Biochemical characterization of lysine auxotrophs of Staphylococcus aureus.
Lysine biosynthesis in Staphylococcus aureus has been studied by use of a series of lysine auxotrophs. The strains were isolated after chemical mutagenesis. The majority of these mutant strains were classified according to the enzymatic step found to be deficient. Specific enzyme assays as well as nutritional tests were used to group the organisms. The enzymes included were dihydrodipicolinate synthetase, dihydrodipicolinate reductase, diaminopimelate epimerase, and diaminopimelate decarboxylase. The accumulation of diaminopimelate in certain mutants and the demonstration of dihydrodipicolinate synthetase and reductase provide the first detailed evidence that S. aureus utilizes the diaminopimelate pathway for lysine biosynthesis. A cell-free system was used to study the regulation of these enzymes with the exception of diaminopimelate epimerase. Lysine repressed all of the enzymes tested. The repression appeared to be coordinate in nature. The data presented provide suggestive evidence that the lysine biosynthetic region in S. aureus constitutes an operon.
D002262:Carboxy-Lyases; D004794:Enzyme Repression; D007535:Isomerases; D008239:Lysine / Q000096:biosynthesis* / Q000494:pharmacology; D009154:Mutation; D010088:Oxidoreductases; D010848:Picolinic Acids / Q000378:metabolism; D013210:Staphylococcus / Q000201:enzymology
D010848:Picolinic Acids; D010088:Oxidoreductases; D002262:Carboxy-Lyases; D007535:Isomerases; D008239:Lysine