Effect of cytidine-5'-monophosphate on peptidyl transferase activity.
The transfer reaction with pA-fMet as a donor substrate is strongly stimulated by CMP, whereas the transfer reaction with CpApCpCpA-acLeu as a donor substrate is inhibited by CMP. These results indicate that the donor site of peptidyl transferase contains specific binding sites for the terminal adenosine and for the cytidylic acid residue in the terminal sequence CpCpA of tRNA and that an attachment of proper nucleotides to the donor site induces a conformational change in peptidyl transferase.
D000217:Acyltransferases / Q000378:metabolism*; D000227:Adenine Nucleotides / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001665:Binding Sites; D003568:Cytidine Monophosphate / Q000494:pharmacology*; D003597:Cytosine Nucleotides / Q000494:pharmacology*; D004789:Enzyme Activation; D009239:N-Formylmethionine / Q000378:metabolism; D010458:Peptidyl Transferases / Q000378:metabolism*; D011487:Protein Conformation / Q000187:drug effects; D012343:RNA, Transfer / Q000378:metabolism; D012270:Ribosomes / Q000201:enzymology*; D013329:Structure-Activity Relationship
D000227:Adenine Nucleotides; D000900:Anti-Bacterial Agents; D003597:Cytosine Nucleotides; D009239:N-Formylmethionine; D012343:RNA, Transfer; D000217:Acyltransferases; D010458:Peptidyl Transferases; D003568:Cytidine Monophosphate