Aminoacylation of rat liver transfer RNA with L-penicillamine. On the specificity of the aminoacylation reaction.
L-]14C]Penicillamine is bound to RNA from rat liver in an in vitro reaction catalyzed by rat liver aminoacyl-tRNA synthetases. Addition of certain naturally occuring amino acids results in a significant decrease of L-penicillamine binding. The most potent inhibitor of this binding is L-valine, followed by L-isoleucine and L-threonine. Amino acids without structural relationship to L-penicillamine in the non-functional part of the molecule, such as L-phenylalanine, are ineffective. Studies on the competition of L-penicillamine and L-isoleucine, respectively, with L-valine demonstrate the high specificity of the aminoacylation reaction. They show that the change of L-penicillamine binding to tRNA Val is considerably lower than that of L-valine.
D000596:Amino Acids / Q000494:pharmacology; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D010396:Penicillamine / Q000378:metabolism*; D012343:RNA, Transfer / Q000378:metabolism*; D051381:Rats; D012260:Ribonucleases; D013329:Structure-Activity Relationship
D000596:Amino Acids; D012343:RNA, Transfer; D012260:Ribonucleases; D000604:Amino Acyl-tRNA Synthetases; D010396:Penicillamine