2.3.2.12: peptidyltransferase
This is an abbreviated version!
For detailed information about peptidyltransferase, go to the full flat file.
Word Map on EC 2.3.2.12
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2.3.2.12
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rrnas
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puromycin
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aminoacyl-trnas
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exit
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tunnel
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p-site
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chloramphenicol
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macrolide
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decoding
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aminoacylated
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erythromycin
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stall
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trnaphe
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haloarcula
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peptide-bond
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protuberance
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oxazolidinones
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lincosamide
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transpeptidation
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penicillin-binding
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polyu
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cryo-electron
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ribozyme
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streptogramins
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carbapenems
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anticodon
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linezolid
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ribosome-bound
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marismortui
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pleuromutilins
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clarithromycin
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polyphenylalanine
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polyu-directed
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ketolide
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virginiamycin
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lincomycin
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fmet-trna
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polyphe
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blasticidin
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aa-trnas
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tylosin
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phe-trna
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clindamycin
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pseudouridine
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medicine
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spiramycin
- 2.3.2.12
- rrnas
- puromycin
- aminoacyl-trnas
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exit
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tunnel
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p-site
- chloramphenicol
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macrolide
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decoding
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aminoacylated
- erythromycin
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stall
- trnaphe
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haloarcula
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peptide-bond
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protuberance
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oxazolidinones
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lincosamide
-
transpeptidation
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penicillin-binding
- polyu
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cryo-electron
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ribozyme
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streptogramins
- carbapenems
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anticodon
- linezolid
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ribosome-bound
- marismortui
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pleuromutilins
- clarithromycin
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polyphenylalanine
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polyu-directed
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ketolide
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virginiamycin
- lincomycin
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fmet-trna
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polyphe
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blasticidin
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aa-trnas
- tylosin
- phe-trna
- clindamycin
- pseudouridine
- medicine
- spiramycin
Reaction
Synonyms
ArfB, L,D-transpeptidase, L,D-transpeptidase 2, LD-transpeptidase, LDT, LdtD, Ldtfm, LdtMt2, LdtMt5, MSMEI_5283, peptidoglycan transpeptidase, peptidyl transferase, peptidyl transferase center, peptidyltransferase centre, PT, PTase, PTC, PTH, ribosomal peptidyl transferase, ribosomal peptidyltransferase, ribosomal protein L27, transpeptidase
ECTree
2.3.2.12 peptidyltransferaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 2.3.2.12 - peptidyltransferase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
40S subunits of ribosomes
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inhibition proportional to the 40S-subunit-concentration
