The modification of the peptidyltransferase activity of 50-S ribosomal subunits, LiCl-split proteins and L16 ribosomal protein by pyridoxal phosphate.
Pyridoxal phosphate photoinactivates the peptidyltransferase activity of 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.
D000217:Acyltransferases / Q000037:antagonists & inhibitors*; D002712:Chlorides; D004305:Dose-Response Relationship, Drug; D004926:Escherichia coli / Q000201:enzymology; D006639:Histidine / Q000378:metabolism; D007700:Kinetics; D008027:Light; D008094:Lithium; D018021:Lithium Chloride; D010458:Peptidyl Transferases / Q000037:antagonists & inhibitors* / Q000528:radiation effects; D011732:Pyridoxal Phosphate / Q000494:pharmacology*; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000201:enzymology*
D002712:Chlorides; D012269:Ribosomal Proteins; C027937:ribosomal protein L16; D006639:Histidine; D011732:Pyridoxal Phosphate; D008094:Lithium; D000217:Acyltransferases; D010458:Peptidyl Transferases; D018021:Lithium Chloride