The Peptidyl transferase is an aminoacyltransferase (EC 22.214.171.124), and the primary enzymatic function of the ribosome which forms peptide links between adjacent amino acids using tRNAs during the translation process of protein biosynthesis.
Peptidyl transferase activity is carried out by the ribosome, and in particular, an RNA (not a protein) component of the ribosome. There are few protein complexes that act as peptidyl tranferases. Chloramphenicol binds to A2451 and A2452 residues in the 23S rRNA of the ribosome and inhibits peptide bond formation.
Transferases: acyltransferases (EC 2.3)
|2.3.1: other than amino-acyl groups|
|N-Acetylglutamate synthase - Choline acetyltransferase - Acetyl-Coenzyme A acetyltransferase - Dihydrolipoyl transacetylase - Acetyl-CoA C-acyltransferase - Beta-galactoside transacetylase - Carnitine O-palmitoyltransferase (CPT1, CPT2) - Acyltransferase like 2 - Chloramphenicol acetyltransferase - Aminolevulinic acid synthase - Beta-ketoacyl-ACP synthase - Glyceronephosphate O-acyltransferase - Lecithin-cholesterol acyltransferase - Histone acetyltransferase (P300/CBP) - Serotonin N-acetyl transferase|
|2.3.2 - Aminoacyltransferases||Gamma glutamyl transpeptidase - Peptidyl transferase - Transglutaminase (Tissue transglutaminase, Keratinocyte transglutaminase, Factor XIII)|
|2.3.3 - converted into alkyl on transfer||Citrate synthase - ATP citrate lyase - HMG-CoA synthase|
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