Covalent attachment of aspartic acid to yeast aspartyl‐tRNA synthetase induced by the enzyme

FEBS Letters

Giegé, R.¹  Lorber, B.¹  Ebel, J.-P.¹  Kern, D.¹ 

[1] Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire de CNRS, 15, rue René Descartes, 67084 Strasbourg Cédex, France

关键词: Aminoacyl-tRNA synthetase;    Aspartyl-tRNA synthetase;    Amino acid activation;    Aspartic acid;    Protein modification;   

DOI  :  10.1016/0014-5793(82)80705-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Aspartic acid can be covalently linked to yeast aspartyl-tRNA synthetase and to other proteins, in the absence of tRNA, under conditions where the synthetase activates the amino acid into aspartyl-adenylate, i.e., in the presence of ATP and MgCl₂. The linkage between aspartic acid and the protein is acid and alkali resistant; thus it is likely a peptide-like amide bond formed between the activated carboxylate group of aspartic acid and the primary amine function of the side chain of lysine residues.

【 授权许可】

Unknown