Ahmad S, Jensen R A
FEBS Lett. 1987 May 25;216(1):133-9. doi: 10.1016/0014-5793(87)80771-8.
The prephenate dehydrogenase component of the bifunctional T-protein (chorismate mutase:prephenate dehydrogenase) has been shown to utilize L-arogenate, a common precursor of phenylalanine and tyrosine in nature, as a substrate. Partially purified T-protein from Klebsiella pneumoniae and from Escherichia coli strains K 12, B, C and W was used to demonstrate the utilization of L-arogenate as an alternative substrate for prephenate in the presence of nicotinamide adenine dinucleotide as cofactor. The formation of L-tyrosine from L-arogenate by the T-protein dehydrogenase was confirmed by high-performance liquid chromatography. As expected of a common catalytic site, dehydrogenase activity with either prephenate or L-arogenate was highly sensitive to inhibition by L-tyrosine.
双功能T蛋白（分支酸变位酶：预苯酸脱氢酶）的预苯酸脱氢酶组分已被证明可利用L-阿洛酸（一种在自然界中苯丙氨酸和酪氨酸的常见前体）作为底物。使用从肺炎克雷伯菌以及大肠杆菌K12、B、C和W菌株中部分纯化得到的T蛋白，来证明在烟酰胺腺嘌呤二核苷酸作为辅因子存在的情况下，L-阿洛酸可作为预苯酸的替代底物。通过高效液相色谱法证实了T蛋白脱氢酶可将L-阿洛酸转化为L-酪氨酸。正如对共同催化位点所预期的那样，预苯酸或L-阿洛酸的脱氢酶活性对L-酪氨酸的抑制高度敏感。
