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Information on EC 2.7.4.27 - [pyruvate, phosphate dikinase]-phosphate phosphotransferase
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EC Tree
2.7.4.27 [pyruvate, phosphate dikinase]-phosphate phosphotransferaseIUBMB Comments
The enzyme from the plants maize and Arabidopsis is bifunctional and also catalyses the phosphorylation of pyruvate, phosphate dikinase (EC 2.7.9.1), cf. EC 2.7.11.32, [pyruvate, phosphate dikinase] kinase [2-5].
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
[pyruvate, phosphate dikinase] phosphate
+
=
[pyruvate, phosphate dikinase]
+
Synonyms
pdrp1, atrp1, ppdk regulatory protein, pdrp2, c4 chloroplast ppdk, pyruvate,pi dikinase regulatory protein, pyruvate orthophosphate dikinase regulatory protein, bifunctional regulatory protein of pyruvate,orthophosphate dikinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PDRP1
PDRP2
PPDK regulatory protein
pyruvate, orthophosphate dikinase regulatory protein 1
bifunctional protein kinase/protein phosphatase
pyruvate,Pi dikinase regulatory protein
PDRP1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[pyruvate, phosphate dikinase] phosphate + phosphate = [pyruvate, phosphate dikinase] + diphosphate
[pyruvate, phosphate dikinase] phosphate + phosphate = [pyruvate, phosphate dikinase] + diphosphate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
[pyruvate, phosphate dikinase] phosphate:phosphate phosphotransferase
The enzyme from the plants maize and Arabidopsis is bifunctional and also catalyses the phosphorylation of pyruvate, phosphate dikinase (EC 2.7.9.1), cf. EC 2.7.11.32, [pyruvate, phosphate dikinase] kinase [2-5].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[pyruvate, phosphate dikinase] phosphate + phosphate
pyruvate, phosphate dikinase + diphosphate
[pyruvate, phosphate dikinase] phosphate + phosphate
[pyruvate, phosphate dikinase] + diphosphate
[pyruvate,phosphate dikinase]phosphate + phosphate
pyruvate,phosphate dikinase + diphosphate
[pyruvate, phosphate dikinase] phosphate + phosphate
pyruvate, phosphate dikinase + diphosphate
His458 and Thr456 phosphorylated (inactive), strict requirement for the threonyl phosphate, unable to dephosphorylate Ser-P at this same position
His458 phosphorylated (active)
-
?
[pyruvate, phosphate dikinase] phosphate + phosphate
pyruvate, phosphate dikinase + diphosphate
-
Thr residue phosphorylated (inactive)
active
-
?
[pyruvate, phosphate dikinase] phosphate + phosphate
pyruvate, phosphate dikinase + diphosphate
-
-
-
?
[pyruvate, phosphate dikinase] phosphate + phosphate
pyruvate, phosphate dikinase + diphosphate
-
Thr456 and His458 phosphorylated (inactive)
His458 phosphorylated (active)
-
?
[pyruvate, phosphate dikinase] phosphate + phosphate
[pyruvate, phosphate dikinase] + diphosphate
-
-
-
?
[pyruvate, phosphate dikinase] phosphate + phosphate
[pyruvate, phosphate dikinase] + diphosphate
-
reversible phosphorylation at Thr527 by maize pyruvate orthophosphate dikinase regulatory protein. The level of C4PPDK phosphorylated at Ser528 is much lower than that at Thr527 in maize leaves, meaning that phosphorylation at Ser528 is not as important as at Thr527 for the regulation of PPDK activity. The bifunctional enzyme exhibits kinase activity, EC 2.7.11.32, and dephosphorylation activity, EC 2.7.4.27, reversible phosphorylation by maize pyruvate orthophosphate dikinase regulatory protein. Residues Thr527 and Ser528, but not Thr309 and Ser506, are targets of PDRP. The bifunctional enzyme exhibits kinase activity, EC 2.7.11.32, and dephosphorylation activity, EC 2.7.4.27
-
?
[pyruvate, phosphate dikinase] phosphate + phosphate
[pyruvate, phosphate dikinase] + diphosphate
-
-
reversible phosphorylation by maize pyruvate orthophosphate dikinase regulatory protein. Residues Thr527 and Ser528, but not Thr309 and Ser506, are targets of PDRP. The bifunctional enzyme exhibits kinase activity, EC 2.7.11.32, and dephosphorylation activity, EC 2.7.4.27
-
?
