peptidyltransferase

pep·tid·yl·trans·fer·ase

(pep-ti'dil-trans'fĕr-ās),
The enzyme responsible for the formation of the peptide bond on the ribosome during protein biosynthesis, peptidyl-tRNA1 + aminoacyl-tRNA2 → tRNA1 + peptidylaminoacyl-tRNA2.
References in periodicals archive ?
However, rapidly growing mycobacteria can develop resistance by mutations in the peptidyltransferase region of the 23S ribosome gene (24).
DON binds to RNA peptidyltransferase site and inhibits protein synthesis (De Walle et al., 2010).
Ribosomal inactivation can be induced by a large family of ribonucleolytic proteins that cleave 28s ribosomal RNA at single phosphodiester bonds within a universally conserved sequence known as the sarcin-ricin loop, which leads to the dysfunction of peptidyltransferase and subsequent global translational arrest [7,8].
T Caskey, "Peptidyltransferase inhibition by trichodermin," The Journal of Biological Chemistry, vol.
Kinetics of inhibition of rabbit reticulocyte peptidyltransferase by anisomycin and sparsomycin.
The cycloheximide inhibits peptidyltransferase, which is responsible for peptide bond synthesis during translation (26).
Erythromycin binds to the ribosome but, unlike larger macrolides, appears to cause dissociation of the peptidyl-tRNA, rather than blocking the peptidyltransferase activity (11).