title: [Fragment reaction catalyzed by E. coli ribosomes].
abstract: It has been shown that 50S subunits of E. coli MRE-600 ribosomes catalyze the reaction of N-(formyl)-methionyl ester of adenosine 5'-phosphate acting as peptide donor, with Phe-tRNA or CACCA-Phe serving as a peptide acceptor. The reaction is stimulated by cytidine 5'phosphate and inhibited by lincomycin, puromycin and chloramphenicol. The obtained results show that the structure of the donor site of peptidyltransferase is completely assembled on the 50S subunit and 30S subunit is not required for its formation.
mesh_terms: D002701:Chloramphenicol / Q000494:pharmacology; D003568:Cytidine Monophosphate / Q000494:pharmacology; D004926:Escherichia coli / Q000378:metabolism*; D007700:Kinetics; D008034:Lincomycin / Q000494:pharmacology; D010458:Peptidyl Transferases / Q000378:metabolism; D014176:Protein Biosynthesis / Q000187:drug effects*; D011691:Puromycin / Q000494:pharmacology; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism*
chemical_list: D011691:Puromycin; D002701:Chloramphenicol; D008034:Lincomycin; D010458:Peptidyl Transferases; D003568:Cytidine Monophosphate
vernacular_title: Issledovanie fragmentnoĭ reaktsii, kataliziruemoĭ ribosomami E. coli.