Biochemical-genetic study of the first enzyme of histidine biosynthesis in Salmonella typhimurium: substrate and feedback binding regions.
Twenty-five strains of Salmonella typhimurium containing different mutations in the first gene of histidine biosynthesis were studied to correlate regions of the genetic map with biochemical functions. These strains contained either missense, double-frameshift, or suppressed nonsense mutations, all of which resulted in altered, though active, enzymes. Each mutant enzyme was assayed for activity in the presence of varying concentrations of the feedback inhibitor L-histidine or the substrates ATP and 5-phosphoribosyl-1-pyrophosphate. The feedback properties and substrate kinetics of each mutant enzyme were compared to wild-type values, and these results indicated that the following functions were correlated with regions of the hisG gene: feedback inhibition in two general areas, including regions IA and IB and regions V, VI, and VII; ATP binding in two general areas, including regions IA, IB, and II and regions V, VI, and VII; and 5-phosphoribosyl-1-pyrophosphate binding in two general areas, including regions IB, II, and III and regions V and VI.
D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D002874:Chromosome Mapping; D005246:Feedback; D005796:Genes; D006639:Histidine / Q000096:biosynthesis*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009154:Mutation; D010754:Phosphoribosyl Pyrophosphate / Q000378:metabolism; D012486:Salmonella typhimurium / Q000201:enzymology* / Q000235:genetics
D006639:Histidine; D010754:Phosphoribosyl Pyrophosphate; D000255:Adenosine Triphosphate