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Peptide‐Bond Synthesis on the Ribosome: No Free Vicinal Hydroxy Group Required on the Terminal Ribose Residue of Peptidyl‐tRNA
Author(s) -
Koch Miriam,
Huang Yiwei,
Sprinzl Mathias
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200801511
Subject(s) - residue (chemistry) , transfer rna , ribosome , peptide , chemistry , stereochemistry , peptide bond , p site , vicinal , ribose , peptidyl transferase , biochemistry , enzyme , rna , organic chemistry , gene
OH?—OH no! The generally accepted explanation for peptide transfer in ribosomal peptidyltransferase is that the 2′‐OH group of the adenosine residue (Ad) in the P site accepts a proton from the incoming α‐amino group and transfers it to the outgoing deacylated tRNA (left). However, it has now been shown that peptide transfer still takes place in the absence of the 2′‐hydroxy group (right: proposed alternative mechanism).