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Aminoacylation of tRNA Trp from beef liver, yeast and E. coli by beef pancrease tryptophan-tRNA ligase. Stoichiometry of tRNATrp binding.

M Dorizzi·G Merault·M Fournier·J Labouesse·G Keith·G Dirheimer·R H Buckingham
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Abstract

The Michaelis constants and the maximum velocities in the aminoacylation reaction of tRNATrp from beef liver, yeast and E. coli by pure beef pancreas tryptophan-tRNA ligase show that this mammalian enzyme recognizes and charges the two eucaryotic tRNAs with the same efficiency. The rate of aminoacylation of the procaryotic tRNATrp by the enzyme is three orders of magnitude lower. The pH optimum of aminoacylation is 8 for both eucaryotic tRNAs. The optimum magnesium concentration is different. The rate is maximum when magnesium concentration is stoichiometric to ATP concentration for tRNATrp from beef liver and 10 mM above ATP concentration for tRNATrp from yeast. The number of binding sites on the enzyme for the two eucaryotic tRNAs has been measured by equilibrium filtration on Sephadex G-100 and found equal to two.

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Adenosine TriphosphateAmino Acyl-tRNA SynthetasesAnimalsBinding SitesCattleEscherichia coliHydrogen-Ion ConcentrationKineticsLiverMagnesiumOsmolar ConcentrationPancreasRNA, BacterialRNA, TransferSaccharomyces cerevisiaeSpecies SpecificityTransfer RNA AminoacylationTryptophanTryptophan-tRNA LigaseJournal Article

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M Dorizzi, G Merault, M Fournier, J Labouesse, G Keith, G Dirheimer, R H Buckingham. 1977. Aminoacylation of tRNA Trp from beef liver, yeast and E. coli by beef pancrease tryptophan-tRNA ligase. Stoichiometry of tRNATrp binding.. https://doi.org/10.1093/nar%2F4.1.31

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