title: Purification of arogenate dehydrogenase from Phenylobacterium immobile.
abstract: Phenylobacterium immobile, a bacterium which is able to degrade the herbicide chloridazon, utilizes for L-tyrosine synthesis arogenate as an obligatory intermediate which is converted in the final biosynthetic step by a dehydrogenase to tyrosine. This enzyme, the arogenate dehydrogenase, has been purified for the first time in a 5-step procedure to homogeneity as confirmed by electrophoresis. The Mr of the enzyme that consists of two identical subunits amounts to 69000 as established by gel electrophoresis after cross-linking the enzyme with dimethylsuberimidate. The Km values were 0.09 mM for arogenate and 0.02 mM for NAD+. The enzyme has a high specificity with respect to its substrate arogenate.
mesh_terms: D004591:Electrophoresis, Polyacrylamide Gel; D006090:Gram-Negative Bacteria / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D046911:Macromolecular Substances; D008970:Molecular Weight; D010088:Oxidoreductases / Q000302:isolation & purification*; D011303:Prephenate Dehydrogenase; D013379:Substrate Specificity
chemical_list: D046911:Macromolecular Substances; D010088:Oxidoreductases; D011303:Prephenate Dehydrogenase; C027017:cyclohexadienyl dehydrogenase