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Literature summary extracted from

  • Budde, R.; Ernst, S.; Chollet, R.
    Substrate specificity and regulation of the maize (Zea mays) leaf ADP: protein phosphotransferase catalysing phosphorylation/inactivation of pyruvate, orthophosphate dikinase (1986), Biochem. J., 236, 579-584.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.32 pyruvate competitive, interaction with the substrate catalytic phosphorylated intermediate of dikinase Zea mays

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.32 Zea mays
-
 cv. Golden Cross Bantam
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.32 partially, Blue Sepharose chromatography Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.32 leaf
-
 Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.32 pyruvate,Pi dikinase + ADP His phosphorylated (active), substrate is dephosphorylated by conversion of pyruvate to phosphoenolpyruvate, dephosphorylated substrate serves not as substrate Zea mays [pyruvate,Pi dikinase]phosphate + AMP Thr and His phosphorylated (inactive) ?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.32 ADP:protein phosphotransferase
-
 Zea mays
2.7.11.32 regulatory protein
-
 Zea mays

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.11.32 0.08
-
 pyruvate interaction with the substrate catalytic phosphorylated intermediate of dikinase, pH 8.3, 30°C Zea mays