Histidine dissimilation in Streptomyces coelicolor.
A growth technique that allows strains of Streptomyces coelicolor to grow dispersed in defined liquid medium has been devised and used to determine the pathway of histidine degradation by S. coelicolor. Enzymic, chromatographic and stoichiometric analyses indicated that histidine is dissimilated via N-formyl-L-glutamic acid. The enzymes for histidine utilization (hut) are induced when histidine or urocanate is included in the culture medium. Biochemical evidence suggested that urocanate, or a further metabolite, is the physiological inducer. Three hut mutants were isolated and characterized. Two of the mutants exhibit an uninducible phenotype, whereas the third mutant appears to be defective in the structural gene for formiminoglutamate iminohydrolase. Haploid recombinant analysis was employed to locate all three mutations in the left empty region of the chromosomal map.
D000581:Amidohydrolases / Q000096:biosynthesis; D001426:Bacterial Proteins; D002874:Chromosome Mapping; D003433:Crosses, Genetic; D003470:Culture Media; D004790:Enzyme Induction; D005565:Formiminoglutamic Acid / Q000378:metabolism; D006639:Histidine / Q000378:metabolism*; D006638:Histidine Ammonia-Lyase / Q000096:biosynthesis; D006867:Hydrolases / Q000096:biosynthesis / Q000378:metabolism; D009154:Mutation; D013302:Streptomyces / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D014559:Urocanate Hydratase / Q000096:biosynthesis; D014560:Urocanic Acid / Q000378:metabolism
D001426:Bacterial Proteins; D003470:Culture Media; D006639:Histidine; D005565:Formiminoglutamic Acid; D006867:Hydrolases; D000581:Amidohydrolases; C036370:formiminoglutamate deiminase; C020147:EE57C protein, Bacillus subtilis; D014559:Urocanate Hydratase; D006638:Histidine Ammonia-Lyase; D014560:Urocanic Acid