title: Phenylalanyl-tRNA and seryl-tRNA synthetases from baker's yeast. Substrate specificity with regard to ATP analogs and mechanism of the aminoacylation reaction.
abstract: 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.
mesh_terms: D000255:Adenosine Triphosphate / Q000031:analogs & derivatives*; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D007700:Kinetics; D010652:Phenylalanine-tRNA Ligase / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D012714:Serine-tRNA Ligase / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D000255:Adenosine Triphosphate; D000604:Amino Acyl-tRNA Synthetases; D012714:Serine-tRNA Ligase; D010652:Phenylalanine-tRNA Ligase