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Literature summary extracted from

  • Polacek, N.; Mankin, A.S.
    The ribosomal peptidyl transferase center: structure, function, evolution, inhibition (2005), Crit. Rev. Biochem. Mol. Biol., 40, 285-311.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.3.2.12 medicine antibiotic target Haloarcula marismortui
2.3.2.12 medicine antibiotic target Mycolicibacterium smegmatis
2.3.2.12 medicine antibiotic target Deinococcus radiodurans

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.12 A2451U the base identity at this highly conserved residue is not absolutely critical for peptide bond synthesis Mycolicibacterium smegmatis
2.3.2.12 A2451U with puromycin as an acceptor substrate, the catalytic rate of the mutant enzyme decreases about 150fold relative to wild type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.12 carbomycin
-
 Deinococcus radiodurans
2.3.2.12 carbomycin
-
 Haloarcula marismortui
2.3.2.12 carbomycin
-
 Mycolicibacterium smegmatis
2.3.2.12 chloramphenicol
-
 Deinococcus radiodurans
2.3.2.12 chloramphenicol
-
 Haloarcula marismortui
2.3.2.12 chloramphenicol
-
 Mycolicibacterium smegmatis
2.3.2.12 clindamycin
-
 Deinococcus radiodurans
2.3.2.12 clindamycin
-
 Haloarcula marismortui
2.3.2.12 clindamycin
-
 Mycolicibacterium smegmatis
2.3.2.12 sparsomycin
-
 Deinococcus radiodurans
2.3.2.12 sparsomycin
-
 Haloarcula marismortui
2.3.2.12 sparsomycin
-
 Mycolicibacterium smegmatis
2.3.2.12 streptogramin A
-
 Deinococcus radiodurans
2.3.2.12 streptogramin A
-
 Haloarcula marismortui
2.3.2.12 streptogramin A
-
 Mycolicibacterium smegmatis
2.3.2.12 tiamulin
-
 Deinococcus radiodurans
2.3.2.12 tiamulin
-
 Haloarcula marismortui
2.3.2.12 tiamulin
-
 Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.12 Deinococcus radiodurans
-
-
-
2.3.2.12 Escherichia coli
-
-
-
2.3.2.12 Haloarcula marismortui
-
-
-
2.3.2.12 Mycolicibacterium smegmatis
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.2.12 peptidyl-tRNA1 + aminoacyl-tRNA2 = tRNA1 + peptidyl(aminoacyl-tRNA2) The peptidyl transferase reaction involves aminolysis by the alpha-amino group of the A-site aminoacyl-tRNA of the ester bond that links the nascent peptide to the 3' hydroxyl of the 3' terminal ribose of the P-site tRNA. The termination reaction involves the transfer of the peptidyl moiety of P-site located peptidyl-tRNA to a water molecule, in the course of the reaction the nucleophilic attack of an activated water molecule in the peptidyl transferase center acceptor site onto the carbonyl carbon of the peptidyl-tRNA ester leads to formation of a tetrahedral intermediate, a proton from the water is subsequently transferred to the 2'(3')-hydroxyl of the 3'-terminal adenosine of peptidyl-tRNA, breaking the ester bond between the peptide and tRNA Mycolicibacterium smegmatis
a
2.3.2.12 peptidyl-tRNA1 + aminoacyl-tRNA2 = tRNA1 + peptidyl(aminoacyl-tRNA2) The peptidyl transferase reaction involves aminolysis by the alpha-amino group of the A-site aminoacyl-tRNA of the ester bond that links the nascent peptide to the 3'-hydroxyl of the 3'-terminal ribose of the P-site tRNA. The termination reaction involves the transfer of the peptidyl moiety of P-site located peptidyl-tRNA to a water molecule, in the course of the reaction the nucleophilic attack of an activated water molecule in the peptidyl transferase center acceptor site onto the carbonyl carbon of the peptidyl-tRNA ester leads to formation of a tetrahedral intermediate, a proton from the water is subsequently transferred to the 2'(3')-hydroxyl of the 3'-terminal adenosine of peptidyl-tRNA, breaking the ester bond between the peptide and tRNA Haloarcula marismortui
