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Autoadenylation of tryptophanyl-tRNA synthetase

Merkulova, T.I.; Kovaleva, G.K.; Kiselev, L.L.

Molekuliarnaia Biologiia 21(3): 769-776

1987

ISSN/ISBN: 0026-8984
PMID: 3657776
Document Number: 289224
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.

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