The Photochemical Inactivation of Peptidyl Transferase Activity [PDF]
European Journal of Biochemistry, 1975 The photochemical oxidation of the 50‐S ribosomal subunit results in a rapid irreversible loss of peptidyl transferase activity. The first‐order rate of inactivation occurring during the first forty minutes suggests that a single reactive group is being inactivated.
Kwong K. WAN, Nasir Zahid, R.M. Baxter
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Hydrolysis of fMet-tRNA by Peptidyl Transferase [PDF]
Proceedings of the National Academy of Sciences, 1971 Escherichia coli and rabbit reticulocyte (f[ 3 H]Met-tRNA·AUG·ribosome) intermediates undergo hydrolysis, with release of f[ 3 H]methionine, upon addition of tRNA or CpCpA in the presence of acetone.
C. Thomas Caskey +3 more
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The Bacillus subtilis ywbD gene encodes RlmQ, the 23S rRNA methyltransferase forming m7G2574 in the A-site of the peptidyl transferase center. [PDF]
RNA, 2023 Wolff P +8 more
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Substrate Specificity of Escherichia coli Peptidyl‐Transferase [PDF]
European Journal of Biochemistry, 1970 The kinetics of the puromycin interaction with different ribosomal bound peptidyl‐tRNAs were studied. The rates of the puromycin reaction with AA‐Phe‐tRNA and AA2‐Phe‐tRNA using three different amino acids (AA) were compared. At 4° all the three dipeptidyl‐tRNAsPhe reacted considerably slower than the three tripeptidyl‐tRNAsPhe. Acetyl‐Phe‐tRNA reacted
Amos Panet, Nathan de Groot, Y. Lapidot
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Recognition of Hybrid Peptidyl Carrier Proteins/Acyl Carrier Proteins in Nonribosomal Peptide Synthetase Modules by the 4′-Phophopantetheinyl Transferases AcpS and Sfp [PDF]
Journal of Biological Chemistry, 2002 Mohammad Reza Mofid +2 more
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Microbiology Spectrum, 2022 Phosphopantetheinyl transferases (PPTases) play important roles in activating apo-acyl carrier proteins (apo-ACPs) and apo-peptidyl carrier proteins (apo-PCPs) in both primary and secondary metabolism. PPTases catalyze the posttranslational modifications
Songya Zhang +7 more
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The Ribosomal Peptidyl Transferase [PDF]
Molecular Cell, 2007 Peptide bond formation on the ribosome takes place in an active site composed of RNA. Recent progress of structural, biochemical, and computational approaches has provided a fairly detailed picture of the catalytic mechanism of the reaction. The ribosome accelerates peptide bond formation by lowering the activation entropy of the reaction due to ...
Beringer, M., Rodnina, M.
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A single Sfp-type phosphopantetheinyl transferase plays a major role in the biosynthesis of PKS and NRPS derived metabolites in Streptomyces ambofaciens ATCC23877. [PDF]
PLoS ONE, 2014 The phosphopantetheinyl transferases (PPTases) are responsible for the activation of the carrier protein domains of the polyketide synthases (PKS), non ribosomal peptide synthases (NRPS) and fatty acid synthases (FAS).
Robert Bunet +9 more
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The insect pathogen Serratia marcescens Db10 uses a hybrid non-ribosomal peptide synthetase-polyketide synthase to produce the antibiotic althiomycin [PDF]
, 2012 There is a continuing need to discover new bioactive natural products, such as antibiotics, in genetically-amenable micro-organisms. We observed that the enteric insect pathogen, Serratia marcescens Db10, produced a diffusible compound that inhibited the
Amy J. Gerc +5 more
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Peptidyl transferase: ancient and exiguous [PDF]
Chemistry & Biology, 2000 The finding that the universal ribosomal peptidyl transferase is an RNA enzyme casts new light on its ancient origins, on the use of transition state analogues for ribozymes, and on the role of selection-amplification in studies of molecular evolution.
Yarus, Michael, Welch, Mark
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