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
-
exit
-
tunnel
-
p-site
- chloramphenicol
-
macrolide
-
decoding
-
aminoacylated
- erythromycin
-
stall
- trnaphe
-
haloarcula
-
peptide-bond
-
protuberance
-
oxazolidinones
-
lincosamide
-
transpeptidation
-
penicillin-binding
- polyu
-
cryo-electron
-
ribozyme
-
streptogramins
- carbapenems
-
anticodon
- linezolid
-
ribosome-bound
- marismortui
-
pleuromutilins
- clarithromycin
-
polyphenylalanine
-
polyu-directed
-
ketolide
-
virginiamycin
- lincomycin
-
fmet-trna
-
polyphe
-
blasticidin
-
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
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results (Engineering
Engineering on EC 2.3.2.12 - peptidyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A2451U
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with puromycin as an acceptor substrate, the catalytic rate of the mutant enzyme decreases about 150fold relative to wild type enzyme
A2451U
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the base identity at this highly conserved residue is not absolutely critical for peptide bond synthesis
additional information
additional information
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changes of 23S rRNA nucleotides in the 2585 region of the peptidyl transferase center, G2583A and U2584C, reduce maximum induction of tna operon expression by tryptophan in vivo without affecting the concentration of tryptophan necessary to obtain 50% induction. The growth rate of strains with ribosomes with either of these changes is not altered appreciably. In vitro analyses show that tryptophan is not as efficient in protecting TnaC-tRNAPro from puromycin action as wild-type ribosomes. However, added tryptophan does prevent sparsomycin action as it normally does with wild-type ribosomes. These two mutational changes act by reducing the ability of ribosome-bound tryptophan to inhibit peptidyl transferase activity rather than by reducing the ability of the ribosome to bind tryptophan
additional information
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lack of pseudouridine at position 2504 of 23S rRNA significantly increases the susceptibility of Escherichia coli to peptidyl transferase inhibitors
additional information
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the lethal mutation UU2492-3C affects the function of ribosomal peptidyl transferase center. Binding of Phe-tRNAPhe to the A site of ribosomes with mutation UU2492-3C is much lower comparing to wild type ribosomes (27% and 77%, respectively). Mutant ribosomes are not able to catalyze peptidyl transfer reaction with puromycin as the A-site substrate
additional information
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the antibiotic resistance mutation G2482A enhances conformational fluctuation at the antibiotic binding site, weakens the hydrogen-bonding network, and increases flexibility at the 50S peptidyl transferase center
additional information
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introduction of individual 23S rRNA mutations associated with pleuromutilin resistance at positions 2055, 2447, 2504 and 2572, Escherichia coli numbering, into a Mycobacterium smegmatis strain with a single rRNA operon. The single mutations each confer a significant and similar degree of valnemulin resistance and those at 2447 and 2504 also confer cross-resistance to other antibiotics that bind to the peptidyl transfer center. The introduced mutations cause structural perturbations at the peptidyl transfer center and reduce binding of pleuromutilin antibiotics
additional information
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single mutations at positions 2032, 2453, and 2499 to human cytosolic base identity do not confer significantly reduced susceptibility to linezolid. The largest decrease in linezolid susceptibility is observed with the G2576U mutation
additional information
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mutant DELTAldtC is hypersusceptible to imipenem
additional information
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
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mutant DELTAldtC is hypersusceptible to imipenem
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additional information
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single mutations at positions 2032, 2453, and 2499 to human cytosolic base identity do not confer significantly reduced susceptibility to linezolid. The largest decrease in linezolid susceptibility is observed with the G2576U mutation
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additional information
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three bases in the catalytic core of the peptidyltransferase center - A2819-20 (A2450 and A2451) and U2875 (U2506) - are hyperprotected from 1M7 reagent but not dimethylsulfate modification in U2861A ribosomes
additional information
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mutations at base A2451 lead to strongly decreased enzyme activity
