨酰化的第一步

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摘要

The crystal structure of an enzyme- substrate complex with histidyl-tRNA synthetase from Esch- erichia coli, ATP, and the amino acid analog histidinol is described and compared with the previously obtained en- zyme-product complex with histidyl-adenylate. An active site arginine, Arg-259, unique to all histidyl-tRNA synthetases, plays the role of the catalytic magnesium ion seen in seryl- tRNA synthetase. When Arg-259 is substituted with histidine, the apparent second order rate constant (k_cat/K_m) for the pyrophosphate exchange reaction and the aminoacylation reaction decreases 1,000-fold and 500-fold, respectively.
机译:描述了一种酶-底物复合物的晶体结构,该酶-底物复合物具有来自大肠杆菌,ATP和氨基酸类似物组氨醇的组氨酸-tRNA合成酶,并与先前获得的具有组氨酸-腺苷酸的酶-产物复合物进行了比较。所有组氨酸-tRNA合成酶都具有的活性位点精氨酸Arg-259发挥了在丝氨酰tRNA合成酶中所见的催化镁离子的作用。当用组氨酸取代Arg-259时,焦磷酸盐交换反应和氨基酰化反应的表观二阶速率常数(k_cat / K_m)分别降低1000倍和500倍。

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