Transport of basic amino acids and regulation of aspartate kinase activity in thialysine and L-canavanine resistant strains of Serratia marcescens.
Growth of Serratia marcescens was not inhibited by high concentrations of L-lysine and its structural analogues, L-cancavanine and S-(2-aminoethyl)-L-cysteine (thialysine). This insensitivity was not caused by deficient transport of basic amino acids, unlike in mutant strains of Escherichia coli having the same properties. The tested strains showed a lack of regulation at the aspartate kinase level toward L-lysine and thialysine. The data indicate great intraspecific variability for aspartate kinase regulation in S. marcescens.
D000596:Amino Acids / Q000378:metabolism*; D001120:Arginine / Q000378:metabolism; D001222:Aspartate Kinase / Q000378:metabolism*; D001224:Aspartic Acid / Q000378:metabolism; D001692:Biological Transport; D002172:Canavanine / Q000494:pharmacology*; D003545:Cysteine / Q000031:analogs & derivatives* / Q000494:pharmacology; D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000187:drug effects; D008239:Lysine / Q000378:metabolism; D010770:Phosphotransferases / Q000378:metabolism*; D012706:Serratia marcescens / Q000378:metabolism*
D000596:Amino Acids; D001224:Aspartic Acid; D002172:Canavanine; D001120:Arginine; D010770:Phosphotransferases; D001222:Aspartate Kinase; D008239:Lysine; D003545:Cysteine