a
2.3.2.12 peptidyl-tRNA1 + aminoacyl-tRNA2 = tRNA1 + peptidyl(aminoacyl-tRNA2) The peptidyl transferase reaction involves aminolysis by the alpha-amino group of the A-site aminoacyl-tRNA of the ester bond that links the nascent peptide to the 3'-hydroxyl of the 3'-terminal ribose of the P-site tRNA. The termination reaction involves the transfer of the peptidyl moiety of P-site located peptidyl-tRNA to a water molecule, in the course of the reaction the nucleophilic attack of an activated water molecule in the peptidyl transferase center acceptor site onto the carbonyl carbon of the peptidyl-tRNA ester leads to formation of a tetrahedral intermediate, a proton from the water is subsequently transferred to the 2'(3')-hydroxyl of the 3'-terminal adenosine of peptidyl-tRNA, breaking the ester bond between the peptide and tRNA Escherichia coli
a
2.3.2.12 peptidyl-tRNA1 + aminoacyl-tRNA2 = tRNA1 + peptidyl(aminoacyl-tRNA2) The peptidyl transferase reaction involves aminolysis by the alpha-amino group of the A-site aminoacyl-tRNA of the ester bond that links the nascent peptide to the 3'-hydroxyl of the 3'-terminal ribose of the P-site tRNA. The termination reaction involves the transfer of the peptidyl moiety of P-site located peptidyl-tRNA to a water molecule, in the course of the reaction the nucleophilic attack of an activated water molecule in the peptidyl transferase center acceptor site onto the carbonyl carbon of the peptidyl-tRNA ester leads to formation of a tetrahedral intermediate, a proton from the water is subsequently transferred to the 2'(3')-hydroxyl of the 3'-terminal adenosine of peptidyl-tRNA, breaking the ester bond between the peptide and tRNA Deinococcus radiodurans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.12 AcPhe-tRNA + puromycin
-
 Haloarcula marismortui tRNA + AcPhe-puromycin
-
 ?
2.3.2.12 AcPhe-tRNA + puromycin
-
 Escherichia coli tRNA + AcPhe-puromycin
-
 ?
2.3.2.12 AcPhe-tRNA + puromycin
-
 Mycolicibacterium smegmatis tRNA + AcPhe-puromycin
-
 ?
2.3.2.12 AcPhe-tRNA + puromycin
-
 Deinococcus radiodurans tRNA + AcPhe-puromycin
-
 ?
2.3.2.12 peptidyl-tRNA1 + alpha-aminoacyl-tRNA2
-
 Haloarcula marismortui tRNA1 + peptidyl-amino-tRNA2
-
 ?
2.3.2.12 peptidyl-tRNA1 + alpha-aminoacyl-tRNA2
-
 Escherichia coli tRNA1 + peptidyl-amino-tRNA2
-
 ?
2.3.2.12 peptidyl-tRNA1 + alpha-aminoacyl-tRNA2
-
 Mycolicibacterium smegmatis tRNA1 + peptidyl-amino-tRNA2
-
 ?
2.3.2.12 peptidyl-tRNA1 + alpha-aminoacyl-tRNA2
-
 Deinococcus radiodurans tRNA1 + peptidyl-amino-tRNA2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.12 PT
-
 Haloarcula marismortui
2.3.2.12 PT
-
 Escherichia coli
2.3.2.12 PT
-
 Mycolicibacterium smegmatis
2.3.2.12 PT
-
 Deinococcus radiodurans
2.3.2.12 ribosomal peptidyl transferase
-
 Haloarcula marismortui
2.3.2.12 ribosomal peptidyl transferase
-
 Escherichia coli
2.3.2.12 ribosomal peptidyl transferase
-
 Mycolicibacterium smegmatis
2.3.2.12 ribosomal peptidyl transferase
-
 Deinococcus radiodurans