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Information on EC 2.7.11.32 - [pyruvate, phosphate dikinase] kinase
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2.7.11.32 [pyruvate, phosphate dikinase] kinaseIUBMB Comments
The enzymes from the plants Zea mays (maize) and Arabidopsis thaliana are bifunctional and catalyse both the phosphorylation and dephosphorylation of EC 2.7.9.1 (pyruvate, phosphate dikinase). cf. EC 2.7.4.27, [pyruvate, phosphate dikinase]-phosphate phosphotransferase [2-5]. The enzyme is specific for a reaction intermediate form of EC 2.7.9.1, and phosphorylates a threonine located adjacent to the catalytic histidine. The phosphorylation only takes place if the histidine is already phosphorylated [3-5].
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- 2.7.11.32
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steroidogenic
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steroidogenesis
- cholesterol
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- progesterone
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granulosa
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herpes
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nucleotide-binding
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beta-adrenergic
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immediate-early
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3beta-hydroxysteroid
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adp-ribosylation
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complement-mediated
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adrenocortical
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gtp-binding
- acth
- phospholamban
- c3b
-
forskolin-stimulated
-
gppnhp
- p450arom
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
[pyruvate, phosphate dikinase]
=
+
[pyruvate, phosphate dikinase] phosphate
Synonyms
regulatory protein, bifunctional regulatory protein, atrp2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PPDK regulatory protein
pyruvate, orthophosphate dikinase regulatory protein
pyruvate, orthophosphate dikinase regulatory protein 1
pyruvate, orthophosphate dikinase regulatory protein 2
pyruvate,Pi dikinase regulatory protein
pyruvate, orthophosphate dikinase regulatory protein
-
bifunctional protein kinase/phosphatase
pyruvate, orthophosphate dikinase regulatory protein 1
bifunctional
pyruvate, orthophosphate dikinase regulatory protein 1
bifunctional Ser/Thr protein kinase/protein phosphatase
pyruvate, orthophosphate dikinase regulatory protein 2
monofunctional Ser/Thr protein kinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ADP + [pyruvate, phosphate dikinase] = AMP + [pyruvate, phosphate dikinase] phosphate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ADP:[pyruvate, phosphate dikinase] phosphotransferase
The enzymes from the plants Zea mays (maize) and Arabidopsis thaliana are bifunctional and catalyse both the phosphorylation and dephosphorylation of EC 2.7.9.1 (pyruvate, phosphate dikinase). cf. EC 2.7.4.27, [pyruvate, phosphate dikinase]-phosphate phosphotransferase [2-5]. The enzyme is specific for a reaction intermediate form of EC 2.7.9.1, and phosphorylates a threonine located adjacent to the catalytic histidine. The phosphorylation only takes place if the histidine is already phosphorylated [3-5].
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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
ADP + [pyruvate phosphate dikinase]
AMP + [pyruvate phosphate dikinase] phosphate
-
-
-
-
?
C4-pyruvate,phosphate dikinase + ADP
[C4-pyruvate,phosphate dikinase]phosphate + AMP
-
active
Thr456 phosphorylated (inactive)
-
?
ADP + [pyruvate, phosphate dikinase]
AMP + [pyruvate, phosphate dikinase] phosphate
-
-
-
?
ADP + [pyruvate, phosphate dikinase]
AMP + [pyruvate, phosphate dikinase] phosphate
-
reversible phosphorylation at Thr527 and Ser528, but not Thr309 and Ser506, of PPDK
-
-
r
ADP + [pyruvate, phosphate dikinase]
AMP + [pyruvate, phosphate dikinase] phosphate
-
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
-
-
r
pyruvate, phosphate dikinase + ADP
[pyruvate, phosphate dikinase] phosphate + AMP
active
inactive
-
?
