Schneider S, Fuchs G
Mikrobiologie, Institut Biologie II, Universität Freiburg, Schänzlestrasse 1, D-79104 Freiburg, Germany.
Arch Microbiol. 1998 Jun;169(6):509-16. doi: 10.1007/s002030050604.
Anaerobic oxidation of phenylalanine and phenylacetate proceeds via alpha-oxidation of phenylacetyl-CoA to phenylglyoxylate. This four-electron oxidation system was studied in the denitrifying bacterium Thauera aromatica. It is membrane-bound and was solubilized with Triton X-100. The system used dichlorophenolindophenol as an artificial electron acceptor; a spectrophotometric assay was developed. No other products besides phenylglyoxylate and coenzyme A were observed. The enzyme was quite oxygen-insensitive and was inactivated by low concentrations of cyanide. Enzyme activity was induced under denitrifying conditions with phenylalanine and phenylacetate, it was low in cells grown with phenylglyoxylate, and it was virtually absent in cells grown with benzoate and nitrate or after aerobic growth with phenylacetate.
苯丙氨酸和苯乙酸的厌氧氧化通过苯乙酰辅酶A的α-氧化生成苯乙二醛酸进行。在反硝化细菌嗜芳烃陶厄氏菌中研究了这种四电子氧化系统。它与膜结合，并用Triton X-100溶解。该系统使用二氯酚靛酚作为人工电子受体；开发了一种分光光度法测定方法。除了苯乙二醛酸和辅酶A外，未观察到其他产物。该酶对氧气相当不敏感，并且会被低浓度的氰化物灭活。在反硝化条件下，用苯丙氨酸和苯乙酸诱导酶活性，在用苯乙二醛酸生长的细胞中酶活性较低，而在用苯甲酸盐和硝酸盐生长的细胞中或在用苯乙酸进行有氧生长后，酶活性几乎不存在。