[pyruvate, phosphate dikinase] phosphate + phosphate
[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
-
?
[pyruvate,phosphate dikinase]phosphate + phosphate
pyruvate,phosphate dikinase + diphosphate
-
His458 and Thr456 phosphorylated (inactive)
His458 phosphorylated (active)
-
?
[pyruvate,phosphate dikinase]phosphate + phosphate
pyruvate,phosphate dikinase + diphosphate
-
Thr residue phosphorylated (inactive)
active
-
ir
[pyruvate,phosphate dikinase]phosphate + phosphate
pyruvate,phosphate dikinase + diphosphate
-
Thr456 phosphorylated (inactive)
active
-
?
[pyruvate,Pi dikinase]phosphate + phosphate
pyruvate,Pi dikinase + diphosphate
-
a His residue and a Thr residue phosphorylated (inactive)
one His residue phosphorylated (active)
-
?
[pyruvate,Pi dikinase]phosphate + phosphate
pyruvate,Pi dikinase + diphosphate
-
phosphorylated at a Thr residue, inactive, additionally catalytically phosphorylated substrate (at His residue) is a much poorer substrate
active
-
?
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
-
-
?
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
-
-
?
additional information
?
-
isoform PDRP2 lacks the PPDK-P dephosphorylation activity of the PDRP1 isoform except when PDRP2 in the assays is elevated 5- to 10fold
-
-
-
additional information
?
-
isoform PDRP2 lacks the PPDK-P dephosphorylation activity of the PDRP1 isoform except when PDRP2 in the assays is elevated 5- to 10fold
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[pyruvate, phosphate dikinase] phosphate + phosphate
[pyruvate, phosphate dikinase] + diphosphate
[pyruvate, phosphate dikinase] phosphate + phosphate
[pyruvate, phosphate dikinase] + diphosphate
-
-
-
?
[pyruvate, phosphate dikinase] phosphate + phosphate
[pyruvate, phosphate dikinase] + diphosphate
-
reversible phosphorylation at Thr527 by maize pyruvate orthophosphate dikinase regulatory protein. The level of C4PPDK phosphorylated at Ser528 is much lower than that at Thr527 in maize leaves, meaning that phosphorylation at Ser528 is not as important as at Thr527 for the regulation of PPDK activity. The bifunctional enzyme exhibits kinase activity, EC 2.7.11.32, and dephosphorylation activity, EC 2.7.4.27
-
?
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
-
-
?
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP-beta-S
-
competitive to substrate [pyruvate,Pi dikinase]phosphate (phosphorylated at a Thr residue)
Cibacron blue
-
competitive to substrate [pyruvate,Pi dikinase]phosphate (phosphorylated at a Thr residue)
diphosphate
-
competitive to substrate [pyruvate,Pi dikinase]phosphate (phosphorylated at a Thr residue)
pyruvate,Pi dikinase phosphorylated at a His residue
-
competitive to substrate [pyruvate,Pi dikinase]phosphate (phosphorylated at a Thr residue)
-
ADP
-
competitive to substrate [pyruvate,Pi dikinase]phosphate (phosphorylated at a Thr residue)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007
[pyruvate,Pi dikinase]phosphate
-
phosphorylated at a Thr residue, pH 8.3, temperature not specified in the publication
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
ADP-beta-S
-
Ki-value below 0.08 mM, pH 8.3, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
isoform PDRP2 is strictly expressed in bundle sheath strand cells
brenda
isoform PDRP1 is strictly expressed in mesophyll cells
brenda
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
PDRP shares no significant sequence similarity with other protein kinases or phosphatases
evolution
two loci for PPDK genes in maize chromosomes: one locus can transcribe two overlapping genes (C4 chloroplast PPDK [C4ppdk] and cytosolic PPDK [CyppdkZm1]) that are divergent at their 5' ends owing to different transcription initiation sites, isozyme sequences comparisons, the two peptides differ by 42 D, overview
physiological function
in C4 plants, pyruvate orthophosphate dikinase (PPDK) activity is tightly dark/light regulated by reversible phosphorylation of an active-site threonine residue catalyzed by PPDK regulatory protein (PDRP). Phosphorylation and dephosphorylation of PPDK lead to its inactivation and activation of PPDK, respectively. Light intensity rather than the light/dark transition regulates PPDK activity by modulating the reversible phosphorylation at Thr527 of PPDK in Zea mays. The amount of unphosphorylated PPDK involved in C4 photosynthesis is strictly controlled by light intensity, despite the high levels of PPDK protein that accumulate in mesophyll chloroplasts. The regulation of maize plastid PPDK isoform (C4PPDK) activity is complex, overview
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
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
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
additional information
the two hydrogen bonds between the highly conserved residues Ser528 and Gly525 are required for enzyme PDRP-mediated phosphorylation of the active site residue Thr527 of PPDK
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
180000
48000
90000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homotetramer
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, dye ligand chromatography (agarose-Blue Dextran), gel filtration
-
immobilized metal ion affinity chromatography (Ni2+)
partially purified, ammonium sulfate precipitation, dye ligand chromatography (Blue-Sepharose, agarose-blue dextran), gel filtration
-
partially purified, ammonium sulfate precipitation, dye-ligand chromatography (Blue Sepharose), gel filtration, anion exchange chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) RIL by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged and GFP-fusion proteins expressed in Escherichia coli BL21(DE3)
recombinant overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) RIL
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Smith, C.M.; Duff, S.M.; Chollet, R.
