Literature summary for 2.7.4.27 extracted from

Jiang, L.; Chen, Y.B.; Zheng, J.; Chen, Z.; Liu, Y.; Tao, Y.; Wu, W.; Chen, Z.; Wang, B.C.
Structural basis of reversible phosphorylation by maize pyruvate orthophosphate dikinase regulatory protein (2016), Plant Physiol., 170, 732-741.

Search for more literature for 2.7.4.27

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) RIL	Zea mays

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified apoenzyme, mixing of 10 mg/m protein with a well solution containing 1.0 M K/Na tartrate, 0.1 M MOPS, pH 8.0, 1% dioxane, 1 mM AMP, and 2 mM Mg2+,.X-ray diffraction structure determination and analysis at 3.2 A resolution	Zea mays

Localization

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Zea mays	pyruvate orthophosphate dikinase regulatory protein, PDRP, is a bifunctional enzyme that catalyzes both phosphorylation and dephosphorylation of the pyruvate orthophosphate dikinase. Enzyme PDRP uses ADP as the phosphoryl donor for kinase activity, and employs a phosphate-dependent, diphosphate-forming dephosphorylation mechanism	?	-	?
[pyruvate, phosphate dikinase] phosphate + phosphate	Zea mays	-	[pyruvate, phosphate dikinase] + diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Zea mays	Q195N6	gene PDRP1	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) RIL by nickel affinity chromatography	Zea mays

Reaction

Reaction	Comment	Organism	Reaction ID
[pyruvate, phosphate dikinase] phosphate + phosphate = [pyruvate, phosphate dikinase] + diphosphate	enzyme PDRP contains a single active site that catalyzes both phosphorylation and dephosphorylation, cf. EC 2.7.11.32. Catalytic mechanism of PPDK regulatory protein, overview	Zea mays	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Zea mays	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	pyruvate orthophosphate dikinase regulatory protein, PDRP, is a bifunctional enzyme that catalyzes both phosphorylation and dephosphorylation of the pyruvate orthophosphate dikinase. Enzyme PDRP uses ADP as the phosphoryl donor for kinase activity, and employs a phosphate-dependent, diphosphate-forming dephosphorylation mechanism	Zea mays	?	-	?
[pyruvate, phosphate dikinase] phosphate + phosphate	-	Zea mays	[pyruvate, phosphate dikinase] + diphosphate	-	?
[pyruvate, phosphate dikinase] phosphate + phosphate	-	Zea mays	[pyruvate, phosphate dikinase] + diphosphate	reversible phosphorylation by maize pyruvate orthophosphate dikinase regulatory protein. The bifunctional enzyme exhibits kinase activity, EC 2.7.11.32, and dephosphorylation activity, EC 2.7.4.27	?

Subunits

Subunits	Comment	Organism
homodimer	enzyme PDRP forms a compact homodimer in which each protomer contains two separate N-terminal and C-terminal domains. The N-terminal domain has conserved intramolecular and intermolecular disulfide bonds for enzyme PDRP dimerization. Three-dimensional structure analysis, overview. The C-terminal domain is the site of both kinase and diphosphorylase activities	Zea mays

Synonyms

Synonyms	Comment	Organism
PDRP	-	Zea mays
PDRP1	-	Zea mays
PPDK regulatory protein	-	Zea mays
pyruvate orthophosphate dikinase regulatory protein	-	Zea mays

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	asay at	Zea mays

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	dephosphorylation assay at	Zea mays
8.3	-	kinase assay at	Zea mays

General Information

General Information	Comment	Organism
evolution	PDRP shares no significant sequence similarity with other protein kinases or phosphatases	Zea mays
additional information	PDRP forms a compact homodimer in which each protomer contains two separate N-terminal and C-terminal domains. The C-terminal domain includes several key elements for performing both phosphorylation and dephosphorylation activities: the phosphate binding loop (P-loop) for binding the ADP and inorganic phosphate substrates, residues Lys274 and Lys299 for neutralizing the negative charge, and residue Asp277 for protonating and deprotonating the target Thr residue of PPDK to promote nucleophilic attack. The N-terminal domain shares the same protein fold as the C-terminal domain and also includes a putative P-loop with AMP bound but lacking enzymatic activities. This loop may participate in the interaction with and regulation of enzyme PPDK. The N-terminal domain has conserved intramolecular and intermolecular disulfide bonds for PDRP dimerization. Three-dimensional structure analysis, overview	Zea mays
physiological function	PPDK regulatory protein (PDRP) regulates the inorganic phosphate-dependent activation and ADP-dependent inactivation of PPDK by reversible phosphorylation. Pyruvate orthophosphate dikinase (PPDK) is one of the most important enzymes in C4 photosynthesis	Zea mays

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Release 2023.1 (January 2023)