The Modification of the Peptidyltransferase Activity of 50‐S Ribosomal Subunits, LiCl‐Split Proteins and L16 Ribosomal Protein by Pyridoxal Phosphate
Open Access
- 1 September 1980
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 110 (1), 161-166
- https://doi.org/10.1111/j.1432-1033.1980.tb04851.x
Abstract
Pyridoxal phosphate photoinactivates the peptidyltransferase activity of [Escherichia coli] 50-S ribosomal subunits, LiCl split proteins and protein L16. Ethyromycin exhibits significant protection. These results, taken together with earlier reports, indicate the involvement of the single histidine of L16 in peptidyltransferase activity. The adjacent association in L16 of histidine and lysine indicates that pyridoxal phosphate should represent a selective inhibitor of peptidyltransferase activity.This publication has 17 references indexed in Scilit:
- The Modification of the Peptidyl Transferase Activity of 50-S Ribosomal Subunits, LiCl-Split Proteins and L16 Ribosomal Protein by Ethoxyformic AnhydrideEuropean Journal of Biochemistry, 1978
- Reaction of pyridoxal 5′-phosphate with Escherichia coli CoA transferase: Evidence for an essential lysine residueArchives of Biochemistry and Biophysics, 1977
- The primary structure of protein L16 located at the peptidyltransferase center of Escherichia coli ribosomesFEBS Letters, 1976
- The Photochemical Inactivation of Peptidyl Transferase ActivityEuropean Journal of Biochemistry, 1975
- Inactivation and reactivation of ribosomal subunits: The peptidyl transferase activity of the 50 s subunit of Escherichia coliJournal of Molecular Biology, 1970
- Interconversions between inactive and active forms of ribosomal subunitsFEBS Letters, 1969
- The inactivation and reactivation of ribosomal-peptidyl transferase of E. coliBiochemical and Biophysical Research Communications, 1968
- Cupric ion catalysis in hydrolysis of aminoacyl-tRNABiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1968
- Catalysis of peptide bond formation by 50 s ribosomal subunits from Escherichia coliJournal of Molecular Biology, 1967
- The behaviour of acetylphenylalanyl soluble ribonucleic acid in polyphenylalanine synthesisBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1966