Partial purification and characterization of maize-leaf pyruvate, orthophosphate dikinase regulatory protein: a low-abundance, mesophyll-chloroplast stromal protein
Arch. Biochem. Biophys.
308
200-206
1994
Zea mays
brenda
Chastain, C.J.; Botschner, M.; Harrington, G.E.; Thompson, B.J.; Mills, S.E.; Sarath, G.; Chollet, R.
Further analysis of maize C(4) pyruvate,orthophosphate dikinase phosphorylation by its bifunctional regulatory protein using selective substitutions of the regulatory Thr-456 and catalytic His-458 residues
Arch. Biochem. Biophys.
375
165-170
2000
Zea mays
brenda
Burnell, J.N.; Chastain, C.J.
Cloning and expression of maize-leaf pyruvate, Pi dikinase regulatory protein gene
Biochem. Biophys. Res. Commun.
345
675-680
2006
Zea mays
brenda
Chastain, C.J.; Heck, J.W.; Colquhoun, T.A.; Voge, D.G.; Gu, X.Y.
Posttranslational regulation of pyruvate, orthophosphate dikinase in developing rice (Oryza sativa) seeds
Planta
224
924-934
2006
Oryza sativa
brenda
Chastain, C.J.; Xu, W.; Parsley, K.; Sarath, G.; Hibberd, J.M.; Chollet, R.
The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis possess a novel, unprecedented Ser/Thr protein kinase primary structure
Plant J.
53
854-863
2008
Arabidopsis thaliana (O49562), Arabidopsis thaliana
brenda
Burnell, J.; Hatch, M.
Regulation of C4 photosynthesis: Identification of a catalytically important histidine residue and its role in the regulation of pyruvate,Pi dikinase
Arch. Biochem. Biophys.
231
175-182
1984
Zea mays
brenda
Burnell, J.; Hatch, M.
Regulation of C4 photosynthesis: Purification and properties of the protein catalyzing ADP-mediated inactivation and Pi-mediated activation of pyruvate,Pi dikinase
Arch. Biochem. Biophys.
237
490-503
1985
Zea mays
brenda
Roeske, C.; Chollet, R.
Chemical modification of the bifunctional regulatory protein of maize leaf pyruvate,orthophosphate dikinase. Evidence for two distinct active sites
J. Biol. Chem.
262
12575-12582
1987
Zea mays
brenda
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
Plant Physiol.
165
534-549
2014
Zea mays (Q195N6), Zea mays
brenda
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
Plant Physiol.
170
732-741
2016
Zea mays (Q195N6), Zea mays
brenda
Chastain, C.J.; Baird, L.M.; Walker, M.T.; Bergman, C.C.; Novbatova, G.T.; Mamani-Quispe, C.S.; Burnell, J.N.
Maize leaf PPDK regulatory protein isoform-2 is specific to bundle sheath chloroplasts and paradoxically lacks a Pi-dependent PPDK activation activity
J. Exp. Bot.
69
1171-1181
2018
Zea mays (A0A1D6IDV8), Zea mays (Q195N6), Zea mays
brenda
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