Absolute dependence of phenylalanine and tyrosine biosynthetic enzyme on tryptophan in Candida maltosa.
Candida maltosa synthesizes phenylalanine and tyrosine only via phenylpyruvate and p-hydroxyphenylpyruvate. Tryptophan is absolutely necessary for the enzymatic reaction of chorismate mutase and prephenate dehydrogenase; activity of prephenate dehydratase can be increased 2.5-fold in the presence of tryptophan. Activation of the chorismate mutase, prephenate dehydratase and prephenate dehydrogenase by tryptophan is competitive with respect to chorismate and prephenate with Ka 0.06mM, 0.56mM and 1.7mM. In addition tyrosine is a competitive inhibitor of chorismate mutase (Ki = 0.55mM) and prephenate dehydrogenase (Ki = 5.5mM).
D002175:Candida / Q000378:metabolism*; D002826:Chorismate Mutase / Q000378:metabolism; D002848:Chromatography, DEAE-Cellulose; D005656:Fungal Proteins / Q000378:metabolism; D006836:Hydro-Lyases / Q000378:metabolism; D007700:Kinetics; D010649:Phenylalanine / Q000096:biosynthesis*; D011303:Prephenate Dehydrogenase / Q000378:metabolism; D014364:Tryptophan / Q000378:metabolism*; D014443:Tyrosine / Q000096:biosynthesis*
D005656:Fungal Proteins; D014443:Tyrosine; D010649:Phenylalanine; D014364:Tryptophan; D011303:Prephenate Dehydrogenase; D006836:Hydro-Lyases; C022437:pretyrosine dehydratase; D002826:Chorismate Mutase