pyruvate, phosphate dikinase + ADP
[pyruvate, phosphate dikinase] phosphate + AMP
His458 phosphorylated (active), maize wild type and T456S mutant pyruvate, phosphate dikinase serve as substrate, T456V mutant pyruvate, phosphate dikinase serves not as substrate
His458 and Thr456 phosphorylated (inactive)
-
?
pyruvate, phosphate dikinase + ADP
[pyruvate, phosphate dikinase] phosphate + AMP
His458 phosphorylated, active
His458 and Thr456 phosphorylated (inactive)
-
?
pyruvate, phosphate dikinase + ADP
[pyruvate, phosphate dikinase] phosphate + AMP
-
active
Thr residue phosphorylated (inactive)
-
?
pyruvate, phosphate dikinase + ADP
[pyruvate, phosphate dikinase] phosphate + AMP
-
His458 phosphorylated (active)
Thr456 and His458 phosphorylated (inactive)
-
?
pyruvate, phosphate dikinase + ADP
[pyruvate, phosphate dikinase] phosphate + AMP
-
His458 phosphorylated, active
His458 and Thr456 phosphorylated (inactive), T456S mutant protein substrate is also phosphorylated, H456N mutant protein substrat is not phosphorylated
-
?
pyruvate,phosphate dikinase + ADP
[pyruvate,phosphate dikinase]phosphate + AMP
-
His phosphorylated (active)
Thr and His phosphorylated (inactive)
-
?
pyruvate,phosphate dikinase + ADP
[pyruvate,phosphate dikinase]phosphate + AMP
-
His458 phosphorylated (activ), substrate mutant proteins T456Y and H458N are not phosphorylated (mutant protein T456S is phosphorylated), therefore a phosphorylated His458 in the substrate protein is necessary and the regulatory protein is functionally a Ser/Thr protein kinase
His458 and Thr456 phosphorylated (inactive)
-
?
pyruvate,Pi dikinase + ADP
[pyruvate,Pi dikinase]phosphate + AMP
-
His phosphorylated (active), substrate is dephosphorylated by conversion of pyruvate to phosphoenolpyruvate, dephosphorylated substrate serves not as substrate
Thr and His phosphorylated (inactive)
-
?
pyruvate,Pi dikinase + ADP
[pyruvate,Pi dikinase]phosphate + AMP
-
one His residue phosphorylated (active)
a His residue and a Thr residue phosphorylated (inactive)
-
?
pyruvate,Pi dikinase + ADP
[pyruvate,Pi dikinase]phosphate + AMP
-
substrate pyruvate,Pi dikinase is phosphorylated at a His residue and active; CDP shows 40% activity, GDP 35% activity and UDP 0% activity in comparison with ADP
phosphorylated at a Thr residue, inactive
-
?
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
-
-
?
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
-
-
?
additional information
?
-
isoform PDRP2 lacks the phosphotransferase activity of the bifunctional PDRP1 isoform except when PDRP2 in the assays is elevated 5-10fold
-
-
-
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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
ADP + [pyruvate phosphate dikinase]
AMP + [pyruvate phosphate dikinase] phosphate
-
-
-
-
?
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
-
-
?