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ampicillin
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strain 18sH Con-, 60 microg/ml, 50 percent inhibition; strain 18s SAI-, 3 microg/ml, 50 percent inhibition
arginine attenuator peptide
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the wild type arginine attenuator peptide (AAP) inhibits peptidyl transferase center (PTC) function. AAP containing the D12N mutation, which eliminates Arg-induced ribosome stalling, also eliminates Arg's effect on PTC function
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Bamicetin
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complete inhibition with AcPhe-tRNA as donor, with polylysyl-tRNA as donor less active
benzyl penicillin
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strain 18sH Con-, 450 microg/ml, 50 percent inhibition; strain 18s SAI-, 0.3 microg/ml, 50 percent inhibition
carbenicillin
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strain 18sH Con-, 50 microg/ml, 50 percent inhibition; strain 18s SAI-, 0.2 microg/ml, 50 percent inhibition
cephaloridine
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strain 18sH Con-, 200 microg/ml, 50 percent inhibition; strain 18s SAI-, 0.1 microg/ml, 50 percent inhibition
cytidylyl-3'-5'-/2'(3')-O-L-phenylalanyl/L-adenosine
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50% inhibition of peptidyltransferase, inhibition can be reversed by increasing concentration of puromycin
Gly-chloramphenicol
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competitive inhibition with acetylphenylalanyl-tRNA-polyU-ribosome complex, newly formed complex is inactive towards puromycin
Gly-Phe-chloramphenicol
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competitive inhibition with acetylphenylalanyl-tRNA-polyU-ribosome complex, newly formed complex is inactive towards puromycin
L-Phe-chloramphenicol
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competitive inhibition with acetylphenylalanyl-tRNA-polyU-ribosome complex, newly formed complex is inactive towards puromycin
L-Phe-Gly-chloramphenicol
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competitive inhibition with acetylphenylalanyl-tRNA-polyU-ribosome complex, newly formed complex is inactive towards puromycin
N1,N12-Diacetylspermine
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both stimulatory and inhibitory effects at the kinetic phase in the presence of the factors washable from ribosomes, depending on ligand concentration
N1,N12-dipivaloylspermine
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both stimulatory and inhibitory effects at the kinetic phase in the presence of the factors washable from ribosomes, depending on ligand concentration
N1-acetylspermine
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both stimulatory and inhibitory effects at the kinetic phase in the presence of the factors washable from ribosomes, depending on ligand concentration
1-ethyl-4-[(2-phenylthiazol-4-yl)methyl]piperazine
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i.e. ZINC19595411
1-ethyl-4-[(2-phenylthiazol-4-yl)methyl]piperazine
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i.e. ZINC19595411
1-[(2-methylthiazol-4-yl)methyl]-4-[(2-phenylthiazol-4-yl)methyl]piperazine
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i.e. ZINC22812775
1-[(2-methylthiazol-4-yl)methyl]-4-[(2-phenylthiazol-4-yl)methyl]piperazine
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i.e. ZINC22812775
1-[(2-methylthiazol-4-yl)methyl]-4-[(2-phenylthiazol-4-yl)methyl]piperazine
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i.e. ZINC22812775
Amicetin
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complete inhibition with AcPhe-tRNA as donor, with polylysyl-tRNA as donor less active
anisomycin
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inhibition of formation of AcPhe-puromycin catalyzed by rabbit reticulocyte ribosomes
blasticidin S
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inhibition of formation of Ac-Phe-puromycin catalyzed by rabbit reticulocyte ribosomes
chloramphenicol
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competitive inhibition with acetylphenylalanyl-tRNA-polyU-ribosome complex, newly formed complex is inactive towards puromycin
chloramphenicol
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CHL, inhibits protein synthesis by targeting the peptidyl transferase center of the bacterial ribosome. Analysis of the binding site of CHL in the peptidyl transferase center of the 50S ribosomal subunit, overview. The identity of the penultimate residue of the nascent peptide is critical for the inhibitory activity, specificity and mechanism
chloramphenicol
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weak peptide bond formation inhibition only by ribosomes with A2451C, A2451U or A2451G, peptide bond formation inhibition by ribosomes with G2447A is essentially unimpaired
linezolid
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binds in the A site pocket at the peptidyltransferase center of the ribosome overlapping the aminoacyl moiety of an A-site bound tRNA as well as many clinically important antibiotics. Binding of linezolid stabilizes a distinct conformation of the universally conserved 23S rRNA nucleotide U2585 that would be nonproductive for peptide bond formation. In a model oxazolidinones impart their inhibitory effect by perturbing the correct positioning of tRNAs on the ribosome
linezolid
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LZD, inhibits protein synthesis by targeting the peptidyl transferase center of the bacterial ribosome. Analysis of the binding site of LZD in the peptidyl transferase center of the 50S ribosomal subunit, overview. The identity of the penultimate residue of the nascent peptide is critical for the inhibitory activity, specificity and mechanism
