Purification and characterization of a novel L-phenylalanine oxidase (Deaminating and decarboxylating) from Pseudomonas sp. P-501.
L-Phenylalanine oxidase from Pseudomonas sp. P-501 has been purified to homogeneity as judged by acrylamide gel electrophoresis and ultracentrifugation. The enzyme produced both beta-phenylpyruvate and alpha-phenylacetamide from L-phenylalanine. Balance studies demonstrated that consumption of 1 mol each of L-phenylalanine and oxygen resulted in the formation of 0.2 mol each of beta-phenylpyruvate, ammonia, and hydrogen peroxide and 0.8 mol each of alpha-phenylacetamide and carbon dioxide under aerobic conditions. Thus, the same enzyme preparation catalyzed simultaneous oxidative deamination and oxygenative decarboxylation of L-phenylalanine. Besides L-phenylalanine, the enzyme oxidized L-tyrosine, L-methionine, and L-tryptophan at lower reaction rates.
D000594:Amino Acid Oxidoreductases / Q000302:isolation & purification*; D001426:Bacterial Proteins / Q000302:isolation & purification*; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity; D014461:Ultracentrifugation
D001426:Bacterial Proteins; D000594:Amino Acid Oxidoreductases; C022342:phenylalanine oxidase