[Nourseothricin (streptothricin) inactivated by plasmid pIE 636-encoded acetyltransferase: detection of N-acetyl-beta-lysine in the inactivated product].
Nourseothricin (streptothricin) can be inactivated by an acetyl transferase synthesized by E. coli strains containing plasmid pIE 636. Nourseothricin inactivated in the presence of 14C-acetyl-coenzyme A was purified and submitted to partial acidic hydrolysis. By electrophoresis of the hydrolysate a 14C-containing substance moving only slowly towards the cathode could be isolated. This substance after complete hydrolysis yields only unlabelled beta-lysine.
D000123:Acetyltransferases / Q000235:genetics* / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology / Q000235:genetics*; D007536:Isomerism; D008239:Lysine / Q000032:analysis* / Q000031:analogs & derivatives; D011815:R Factors; D013309:Streptothricins / Q000378:metabolism / Q000494:pharmacology*
D000900:Anti-Bacterial Agents; C065591:beta-lysine; D013309:Streptothricins; D000123:Acetyltransferases; D008239:Lysine
Nourseothricin (Streptothricin), inaktiviert durch Plasmid pIE 636 codierte Acetyltransferase: Nachweis von N-Acetyl-beta-Lysin im Inaktivierungsprodukt.