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  • Title: Threonyl-tRNA, lysyl-tRNA and arginyl-tRNA synthetases from Baker's yeast. Substrate specificity with regard to ATP analogues.
    Author: Freist W, Sternbach H, von der Haar F, Cramer F.
    Journal: Eur J Biochem; 1978 Mar 15; 84(2):499-502. PubMed ID: 346350.
    Abstract:
    Sixteen analogues of ATP have been tested in the aminoacylation reaction of threonyl-tRNA, lysyl-tRNA, and arginyl-tRNA synthetases from baker's yeast. Two compounds are substrates for threonyl-tRNA and for lysyl-tRNA synthetases and five compounds for arginyl-tRNA synthetase. There are six inhibitors for threonyl-tRNA, nine for lysyl-tRNA, and six for arginyl-tRNA synthetase. Their Km and Ki values have been determined. Thus positions 2, 6, 7, 8 and 9 of the purine moiety and 2' and 3' of the sugar moiety of the ATP molecule are important for catalytic action of these aminoacyl-tRNA synthetases. Remarkably arginyl-tRNA synthetase is the first aminoacyl-tRNA synthetase which tolerates bulky substituents at the sugar moiety of ATP. These data fit with the idea that synthetases of subunit structure need magnesium-ion-ATP complexes with an anti conformation as substrates whereas single-chain enzymes accept this substrate in the syn conformation.
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