Abstract
Pyruvate, orthophosphate dikinase (PPDK, E.C. 2.7.9.1) is a cardinal carbon-assimilating, stromal enzyme of the C 4 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.
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