Inhibition of aminoacyl-tRNA synthetases by the mycotoxin patulin.
The effect of patulin on tRNA aminoacylation has been determined. This mycotoxin inhibits the aminoacylation process by irreversibly inactivating aminoacyl-tRNA synthetases. At neutral and alkaline pH-values, the inactivation occurs mainly by modification of essential thiol groups of the protein, whereas at acidic pH, where the effect is the most pronounced, the modification of other amino acid residues cannot be excluded.
D000604:Amino Acyl-tRNA Synthetases / Q000037:antagonists & inhibitors*; D000818:Animals; D001126:Arginine-tRNA Ligase / Q000037:antagonists & inhibitors; D001226:Aspartate-tRNA Ligase / Q000037:antagonists & inhibitors; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D051379:Mice; D010365:Patulin / Q000494:pharmacology*; D010652:Phenylalanine-tRNA Ligase / Q000037:antagonists & inhibitors; D011485:Protein Binding; D011714:Pyrans / Q000494:pharmacology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D014637:Valine-tRNA Ligase / Q000037:antagonists & inhibitors
D011714:Pyrans; D010365:Patulin; D000604:Amino Acyl-tRNA Synthetases; D001226:Aspartate-tRNA Ligase; D001126:Arginine-tRNA Ligase; D010652:Phenylalanine-tRNA Ligase; D014637:Valine-tRNA Ligase