Peptidyl transferase activity in wheat germ ribosomes. Effect of some antibiotics.
The formation of N-acetyl-leucyl-puromycin in a "fragment reaction" catalyzed by 80 S ribosomes from wheat germ was characterized. The reaction product was identified by high-voltage electrophoresis. The fragment reaction is inhibited by sparsomycin, blasticidin S, gougerotin and to a lesser degree by amicetin and tetracycline. Formation of an acLeu-pentanucleotide-ribosomes complex was strongly stimulated by sparsomycin.
D000217:Acyltransferases / Q000378:metabolism*; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001665:Binding Sites; D002474:Cell-Free System; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D009843:Oligoribonucleotides / Q000378:metabolism; D010458:Peptidyl Transferases / Q000378:metabolism*; D010944:Plants / Q000187:drug effects / Q000201:enzymology*; D011691:Puromycin / Q000494:pharmacology; D012270:Ribosomes / Q000187:drug effects / Q000201:enzymology*; D013033:Sparsomycin / Q000494:pharmacology; D013752:Tetracycline / Q000494:pharmacology; D014908:Triticum / Q000187:drug effects / Q000201:enzymology
D000900:Anti-Bacterial Agents; D009843:Oligoribonucleotides; D011691:Puromycin; D013033:Sparsomycin; D000217:Acyltransferases; D010458:Peptidyl Transferases; D013752:Tetracycline; D008274:Magnesium