KEGG   ENZYME: 2.3.2.12Help
Entry
EC 2.3.2.12                 Enzyme                                 

Name
peptidyltransferase;
transpeptidase;
ribosomal peptidyltransferase
Class
Transferases;
Acyltransferases;
Aminoacyltransferases
BRITE hierarchy
Sysname
peptidyl-tRNA:aminoacyl-tRNA N-peptidyltransferase
Reaction(IUBMB)
peptidyl-tRNA1 + aminoacyl-tRNA2 = tRNA1 + peptidyl(aminoacyl-tRNA2) [RN:R04685]
Reaction(KEGG)
Substrate
peptidyl-tRNA1;
aminoacyl-tRNA2
Product
tRNA1;
peptidyl(aminoacyl-tRNA2)
Comment
The enzyme is a ribozyme. Two non-equivlant ribonucleoprotein subunits operate in non-concerted fashion in peptide elongation. The small subunit forms the mRNA-binding machinery and decoding center, the large subunit performs the main ribosomal catalytic function in the peptidyl-transferase center.
History
EC 2.3.2.12 created 1976
Reference
1  [PMID:5329275]
  Authors
Rychlik I.
  Title
Release of lysine peptides by puromycin from polylysyl-transfer ribonucleic acid in the presence of ribosomes.
  Journal
Biochim Biophys Acta 114:425-7 (1966)
DOI:10.1016/0005-2787(66)90327-3
Reference
2  [PMID:4897787]
  Authors
Rychlik I, Cerna J, Chladek S, Zemlicka J, Haladova Z.
  Title
Substrate specificity of ribosomal peptidyl transferase: 2'(3')-O-aminoacyl nucleosides as acceptors of the peptide chain on the amino acid site.
  Journal
J Mol Biol 43:13-24 (1969)
DOI:10.1016/0022-2836(69)90075-8
Reference
3  [PMID:14222897]
  Authors
TRAUT RR, MONRO RE
  Title
THE PUROMYCIN REACTION AND ITS RELATION TO PROTEIN SYNTHESIS.
  Journal
J Mol Biol 10:63-72 (1964)
DOI:10.1016/S0022-2836(64)80028-0
Reference
4  [PMID:19363482]
  Authors
Voorhees RM, Weixlbaumer A, Loakes D, Kelley AC, Ramakrishnan V
  Title
Insights into substrate stabilization from snapshots of the peptidyl transferase  center of the intact 70S ribosome.
  Journal
Nat Struct Mol Biol 16:528-33 (2009)
DOI:10.1038/nsmb.1577
Other DBs
ExplorEnz - The Enzyme Database: 2.3.2.12
IUBMB Enzyme Nomenclature: 2.3.2.12
ExPASy - ENZYME nomenclature database: 2.3.2.12
BRENDA, the Enzyme Database: 2.3.2.12
CAS: 9059-29-4

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