ADP + [pyruvate, phosphate dikinase]
AMP + [pyruvate, phosphate dikinase] phosphate
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyruvate,Pi dikinase phosphorylated at a Thr residue
-
competitive to ADP; competitive to substrate pyruvate,Pi dikinase
-
[pyruvate,Pi dikinase]phosphate
-
competitive to substrate pyruvate,Pi dikinase; noncompetitive to ADP
-
pyruvate
-
likely inhibits the threonyl-phosphorylation of pyruvate, orthophosphate dikinase by direct competition with regulatory protein for the requisite E-HisP reaction intermediate during catalysis by pyruvate, orthophosphate dikinase, pH not specified in the publication, temperature not specified in the publication
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
pyruvate, phosphate dikinase
-
pH not specified in the publication, temperature not specified in the publication
-
0.0012
pyruvate,Pi dikinase
-
pyruvate,Pi dikinase phosphorylated at a His residue, pH 8.3, temperature not specified in the publication
-
0.05
ADP
-
pH not specified in the publication, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
oxalate
-
pH not specified in the publication, temperature not specified in the publication
0.08
pyruvate
-
interaction with the substrate catalytic phosphorylated intermediate of dikinase, pH 8.3, 30°C
0.08
pyruvate
-
likely inhibits the threonyl-phosphorylation of pyruvate, orthophosphate dikinase by direct competition with regulatory protein for the requisite E-HisP reaction intermediate during catalysis by pyruvate, orthophosphate dikinase, pH not specified in the publication, 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
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme regulates the inorganic phosphate-dependent activation and ADP-dependent inactivation of pyruvate phosphate dikinase by reversible phosphorylation
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
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
additional information from earlier studies included (a) estimates of a monomeric molecular mass of 45000-48000, as determined by size exclusion chromatography and one-dimensional SDS-PAGE; (b) pH-dependent changes in aggregation state (dimeric at pH 7.5, tetrameric at pH 8.3)
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D276A/D277A
-
the mutant exhibits a marked decrease in phosphorylation and dephosphorylation activities as compared to the wild type enzyme
K274A
-
the mutation exhibits little effect on phosphorylation and dephosphorylation activities as compared to the wild type enzyme
P317F
-
the mutant exhibits a marked decrease in phosphorylation and dephosphorylation activities as compared to the wild type enzyme
additional information
additional information
-
many chimeric proteins (regulatory protein 1/regulatory protein 2) are tested for kinase activity and interaction with the substrate protein
additional information
many chimeric proteins (regulatory protein 1/regulatory protein 2) are tested for kinase activity and interaction with the substrate protein
additional information
-
many chimeric proteins (regulatory protein 1/regulatory protein 2) are tested for kinase activity and interaction with the substrate protein, 21 site-directed mutant proteins (conserved amino acid residues) are tested for kinase activity and/or interaction with the substrate protein
additional information
many chimeric proteins (regulatory protein 1/regulatory protein 2) are tested for kinase activity and interaction with the substrate protein, 21 site-directed mutant proteins (conserved amino acid residues) are tested for kinase activity and/or interaction with the substrate protein
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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+)
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged and GFP-fusion proteins expressed in Escherichia coli BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Chastain, C.J.; Chollet, R.
Regulation of pyruvate, orthophosphate dikinase by ADP-/Pi-dependent reversible phosphorylation in C3 and C4 plants
Plant Physiol. Biochem.
41
523-532
2003
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 (Q9MAC9), 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
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
Biochem. J.
236
579-584
1986
Zea mays
brenda
Roeske, C.; Kutny, R.; Budde, R.; Chollet, R.
Sequence of the phosphothreonyl regulatory site peptide from inactive maize leaf pyruvate, orthophosphate dikinase
J. Biol. Chem.
263
6683-6687
1988
Zea mays
brenda
Chastain, C.; Thompson, B.; Chollet, R.
Maize recombinant C4-pyruvate,orthophosphate dikinase: Expression in Escherichia coli, partial purification, and characterization of the phosphorylatable protein
Photosynth. Res.
49
83-89
1996
Zea mays
brenda
Astley, H.; Parsley, K.; Aubry, S.; Chastain, C.; Burnell, J.; Webb, M.; Hibberd, J.
The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis are both bifunctional and interact with the catalytic and nucleotide-binding domains of pyruvate, orthophosphate dikinase
Plant J.
68
1070-1080
2011
Arabidopsis thaliana, Arabidopsis thaliana (O23404)
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
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
brenda
Jiang, L.; Chen, Y.; Zheng, J.; Chen, Z.; Liu, Y.; Tao, Y.; Wu, W.; Chen, Z.; Wang, B.
Structural basis of reversible phosphorylation by maize pyruvate orthophosphate dikinase regulatory protein
Plant Physiol.
170
732-741
2016
Zea mays
brenda
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