Enzymic basis for leakiness of auxotrophs for phenylalanine in Pseudomonas aeruginosa.
The dual enzymic routes for phenylalanine biosynthesis that exist in Pseudomonas aeruginosa complicate the isolation of phenylalanine auxotrophs. Mutants blocked in each of the various phenylalanine-pathway steps are essential for full appreciation of the physiological nature and gene-enzyme relationships of this biochemical system. A leaky phenylalanine-requiring mutant of P. aeruginosa (PAT1051) was found to lack the bifunctional P-protein (chorismate mutase-prephenate dehydratase), but retained the monofunctional isozyme species of chorismate mutase (chorismate mutase-F) as well as cyclohexadienyl dehydratase (components of the arogenate 'overflow' route to phenylalanine). This is the first mutant of P. aeruginosa shown to be deficient in any enzyme specific for phenylalanine synthesis. It is concluded that although the arogenate pathway has the demonstrated potential to overproduce phenylalanine, the substrate levels normally available to the arogenate pathway in the wild-type are inadequate to satisfy the full metabolic demand for phenylalanine.
D002826:Chorismate Mutase / Q000378:metabolism; D002848:Chromatography, DEAE-Cellulose; D006836:Hydro-Lyases / Q000378:metabolism; D009154:Mutation; D010649:Phenylalanine / Q000096:biosynthesis*; D011302:Prephenate Dehydratase / Q000378:metabolism; D011550:Pseudomonas aeruginosa / Q000201:enzymology*
D010649:Phenylalanine; D006836:Hydro-Lyases; C022437:pretyrosine dehydratase; D011302:Prephenate Dehydratase; D002826:Chorismate Mutase