Results 1 to 10 of about 3,749 (103)
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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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 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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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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Living with an imperfect cell wall: compensation of
BMC Genomics, 2007 Background Synthesis of the Staphylococcus aureus peptidoglycan pentaglycine interpeptide bridge is catalyzed by the nonribosomal peptidyl transferases FemX, FemA and FemB.
Bierbaum Gabriele +8 more
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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.
K K, Wan, N D, 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 T, Caskey +3 more
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Nuclear translation or nuclear peptidyl transferase? [PDF]
Nucleus, 2012 It is widely accepted that protein synthesis occurs in the cytoplasms of eukaryotic cells, but some investigators believe that it also occurs in the nucleus. In spite of experiments performed in several labs over many years, the issue of nuclear translation remains unresolved.
James, Dahlberg, Elsebet, Lund
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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
A, Panet, N, de Groot, Y, Lapidot
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Peptidyl‐Donor Substrates for Ribosomal Peptidyl Transferase [PDF]
European Journal of Biochemistry, 1972 A study of the structural requirements for activity of low molecular weight compounds in the donor or peptidyl site of ribosomal peptidyl transferase requires methods for the chemical synthesis of potential donor substrates. Methods are described here for the preparation of cytidylyl‐(3′→ 5′)‐cytidylyl‐(3′→ 5′)‐2′(3′)‐O‐(N‐[3H]acetyl‐l‐leucyl ...
J F, Mercer, R H, Symons
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