Induced hydrolytic activity of yeast phenylalanyl-tRNA synthetase by tRNAPhe-CC.
"Induced hydrolysis" a new hydrolytic activity, was found by measuring AMP-production during aminoacylation of tRNAPhe-CCA by yeast phenylalanyl-tRNA synthetase in the presence of tRNAPhe-CC under conditions of low ionic strength at pH 8.5. Experiments using the elongation factor Tu . GTP provide evidence that transfer of phenylalanine to the tRNAPhe-CCA is followed by rapid hydrolysis in the presence of tRNAPhe-CC. A simple mechanism shows good agreement with the experimental data.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism; D007700:Kinetics; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000378:metabolism; D010652:Phenylalanine-tRNA Ligase / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism / Q000494:pharmacology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013329:Structure-Activity Relationship
D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu; D000604:Amino Acyl-tRNA Synthetases; D010652:Phenylalanine-tRNA Ligase