Regulation of C4 photosynthesis catalytic dephosphorylation and Pi-mediated activation of pyruvate Pi dikinase.
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.
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000249:Adenosine Monophosphate / Q000494:pharmacology; D011756:Diphosphates / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D010728:Phosphoenolpyruvate / Q000378:metabolism; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism*; D010788:Photosynthesis; D010944:Plants / Q000378:metabolism*; D011772:Pyruvate, Orthophosphate Dikinase / Q000378:metabolism*; D011773:Pyruvates / Q000378:metabolism; D019289:Pyruvic Acid; D003313:Zea mays
D011756:Diphosphates; D011773:Pyruvates; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D010728:Phosphoenolpyruvate; D019289:Pyruvic Acid; D010770:Phosphotransferases; D011772:Pyruvate, Orthophosphate Dikinase