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catalytic mechanism of enzyme PDRP, overview
physiological function
in C4 plants, pyruvate orthophosphate dikinase (PPDK) activity is tightly dark/light regulated by reversible phosphorylation of an active-site threonine residue. The process is catalyzed by PPDK regulatory protein (PDRP). Phosphorylation and dephosphorylation of PPDK lead to its inactivation and activation, respectively. The amount of PPDK (unphosphorylated) involved in C4 photosynthesis is indeed strictly controlled by light intensity, despite the high levels of PPDK protein that accumulate in mesophyll chloroplasts, regulation by light intensity rather than the light/dark transition. Diverse regulatory pathways may work alone or in combination to fine-tune C4PPDK activity in response to changes in lighting. Residue Ser528 plays an essential role in PDRP regulation of PPDK phosphorylation at Thr527
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