鸟氨酸脱羧酶
磷酰胆碱
胆碱激酶
鸟氨酸脱羧酶抗体
生物化学
羧基裂解酶
多胺
化学
鸟氨酸
腺苷甲硫氨酸脱羧酶
酶
生物
氨基酸
磷脂酰胆碱
精氨酸
磷脂
膜
作者
Gad M. Gilad,Varda H. Gilad
标识
DOI:10.1016/0006-291x(84)90471-6
摘要
Ornithine decarboxylase, which catalyzes the first step in polyamine biosynthesis, is rapidly and transiently increased in various tissues during growth and after various hormonal or noxious stimuli, prior to an elevation in choline kinase activity. Polyamines themselves have been demonstrated to activate choline kinase. The present study sought to determine the effect of phosphorylcholine, the product of the reaction catalyzed by choline kinase, on ornithine decarboxylase activity. The data demonstrate that ornithine decarboxylase activity. The data demonstrate that ornithine decarboxylase activity is inhibited by phosphorylcholine and more potently by the related compound phosphorylethanolamine. The inhibition by both compounds led to decreased affinity of partially purified ornithine decarboxylase for ornithine. The inhibition is not time dependent and reversible. Both compounds also inhibit glutamic acid decarboxylase activity. The results suggest that high intracellular levels of phosphorylethanolamine and phosphorylcholine can serve as natural inhibitors of decarboxylases.
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