EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    2.7.9.1 | more |
differing functions of PPDK in C4 versus C3 plants, PPDK activity in C3 chloroplasts is light-regulated via reversible phosphorylation of an active-site Thr residue by the C3 PPDK regulatory proteins, most unusual bifunctional protein kinase /protein phosphatase, mechanism, overview. AtRP1 is chloroplast-targeted in predominant in greening and green tissues and organs, while AtRP2 is cytosol-localized mainly in seeds and pollen, overview |
Arabidopsis thaliana |
? |
- |
? |
| 2.7.9.1 | more |
Entamoeba histolytica lacks Krebs cycle and oxidative phosphorylation enzymes, and adopts the exclusive way of ATP synthesis through glycolytic pathway. PPDK is the key enzyme essential for the glycolytic pathway in most common and perilous parasite Entamoeba histolytica |
Entamoeba histolytica |
? |
- |
? |
| 2.7.9.1 | more |
specific late-stage accumulation of the pyruvate orthophosphate dikinase, it plays a critical rolein the starch-protein balance through inorganic pyrophosphate-dependent restriction of ADP-glucose synthesis in addition to its usually reported influence on the alanine-aromatic amino acid synthesis balance, overview |
Zea mays |
? |
- |
? |
| 2.7.9.1 | more |
the filarial parasite Brugia malayi lacks pyruvate kinase and instead utilizes the enzyme pyruvate phosphate dikinase, PPDK. The reversible reaction catalyzed by PPDK occurs in three steps, where the outcome depends on the organism glycolysis and ATP formation, or PEP synthesis |
Brugia malayi |
? |
- |
? |
| 2.7.9.1 | more |
swiveling domain mechanism in pyruvate phosphate dikinase, upon detachment from the His domain, the two nucleotide-binding subdomains undergo a hinge motion that opens the active-site cleft, the nucleotide-binding domain undergoes a conformational transition upon binding of Mg2+, ATP, and phosphate, overview |
[Clostridium] symbiosum |
? |
- |
? |
| 2.7.9.1 | more |
coupled assay method with lactate dehydrogenase |
Trypanosoma cruzi |
? |
- |
? |