madumycin II
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i.e. MADU, an alanine-containing streptogramin A antibiotic, inhibits peptide bond formation by forcing the peptidyl transferase center into an inactive state. It allows binding of the tRNAs to the ribosomal A and P sites, but prevents correct positioning of their CCA-ends into the PTC thus making peptide bond formation impossible. Drug-induced rearrangement of nucleotides U2506 and U2585 of the 23S rRNA resulting in the formation of the U2506-G2583 wobble pair that is attributed to a catalytically inactive state of the PTC. At 0.005 mM concentration, MADU reduces the efficiency of protein synthesis by over 100fold
madumycin II
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i.e. MADU, an alanine-containing streptogramin A antibiotic, inhibits peptide bond formation by forcing the peptidyl transferase center into an inactive state. It allows binding of the tRNAs to the ribosomal A and P sites, but prevents correct positioning of their CCA-ends into the PTC thus making peptide bond formation impossible. Drug-induced rearrangement of nucleotides U2506 and U2585 of the 23S rRNA resulting in the formation of the U2506-G2583 wobble pair that is attributed to a catalytically inactive state of the PTC. Structures of inhibitor madumycin II in complex with the 70S ribosome and A- and P-tRNAs, overview
sparsomycin
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binds to 50S bacterial ribosomal subunit. Calculated binding free energy is about -6 kcal/mol. In the simulation protocol, restraining potentials are activated for the orientational and translational movements of the ligand relative to the binding site when it is decoupled from the binding pocket, and then released once the ligand fully interacts with the rest of the system. The number of water molecules in the binding pocket is allowed to fluctuate dynamically in response to the ligand during the calculations
sparsomycin
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inhibition of formation of AcPhe-puromycin catalyzed by rabbit reticulocyte ribosomes
spermine
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competitive inhibitor of peptide bond formation at the kinetic phase of the puromycin reaction
valnemulin
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single mutations at positions 2055, 2447, 2504 and 2572, Escherichia coli numbering, of 23S rRNA each confer a significant and similar degree of valnemulin resistance
additional information
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streptogramins A is a class of protein synthesis inhibitors that target the peptidyl transferase center (PTC) on the large subunit of the ribosome
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additional information
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reevaluation of the mechanism of inducible CHL resistance. CHL and LZD poorly inhibit peptide bond formation when glycine residues are involved. Induction of CHL resistance genes relies on the stimulatory effect of the penultimate residue of the nascent chain on drug action
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additional information
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improved small molecule inhibitors of the Mtb ribosomal PTC are obtained using a combination of NMR transverse relaxation times (T2) and computational chemistry approaches, inhibitor design from scaffolds, docking study, overview. Two phenylthiazole derivatives with low IC50 values are predicted by machine learning models as effective inhibitors. Screening of the ZINC database. Predicted binding of oxazolidinone antibiotics that target the ribosomal PTC
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additional information
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improved small molecule inhibitors of the Mtb ribosomal PTC are obtained using a combination of NMR transverse relaxation times (T2) and computational chemistry approaches, inhibitor design from scaffolds, overview. Two phenylthiazole derivatives with low IC50 values are predicted by machine learning models as effective inhibitors. Screening of the ZINC database. Predicted binding of oxazolidinone antibiotics that target the ribosomal PTC
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additional information
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the peptidyl transferase center is not inhibited by D-arginine
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additional information
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improved small molecule inhibitors of the Mtb ribosomal PTC are obtained using a combination of NMR transverse relaxation times (T2) and computational chemistry approaches, inhibitor design from scaffolds, docking study, overview. Two phenylthiazole derivatives with low IC50 values are predicted by machine learning models as effective inhibitors. Screening of the ZINC database. Molecular docking of Mycobacterium tuberculosis-homologous Staphylococcus aureus peptidyl transferase center (PTC). Predicted binding of oxazolidinone antibiotics that target the ribosomal PTC
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additional information
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streptogramins A is a class of protein synthesis inhibitors that target the peptidyl transferase center (PTC) on the large subunit of the ribosome. In ribosome complex with mRNA and tRNAs, the binding site of madumycin II is very similar to the binding sites of virginiamycin M, dalfopristin, or flopristin (all proline-containing type A streptogramin antibiotics)
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