Mejdoub H, Kern D, Giegé R, Ebel J P, Boulanger Y, Reinbolt J
Biochemistry. 1987 Apr 7;26(7):2054-9. doi: 10.1021/bi00381a039.
Aspartyl-tRNA synthetase from bakers' yeast gives an unstable complex with the cognate adenylate, which reacts after dissociation with amino acid side chains of the protein. This leads to a covalent incorporation of aspartic acid into aspartyl-tRNA synthetase via amide or ester bonds formed between the alpha-carboxyl group of activated aspartic acid and accessible lysines, serines, and threonines. This property is used to label the peptides at the surface of the enzyme. The main labeled residues have been identified, and their location in the primary structure is discussed in relation to structural properties of aspartyl-tRNA synthetase.
面包酵母中的天冬氨酰 - tRNA合成酶与同源腺苷酸形成不稳定复合物，该复合物在解离后与蛋白质的氨基酸侧链发生反应。这导致天冬氨酸通过活化天冬氨酸的α - 羧基与可及的赖氨酸、丝氨酸和苏氨酸之间形成的酰胺键或酯键共价掺入天冬氨酰 - tRNA合成酶中。这一特性被用于标记酶表面的肽段。已鉴定出主要的标记残基，并结合天冬氨酰 - tRNA合成酶的结构特性讨论了它们在一级结构中的位置。
