Section 17
Chapter 16,646

Phenylalanyl-tRNA and seryl-tRNA synthetases from baker's yeast. Substrate specificity with regard to ATP analogs and mechanism of the aminoacylation reaction

Freist, W.; von der Haar, F.; Sprinzl, M.; Cramer, F.

European Journal of Biochemistry 64(2): 389-393


ISSN/ISBN: 0014-2956
PMID: 776617
DOI: 10.1111/j.1432-1033.1976.tb10313.x
Accession: 016645023

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Eighteen analogs of ATP have been tested in the aminoacylation reaction of phenylalanyl-tRNA and seryl-tRNA synthetases from baker's yeast. Four compounds are substrates for phenylalanyl-tRNA synthetase, five for seryl-tRNA synthetase, one compound is an inhibitor for both enzymes; their Km and Ki and V values have been determined. The substrate specificity shows that for the catalytic action of both enzymes with these substrates positions 6, 7, 8 and 9 of the purine moiety and positions 2' and 3' of the ribose moiety are important.

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