Regulation of the activity of the pyruvate dehydrogenase complex of Escherichia coli.
Regulation of the activity of the pyruvate dehydrogenase complex of Escherichia coli.
复制标题
DOI：
10.1021/bi00808a019
复制
发表时间：
1970-03
期刊：
影响因子：
2.9
通讯作者：
E. R. Schwartz;L. Reed
中科院分区：
文献类型：
--
作者：
E. R. Schwartz;L. Reed
伊迪丝河大肠杆菌丙酮酸脱氢酶复合物的活性被鸟苷三磷酸和乙酰辅酶A抑制。在所用条件下，酶复合物不受腺苷三磷酸、胞苷三磷酸或尿苷三磷酸的抑制。三磷酸鸟苷的抑制作用可被二磷酸鸟苷特异性逆转。乙酰辅酶A与丙酮酸竞争，而鸟苷三磷酸与丙酮酸不竞争。三磷酸鸟苷和乙酰辅酶A似乎作用于该酶的丙酮酸脱氢酶组分上的独立位点
Edith R. Schwartz and Lester J. Reed abstract: The activity of the Escherichia coli pyruvate dehydrogenase complex is inhibited by guanosine triphosphate and by acetyl coenzyme A. The enzyme complex was not inhibited by adenosine triphosphate, cytidine triphosphate, or uridine triphosphate under the conditions used. The inhibition by guanosine triphosphate is reversedspecifically by guanosine diphosphate. Acetyl coenzyme A is competitive with pyruvate, whereas guanosine triphosphate is noncom-petitive with pyruvate. Guanosine triphosphate and acetyl coenzyme A appear to act at separate and independent sites on the pyruvate dehydrogenase component of the enzyme