Keller B, Keller E, Salcher O, Lingens F
J Gen Microbiol. 1982 Jun;128(6):1199-202. doi: 10.1099/00221287-128-6-1199.
Assays of enzyme activities suggest that arogenate, the product of prephenate transamination, is an intermediate in the biosynthesis of both phenylalanine and tyrosine in Pseudomonas aureofaciens ATCC 15926. In addition to prephenate dehydratase and prephenate dehydrogenase, arogenate dehydratase and arogenate dehydrogenase activities were demonstrated. This pattern of aromatic amino acid biosynthesis in pseudomonads had previously been demonstrated only in P. aeruginosa. Arogenate dehydrogenase from P. aureofaciens differs from that in P. aeruginosa in its utilization of either NAD+ or NADP+ as cofactor and its inhibition by L-tyrosine. During ammonium sulphate fractionation, arogenate dehydratase co-precipitated with prephenate dehydratase I activity and not with prephenate dehydratase II. The pattern of regulation of the arogenate route to tyrosine in P. aureofaciens ATCC 15926 differed from that previously reported for strain ATCC 13986.
酶活性测定表明，预苯酸转氨作用的产物莽草酸是金黄色假单胞菌ATCC 15926中苯丙氨酸和酪氨酸生物合成的中间体。除了预苯酸脱水酶和预苯酸脱氢酶外，还检测到了莽草酸脱水酶和莽草酸脱氢酶的活性。假单胞菌中这种芳香族氨基酸生物合成模式此前仅在铜绿假单胞菌中得到证实。金黄色假单胞菌的莽草酸脱氢酶在辅因子利用上与铜绿假单胞菌不同，它可利用NAD⁺或NADP⁺，且受L-酪氨酸抑制。在硫酸铵分级分离过程中，莽草酸脱水酶与预苯酸脱水酶I活性共沉淀，而不与预苯酸脱水酶II共沉淀。金黄色假单胞菌ATCC 15926中莽草酸转化为酪氨酸的调控模式与之前报道的ATCC 13986菌株不同。
