Phenylalanine ammonia-lyase. Induction and purification from yeast and clearance in mammals.
Yeast phenylalanine ammonia-lyase (EC 4.3.1.5) catalyzes the deamination of L-phenylalanine to form trans-cinnamic acid and tyrosine to trans-coumaric acid. Maximal enzyme activity in Rhodotorula glutinis (2 units/g, wet weight, of yeast) was induced in late-log phase (12 to 14 hours) of growth in a culture medium containing 1.0% malt extract, 0.1% yeast extract, and 0.1% L-phenylalanine. A highly purified enzyme was obtained by fractionation with ammonium sulfate and sodium citrate followed by chromatography on DEAE-cellulose and Sephadex G-200. The active preparation yielded a major component on three different polyacrylamide gel electrophoretic systems. Antisera to phenylalanine ammonia-lyase was raised in rabbits and detected by double immunodiffusion. The antigen-antibody complex was enzymatically active in vitro. The biological half-life of the enzyme was approximately 21 hours in several mammalian species (mice without and with BW10232 adenocarcinoma and B16 melanoma, rats, and monkeys) after a single injection; however, upon repeated administration, phenylalanine ammonia-lyase had a much shorter biological half-life. The onset of rapid clearance occurred earlier in tumor-bearing than in nontumor-bearing mice indicating a direct or indirect influence by the tumor on the biological half-life of phenylalanine ammonia-lyase.
D000642:Ammonia-Lyases / Q000378:metabolism*; D000818:Animals; D002460:Cell Line; D004790:Enzyme Induction; D005260:Female; D006207:Half-Life; D008297:Male; D051379:Mice; D003904:Mitosporic Fungi / Q000201:enzymology*; D010650:Phenylalanine Ammonia-Lyase / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D012248:Rhodotorula / Q000201:enzymology*; D013045:Species Specificity; D013997:Time Factors
D000642:Ammonia-Lyases; D010650:Phenylalanine Ammonia-Lyase