@article{mbs:/content/journal/micro/10.1099/00221287-117-1-81, author = "Blumenstock, Erich and Salcher, Olga and Lingens, Franz", title = "Regulation of Phenylalanine and Tyrosine Biosynthesis in Pseudomonas aureofaciens ATCC 15926", journal= "Microbiology", year = "1980", volume = "117", number = "1", pages = "81-87", doi = "https://doi.org/10.1099/00221287-117-1-81", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-117-1-81", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "Association patterns and regulatory properties of chorismate mutase, prephenate dehydratase and prephenate dehydrogenase from Pseudomonas aureofaciens ATCC 15926 were studied. Prephenate dehydrogenase (molecular weight 95000) was separated by Sephadex G-100 chromatography from both the chorismate mutase–prephenate dehydratase I complex (molecular weight 75000) and from a second, low molecular weight prephenate dehydratase (prephenate dehydratase II; molecular weight 30000). The chorismate mutase-prephenate dehydratase complex persisted after DEAE-Sephadex A-50 chromatography. With the exception of prephenate dehydratase II, enzyme activities were influenced by end-products. Chorismate mutase was competitively inhibited by l-phenylalanine (K i = 3·5 μ m). Prephenate dehydratase I was inhibited by l-phenylalanine (K i = 8 μ m) and activated by l-tyrosine (K a = 5 μ m). Prephenate dehydrogenase was feedback-inhibited by l-tyrosine. Substrate saturation curves of chorismate mutase and of prephenate dehydratase II were hyperbolic with K m values of 0·31 mm for chorismate and 0·015 mm for prephenate, respectively. The substrate saturation curve of the complexed prephenate dehydratase I was sigmoid; a K m value of 0·18 mm was calculated for prephenate. Chorismate mutase, prephenate dehydratase and prephenate dehydrogenase were not repressed by aromatic amino acids.", }