Lund P, Wiggins D
Biochem J. 1987 Apr 1;243(1):273-6. doi: 10.1042/bj2430273.
The apparent Ka for N-acetylglutamate of rat liver carbamoyl-phosphate synthase is 11 microM in phosphate buffer, a value 10-fold lower than reported in other buffer systems. Tris and Hepes inhibit competitively with N-acetylglutamate. The proportion of carbamoyl-phosphate synthase in the active enzyme-acetylglutamate complex in vivo may be higher than previous calculations suggest, which re-opens the question of the involvement of N-acetylglutamate in the regulation of urea synthesis.
大鼠肝脏氨甲酰磷酸合成酶的N - 乙酰谷氨酸表观解离常数(Ka)在磷酸盐缓冲液中为11微摩尔,该值比在其他缓冲系统中报道的低10倍。Tris和Hepes与N - 乙酰谷氨酸竞争性抑制。体内活性酶 - 乙酰谷氨酸复合物中氨甲酰磷酸合成酶的比例可能高于先前计算结果所显示的,这重新引发了N - 乙酰谷氨酸参与尿素合成调节的问题。