2.7.11.32	ADP + [pyruvate phosphate dikinase]	-	Zea mays	AMP + [pyruvate phosphate dikinase] phosphate	-	?	458487	
2.7.11.32	ADP + [pyruvate, phosphate dikinase]	-	Zea mays	AMP + [pyruvate, phosphate dikinase] phosphate	-	?	438181	
2.7.11.32	ADP + [pyruvate, phosphate dikinase]	reversible phosphorylation at Thr527 and Ser528, but not Thr309 and Ser506, of PPDK	Zea mays	AMP + [pyruvate, phosphate dikinase] phosphate	-	r	438181	
2.7.11.32	ADP + [pyruvate, phosphate dikinase]	i.e. recombinant His-tagged wild-type and mutant maize PPDKs as substrates, reversible phosphorylation at Thr527 and Ser528, but not Thr309 and Ser506, of PPDK. Phosphorylation is detected on wild-type PPDK, PPDK-T309A, and PPDK-S506A, but not on PPDK-T527A, PPDK-S528A, or PPDK-H529A	Zea mays	AMP + [pyruvate, phosphate dikinase] phosphate	-	r	438181	
2.7.11.32	C4-pyruvate,phosphate dikinase + ADP	active	Zea mays	[C4-pyruvate,phosphate dikinase]phosphate + AMP	Thr456 phosphorylated (inactive)	?	423090	
2.7.11.32	additional information	PPDK regulatory protein (PDRP) is a unique bifunctional enzyme, catalyzes this light-dependent regulation by reversible phosphorylation of an active-site Thr527 in PPDK	Zea mays	?	-	?	89	
2.7.11.32	additional information	modeling suggests that the two hydrogen bonds between the highly conserved residues Ser528 and Gly525 are required for PDRP-mediated phosphorylation of the active-site Thr527 of PPDK, substrate PPDK three-dimensional structure analysis, overview	Zea mays	?	-	?	89	
2.7.11.32	additional information	isoform PDRP2 lacks the phosphotransferase activity of the bifunctional PDRP1 isoform except when PDRP2 in the assays is elevated 5-10fold	Zea mays	?	-	-	89	
2.7.11.32	pyruvate, phosphate dikinase + ADP	active	Arabidopsis thaliana	[pyruvate, phosphate dikinase] phosphate + AMP	inactive	?	423992	
2.7.11.32	pyruvate, phosphate dikinase + ADP	active	Oryza sativa	[pyruvate, phosphate dikinase] phosphate + AMP	Thr residue phosphorylated (inactive)	?	423992