Literature summary for 2.7.11.32 extracted from

Chen, Y.B.; Lu, T.C.; Wang, H.X.; Shen, J.; Bu, T.T.; Chao, Q.; Gao, Z.F.; Zhu, X.G.; Wang, Y.F.; Wang, B.C.
Posttranslational modification of maize chloroplast pyruvate orthophosphate dikinase reveals the precise regulatory mechanism of its enzymatic activity (2014), Plant Physiol., 165, 534-549.

Search for more literature for 2.7.11.32

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of His-tagged enzyme in Escherichia coli	Zea mays

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chloroplast	-	Zea mays	9507	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ADP + [pyruvate, phosphate dikinase]	Zea mays	reversible phosphorylation at Thr527 and Ser528, but not Thr309 and Ser506, of PPDK	AMP + [pyruvate, phosphate dikinase] phosphate	-	r
additional information	Zea mays	PPDK regulatory protein (PDRP) is a unique bifunctional enzyme, catalyzes this light-dependent regulation by reversible phosphorylation of an active-site Thr527 in PPDK	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Zea mays	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli	Zea mays

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Zea mays	-
mesophyll	-	Zea mays	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
PDRP	-	Zea mays
PPDK regulatory protein	-	Zea mays

Cofactor

Cofactor	Comment	Organism	Structure
ADP	-	Zea mays
AMP	-	Zea mays

General Information

General Information	Comment	Organism
additional information	catalytic mechanism of enzyme PDRP, overview	Zea mays
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	Zea mays

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Release 2023.1 (January 2023)