Phenylalanyl-tRNA and seryl-tRNA synthetases from baker's yeast. Substrate specificity with regard to ATP analogs and mechanism of the aminoacylation reaction.
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.
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
D000255:Adenosine Triphosphate; D000604:Amino Acyl-tRNA Synthetases; D012714:Serine-tRNA Ligase; D010652:Phenylalanine-tRNA Ligase