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Literature summary for 2.3.2.12 extracted from
- The ribosomal peptidyl transferase center: structure, function, evolution, inhibition (2005), Crit. Rev. Biochem. Mol. Biol., 40, 285-311.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | antibiotic target | Haloarcula marismortui |
| medicine | antibiotic target | Mycolicibacterium smegmatis |
| medicine | antibiotic target | Deinococcus radiodurans |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A2451U | the base identity at this highly conserved residue is not absolutely critical for peptide bond synthesis | Mycolicibacterium smegmatis |
| 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
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| carbomycin | - |
Deinococcus radiodurans |  |
| carbomycin | - |
Haloarcula marismortui | |
| carbomycin | - |
Mycolicibacterium smegmatis | |
| chloramphenicol | - |
Deinococcus radiodurans | |
| chloramphenicol | - |
Haloarcula marismortui | |
| chloramphenicol | - |
Mycolicibacterium smegmatis | |
| clindamycin | - |
Deinococcus radiodurans | |
| clindamycin | - |
Haloarcula marismortui | |
| clindamycin | - |
Mycolicibacterium smegmatis | |
| sparsomycin | - |
Deinococcus radiodurans | |
| sparsomycin | - |
Haloarcula marismortui | |
| sparsomycin | - |
Mycolicibacterium smegmatis | |
| streptogramin A | - |
Deinococcus radiodurans | |
| streptogramin A | - |
Haloarcula marismortui | |
| streptogramin A | - |
Mycolicibacterium smegmatis | |
| tiamulin | - |
Deinococcus radiodurans | |
| tiamulin | - |
Haloarcula marismortui | |
| tiamulin | - |
Mycolicibacterium smegmatis | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Deinococcus radiodurans | - |
- |
- |
| Escherichia coli | - |
- |
- |
| Haloarcula marismortui | - |
- |
- |
| Mycolicibacterium smegmatis | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 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 | |
| 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 | |
| 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 | |
| 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 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| AcPhe-tRNA + puromycin | - |
Haloarcula marismortui | tRNA + AcPhe-puromycin | - |
? | |
| AcPhe-tRNA + puromycin | - |
Escherichia coli | tRNA + AcPhe-puromycin | - |
? | |
| AcPhe-tRNA + puromycin | - |
Mycolicibacterium smegmatis | tRNA + AcPhe-puromycin | - |
? | |
| AcPhe-tRNA + puromycin | - |
Deinococcus radiodurans | tRNA + AcPhe-puromycin | - |
? | |
| peptidyl-tRNA1 + alpha-aminoacyl-tRNA2 | - |
Haloarcula marismortui | tRNA1 + peptidyl-amino-tRNA2 | - |
? | |
| peptidyl-tRNA1 + alpha-aminoacyl-tRNA2 | - |
Escherichia coli | tRNA1 + peptidyl-amino-tRNA2 | - |
? | |
| peptidyl-tRNA1 + alpha-aminoacyl-tRNA2 | - |
Mycolicibacterium smegmatis | tRNA1 + peptidyl-amino-tRNA2 | - |
? | |
| peptidyl-tRNA1 + alpha-aminoacyl-tRNA2 | - |
Deinococcus radiodurans | tRNA1 + peptidyl-amino-tRNA2 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PT | - |
Haloarcula marismortui |
| PT | - |
Escherichia coli |
| PT | - |
Mycolicibacterium smegmatis |
| PT | - |
Deinococcus radiodurans |
| ribosomal peptidyl transferase | - |
Haloarcula marismortui |
| ribosomal peptidyl transferase | - |
Escherichia coli |
| ribosomal peptidyl transferase | - |
Mycolicibacterium smegmatis |
| ribosomal peptidyl transferase | - |
Deinococcus radiodurans |
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Release 2023.1 (January 2023)
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