The Enzyme Database

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EC 2.3.2.12     
Accepted name: peptidyltransferase
Reaction: peptidyl-tRNA1 + aminoacyl-tRNA2 = tRNA1 + peptidyl(aminoacyl-tRNA2)
Other name(s): transpeptidase; ribosomal peptidyltransferase
Systematic name: peptidyl-tRNA:aminoacyl-tRNA N-peptidyltransferase
Comments: 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9059-29-4
References:
1.  Rychlik, I. Release of lysine peptides by puromycin from polylysyl-transfer ribonucleic acid in the presence of ribosomes. Biochim. Biophys. Acta 114 (1966) 425–427. [DOI] [PMID: 5329275]
2.  Rychlik, I., Cerná, J., Chládek, S., Zemlicka, J. and Haladová, Z. Substrate specificity of ribosomal peptidyl transferase: 2′(3′)-O-aminoacyl nucleosides as acceptors of the peptide chain on the amino acid site. J. Mol. Biol. 43 (1969) 13–24. [DOI] [PMID: 4897787]
3.  Traut, R.R. and Monro, R.E. The puromycin reaction and its relation to protein synthesis. J. Mol. Biol. 10 (1964) 63–72. [PMID: 14222897]
4.  Voorhees, R.M., Weixlbaumer, A., Loakes, D., Kelley, A.C. and Ramakrishnan, V. Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome. Nat. Struct. Mol. Biol. 16 (2009) 528–533. [DOI] [PMID: 19363482]
[EC 2.3.2.12 created 1976]
 
 


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