Hayashi S, Tanaka T, Naito J, Suda M
J Biochem. 1975 Jan 1;77(1?):207-19.
The importance of the so-called phosphorylated pathway for the synthesis of serine in rat liver was confirmed by studies on in vitro serine synthesis and also by the existence of a correlation between the serine-synthesizing activity of liver extracts and the activities of the enzymes involved in the pathway under various dietary conditions. Serine-synthesizing activity was found to be distributed in various rat tissues such as kidney, brain, testis, spleen, pancreas, and fat pad. However, only in the liver was the synthesis regulated by dietary protein. In the liver, the three enzymes of the phosphorylated pathway were found to be repressed by high-protein diets or by starvation and induced by low-protein diets. The dietary induction of the enzymes required the presence of insulin and was suppressed by glucocorticoids. A suggestion is made that the effects of diet or hormones may be mediated by changes in the hepatic pool of essential amino acids.
通过对体外丝氨酸合成的研究以及在各种饮食条件下肝脏提取物的丝氨酸合成活性与该途径中相关酶活性之间存在的相关性,证实了大鼠肝脏中所谓的磷酸化途径对丝氨酸合成的重要性。发现丝氨酸合成活性分布于大鼠的各种组织中,如肾脏、大脑、睾丸、脾脏、胰腺和脂肪垫。然而,只有肝脏中的合成受饮食蛋白质的调节。在肝脏中,发现磷酸化途径的三种酶受到高蛋白饮食或饥饿的抑制,并被低蛋白饮食诱导。这些酶的饮食诱导需要胰岛素的存在,并受到糖皮质激素的抑制。有人提出,饮食或激素的作用可能是由肝脏必需氨基酸池的变化介导的。