C4光合作用中丙酮酸磷酸双激酶的催化去磷酸化及Pi介导的激活调控

Regulation of C4 photosynthesis catalytic dephosphorylation and Pi-mediated activation of pyruvate Pi dikinase.

作者信息

Burnell J N

出版信息

Biochem Biophys Res Commun. 1984 Apr 30;120(2):559-65. doi: 10.1016/0006-291x(84)91291-9.

DOI:10.1016/0006-291x(84)91291-9

Abstract

In experiments designed to test the reversibility of ADP-dependent inactivation and Pi-dependent activation of pyruvate, Pi dikinase , it was found that the preferred substrate for Pi dependent activation is the catalytically non-phosphorylated form of pyruvate, Pi dikinase . Only the second of the two partial reactions catalysed by pyruvate, Pi dikinase is inhibited when pyruvate, Pi dikinase is inactivated by ADP-dependent phosphorylation. Neither ADP-dependent inactivation nor Pi-dependent activation reactions were found to be reversible.

摘要

在旨在测试丙酮酸磷酸二激酶的ADP依赖性失活和Pi依赖性激活的可逆性的实验中，发现Pi依赖性激活的优选底物是丙酮酸磷酸二激酶的催化非磷酸化形式。当丙酮酸磷酸二激酶通过ADP依赖性磷酸化失活时，丙酮酸磷酸二激酶催化的两个部分反应中只有第二个反应受到抑制。未发现ADP依赖性失活反应和Pi依赖性激活反应是可逆的。

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