Fazel A M, Bowen J R, Jensen R A
Proc Natl Acad Sci U S A. 1980 Mar;77(3):1270-3. doi: 10.1073/pnas.77.3.1270.
Wild-type Brevibacterium flavum has been shown to possess arogenate dehydrogenase activity and to lack prephenate dehydrogenase, thereby providing presumptive evidence that arogenate (previously named "pretyrosine") is an obligatory intermediate of L-tyrosine biosynthesis. A similar enzymological pattern has been discerned in extracts made from wild-type cultures of various species of cyanobacteria. Application of rigorous molecular genetic criteria in confirmation of the exclusive role of arogenate in L-tyrosine synthesis was made possible by the isolation of an auxotrophic mutant exhibiting a nutritional requirement for L-tyrosine. The mutant was found to lack activity for arogenate dehydrogenase and to accumulate substantial amounts of arogenate behind the mutant block during starvation for L-tyrosine.
野生型黄色短杆菌已被证明具有预苯酸脱氢酶活性且缺乏苯丙酮酸脱氢酶,从而提供了推测性证据,表明预苯酸(以前称为“前酪氨酸”)是L-酪氨酸生物合成的必需中间体。在从各种蓝细菌的野生型培养物中提取的提取物中也发现了类似的酶学模式。通过分离出对L-酪氨酸有营养需求的营养缺陷型突变体,得以应用严格的分子遗传学标准来证实预苯酸在L-酪氨酸合成中的唯一作用。该突变体被发现缺乏预苯酸脱氢酶活性,并且在缺乏L-酪氨酸的饥饿期间,在突变体阻断位点之后积累了大量的预苯酸。