Literature summary for 2.7.11.32 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.

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Inhibitors

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

Organism

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

Purification (Commentary)

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

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Zea mays	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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

Synonyms	Comment	Organism
ADP:protein phosphotransferase	-	Zea mays
regulatory protein	-	Zea mays

Ki Value [mM]

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

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Release 2023.1 (January 2023)