| Abstract: | Incubating chloridazon-degrading bacteria with L-phenylalanine leads to the accumulation of L-2,3-dihydroxyphenylalanine, o-tyrosine and m-tyrosine in the medium. Incubating the bacteria with N-acetyl-L-phenylalanine leads to N-acetyl-(2,3-dihydroxyphenyl)alanine. Using phenylacetic acid as substrate leads to the accumulation of malonic acid. The products are isolated by gel chromatography and high performance liquid chromatography. 2,3-Dihydroxy-L-phenylalanine is attacked by a catechol 2,3-dioxygenase in the presence of Fe2. An unstable yellow compound is formed in this reaction. This meta-cleavage-product is again cleaved by a hydrolase, leading to aspartic acid and 4-hydroxy-2-oxovaleric acid. Both products were isolated fromthe reaction buffer by amino acid analysis and high performance liquid chromatography. The dioxygenase and hydrolase were partially purified and characterized. A new degradation pathway for phenylalanine is discussed and compared with known pathways. The enzymes chorismate mutase, prephenate dehydratase and prephenate dehydrogenase are characterized and inhibition as well as repression are investigated. Only prephenate dehydrogenase is inhibited by phenylalanine, tyrosine and tryptophane. Chorismate mutase is repressed by phenylalanine, prephenate dehydrogenase by phenylalanine and tyrosine. Prephenate dehydratase is not repressed by aromatic amino acids. Regulation of aromatic amino acid biosynthesis in connection with phenylalanine degradation is discussed. |
