Abstract
After the peptidyl-tRNA has occupied the P site and the aminoacyl-tRNA has been fully bound at the A site, the 3′-ends of the two tRNA residues are found close to each other in the region of the peptidyl transferase center (PTC) of the large ribosomal subunit. This is followed by a nucleophilic attack on the carbonyl group of the ester bond between the peptide residue and the tRNA moiety of the peptidyl-tRNA molecule by the amino group of the aminoacyl-tRNA molecule. As a result, an amide (peptide) bond is formed between the peptide residue and the aminoacyl-tRNA molecule (Fig. 11.1). The peptidyl-tRNA and the aminoacyl-tRNA are the substrates of this reaction. The peptidyl-tRNA is a donor substrate, and the aminoacyl-tRNA plays the part of an acceptor substrate. The products of the reaction are the deacylated tRNA in the P site and the peptidyl-tRNA with the peptide moiety elongated by one aminoacyl residue attached to the tRNA in the A site, as is shown schematically in Fig. 11.2.
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© 1999 Kluwer Academic/Plenum Publishers, New York
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Spirin, A.S. (1999). Elongation Cycle, Step II: Transpeptidation (Peptide Bond Formation). In: Ribosomes. Cellular Organelles. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-7817-8_11
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DOI: https://doi.org/10.1007/978-1-4615-7817-8_11
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