Information on EC 2.7.11.32 - [pyruvate, phosphate dikinase] kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.11.32
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RECOMMENDED NAME
GeneOntology No.
[pyruvate, phosphate dikinase] kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ADP + [pyruvate, phosphate dikinase] = AMP + [pyruvate, phosphate dikinase] phosphate
show the reaction diagram
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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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
additional information
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catalytic mechanism of enzyme PDRP, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + [pyruvate, phosphate dikinase]
AMP + [pyruvate, phosphate dikinase] phosphate
show the reaction diagram
C4-pyruvate,phosphate dikinase + ADP
[C4-pyruvate,phosphate dikinase]phosphate + AMP
show the reaction diagram
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active
Thr456 phosphorylated (inactive)
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?
pyruvate, phosphate dikinase + ADP
[pyruvate, phosphate dikinase] phosphate + AMP
show the reaction diagram
pyruvate,phosphate dikinase + ADP
[pyruvate,phosphate dikinase]phosphate + AMP
show the reaction diagram
pyruvate,Pi dikinase + ADP
[pyruvate,Pi dikinase]phosphate + AMP
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + [pyruvate, phosphate dikinase]
AMP + [pyruvate, phosphate dikinase] phosphate
show the reaction diagram
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reversible phosphorylation at Thr527 and Ser528, but not Thr309 and Ser506, of PPDK
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r
additional information
?
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PPDK regulatory protein (PDRP) is a unique bifunctional enzyme, catalyzes this light-dependent regulation by reversible phosphorylation of an active-site Thr527 in PPDK
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
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AMP
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP-beta-S
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competitive to ADP
oxalate
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competitive to ADP
oxamate
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pyruvate
pyruvate,Pi dikinase phosphorylated at a Thr residue
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competitive to ADP; competitive to substrate pyruvate,Pi dikinase
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[pyruvate,Pi dikinase]phosphate
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competitive to substrate pyruvate,Pi dikinase; noncompetitive to ADP
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 0.052
ADP
0.0012
pyruvate, phosphate dikinase
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pH not specified in the publication, temperature not specified in the publication
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0.0012
pyruvate,Pi dikinase
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pyruvate,Pi dikinase phosphorylated at a His residue, pH 8.3, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
oxalate
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pH not specified in the publication, temperature not specified in the publication
0.08
pyruvate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.1
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broad optimum pH 7.8-8.4, 68% activity at pH 7.2
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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x * 40000, SDS-PAGE
45000
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x * 45000, SDS-PAGE
90000
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pH 7.5, gel filtration
180000
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pH 8.3, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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)
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilized at 25°C by phosphate, ATP, Blue Dextran and Cibacron blue
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, dye ligand chromatography (agarose-Blue Dextran), gel filtration
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immobilized metal ion affinity chromatography (Ni2+)
immobilized metal ion affinity chromatography (Ni2+); immobilized metal ion affinity chromatography (Ni2+)
partially
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partially purified
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partially, Blue Sepharose chromatography
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recombinant His-tagged enzyme from Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tagged and GFP-fusion proteins expressed in Escherichia coli BL21(DE3); His-tagged and GFP-fusion proteins expressed in Escherichia coli BL21(DE3)
His-tagged protein expressed in Escherichia coli BL21(DE3)pLysS; His-tagged protein expressed in Escherichia coli BL21(DE3)pLysS
His-tagged protein expressed in Escherichia coli NM522
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recombinant expression of His-tagged enzyme in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (5063 entries)
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