[Peptidyl transferase center of ribosomes. I. Difference in the substrate specificity of the acceptor and donor portions].

Autor: Popovkina SV, Zavgorodniĭ SG, Azhaev AV, Kotusov VV, Vigestane RIa
Jazyk: ruština
Zdroj: Molekuliarnaia biologiia [Mol Biol (Mosk)] 1978 Mar-Apr; Vol. 12 (2), pp. 397-403.
Abstrakt: Some model substrates of the peptidyl transferase centre of E. coli MRE-600 ribosomes were synthesised and tested in a cell-free system without a template. In these substances the nucleic bases were linked covalently with the ribose residue or had a limited rotation about the glycosidic bond. 3'(2')-O-(N-formylmethionyl)-8-bromoadenosine 5'-phosphate and 3'(2')-O-phenylalanyl-8,5'-anhydro-8-mercaptoadenosine were shown to possess a high peptide donor and acceptor activity correspondingly. Contrary to that 3'(2')-O-phenylalanyl-8-bromoadenosine was practically inactive as a peptide acceptor and 3'(2')-O-(N-formylmethionyl)-8,5'-anhydro-8-mercaptoadenosine had no peptide donor activity at all. PMR and CD spectra of the compounds synthesised were investigated. The significance of conformation of the model substrates on their activity is discussed.
Databáze: MEDLINE