Multivalent repression of aspartic semialdehyde dehydrogenase in Escherichia coli K-12.
Mutants of Escherichia coli in which the lysine-sensitive aspartokinase is feedback-resistant are described. In these strains, as well as in the wild type, aspartic semialdehyde dehydrogenase is subject to multivalent repression by lysine, threonine, and methionine. When these amino acids were added to a culture in minimal medium, the differential rate of synthesis of the enzyme dropped to zero and remained there for about one generation.
D001223:Aspartate-Semialdehyde Dehydrogenase / Q000037:antagonists & inhibitors / Q000096:biosynthesis*; D001224:Aspartic Acid; D002474:Cell-Free System; D004794:Enzyme Repression / Q000187:drug effects*; D004926:Escherichia coli / Q000201:enzymology* / Q000254:growth & development; D005246:Feedback; D007700:Kinetics; D008239:Lysine / Q000494:pharmacology*; D008715:Methionine / Q000494:pharmacology*; D009153:Mutagens; D009154:Mutation; D009604:Nitrosoguanidines; D010770:Phosphotransferases / Q000037:antagonists & inhibitors / Q000096:biosynthesis; D014176:Protein Biosynthesis; D013237:Stereoisomerism; D013912:Threonine / Q000494:pharmacology*; D014161:Transduction, Genetic
D009153:Mutagens; D009604:Nitrosoguanidines; D013912:Threonine; D001224:Aspartic Acid; D008715:Methionine; D001223:Aspartate-Semialdehyde Dehydrogenase; D010770:Phosphotransferases; D008239:Lysine