Koyama H
J Biochem. 1982 Oct;92(4):1235-40. doi: 10.1093/oxfordjournals.jbchem.a134041.
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.
通过丙烯酰胺凝胶电泳和超速离心判断，来自假单胞菌属P-501的L-苯丙氨酸氧化酶已被纯化至同质状态。该酶由L-苯丙氨酸产生β-苯丙酮酸和α-苯乙酰胺。平衡研究表明，在有氧条件下，消耗1摩尔的L-苯丙氨酸和氧气会分别生成0.2摩尔的β-苯丙酮酸、氨和过氧化氢，以及0.8摩尔的α-苯乙酰胺和二氧化碳。因此，同一酶制剂催化L-苯丙氨酸同时进行氧化脱氨和氧化脱羧反应。除L-苯丙氨酸外，该酶还以较低的反应速率氧化L-酪氨酸、L-甲硫氨酸和L-色氨酸。
