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Regulation of pyruvate, orthophosphate dikinase by ADP-/Pi-dependent reversible phosphorylation in C3 and C4 plants

Journal

PLANT PHYSIOLOGY AND BIOCHEMISTRY
Volume 41, Issue 6-7, Pages 523-532

Publisher

ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/S0981-9428(03)00065-2

Keywords

C-4 photosynthesis; C-3 plant; PPDK; PPDK regulatory protein; protein phosphorylation/dephosphorylation; pyruvate; Pi dikinase; RP

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Pyruvate, orthophosphate dikinase (PPDK, E.C. 2.7.9.1) is a cardinal carbon-assimilating, stromal enzyme of the C, photosynthetic pathway. Like several other photosynthetic pathway enzymes, its activity is strictly and reversibly regulated by light. This regulation is conferred by the PPDK regulatory protein (RP), a bifunctional protein kinase/phosphatase that catalyzes the ADP-/Pi-dependent, reversible phosphorylation of an active-site threonine residue. In this minireview, we highlight how plastidic PPDK in leaves and developing seeds of C-3 plants is regulated in an identical manner as C-4 PPDK via a putative C-3-RP isoform. Additionally, we also detail the progress in research concerning C-4 RP. since this highly unusual regulatory enzyme was last reviewed nearly two decades ago. (C) 2003 Editions scientifiques et medicales Elsevier SAS. All rights reserved.

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