[Autoadenylation of tryptophanyl-tRNA synthetase].
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.
Merkulova
T I
TI
Kovaleva
G K
GK
Kiselev
L L
LL
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*
D000249:Adenosine Monophosphate; D000604:Amino Acyl-tRNA Synthetases; D014369:Tryptophan-tRNA Ligase
Autoadenilirovanie triptofanil-tRNK-sintetazy.