Synthetic and editing reactions of aminoacyl-tRNA synthetases using cognate and non-cognate amino acid substrates

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• 作者：Nevena Cvetesic¹ ; Ita Gruic-Sovulj ; ^{gruic@chem.pmf.hr}
• 关键词：aaRS ; aminoacyl-tRNA synthetase ; aa-AMP ; aminoacyl-adenylate ; aa-tRNA ; aminoacyl-tRNA ; aaRS ; aa-AMP ; noncovalent complex of aaRS and aa-AMP ; aa-Ap ; amionoacyl-adenosine-5&prime ; -monophophate ; Ap ; adenosine-5&prime ; -monophophate ; ArgRS ; arginyl-tRNA synthetase ; GlnRS ; glutaminyl-tRNA synthetase ; GluRS ; glutamyl-tRNA synthetase ; His-tRNAHis ; histidyl-tRNAHis ; Ile-tRNAIle ; isoleucyl-tRNAIle ; IleRS ; isoleucyl-tRNA synthetase ; IPPase ; inorganic pyrophosphatase ; Leu-AMP ; leucyl-AMP ; Leu-tRNALeu ; leucyl
• 刊名：Methods
• 出版年：2017
• 出版时间：15 January 2017
• 年：2017
• 卷：113
• 期：Complete
• 页码：13-26
• 全文大小：1995 K
• 卷排序：113

文摘

Non-cognate amino acids are discriminated at aaRS synthetic and editing reactions. Use of [32P]-tRNA in analysis of the non-cognate reactions is valuable but needs strict controls. Single-turnover approaches are required for analysis of synthetic and editing reactions. Quantitative approaches with extracted rate constants are essential for mechanistic conclusions.