Gueguen P, Padron M, Perbal B, Hervé G
Biochim Biophys Acta. 1980 Sep 9;615(1):59-69. doi: 10.1016/0005-2744(80)90008-x.
Amino acid-requiring mutants capable of producing derepressed levels of aspartate transcarbamylase (carbamoylphosphate:L-aspartate carbamoyltransferase, EC 2.1.3.2) were obtained and used for the incorporation in this enzyme of eight different amino acid analogs. These amino acid replacements enabled the biosynthesis of a series of modified aspartate transcarbamylases altered in their catalytic or regulatory properties. The enzyme in which phenylalanine was rereplaced by 2-fluorophenylalanine was purified to homogeneity and appeared to have the same specific activity as normal asparate transcarbamylase but lacking both homotropic and heterotropic interactions.
获得了能够产生去阻遏水平的天冬氨酸转氨甲酰酶（氨甲酰磷酸：L-天冬氨酸氨甲酰转移酶，EC 2.1.3.2）的氨基酸需求突变体，并将其用于在该酶中掺入八种不同的氨基酸类似物。这些氨基酸替换使得能够生物合成一系列在催化或调节特性上发生改变的修饰天冬氨酸转氨甲酰酶。将苯丙氨酸被2-氟苯丙氨酸取代的酶纯化至同质，其比活性似乎与正常天冬氨酸转氨甲酰酶相同，但缺乏同促和异促相互作用。
