title: [Autoadenylation of tryptophanyl-tRNA synthetase].
abstract: Incubation of bovine tryptophanyl-tRNA synthetase (EC 6.1.1.2) deprived of endogenous tryptophan, with [14C]ATP and without [gamma-32P]ATP, causes an appearance of radioactivity in protein due to formation of adenylated enzyme, [14C]AMP-E. Examination of the properties of the [14C]AMP-E thus obtained led to the conclusion that AMP is linked to the protein molecule via a macroergetic phosphoanhydride bond. ATP is formed when AMP-E is incubated with PPi. However, no tryptophanyl adenylate formation was observed when AMP-E was treated with tryptophan. The functional role of AMP-E remains obscure.
authors: T I
authors: TI
authors: Merkulova
authors: G K
authors: GK
authors: Kovaleva
authors: L L
authors: LL
authors: Kiselev
mesh_terms: D000249:Adenosine Monophosphate / Q000031:analogs & derivatives* / Q000378:metabolism; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D002855:Chromatography, Thin Layer; D004795:Enzyme Stability; D007700:Kinetics; D013379:Substrate Specificity; D014369:Tryptophan-tRNA Ligase / Q000378:metabolism*
chemical_list: D000249:Adenosine Monophosphate; D000604:Amino Acyl-tRNA Synthetases; D014369:Tryptophan-tRNA Ligase
vernacular_title: Autoadenilirovanie triptofanil-tRNK-sintetazy.