Information on EC 2.7.4.27 - [pyruvate, phosphate dikinase]-phosphate phosphotransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.4.27
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RECOMMENDED NAME
GeneOntology No.
[pyruvate, phosphate dikinase]-phosphate phosphotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[pyruvate, phosphate dikinase] phosphate + phosphate = [pyruvate, phosphate dikinase] + diphosphate
show the reaction diagram
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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[pyruvate, phosphate dikinase] phosphate + phosphate
pyruvate, phosphate dikinase + diphosphate
show the reaction diagram
[pyruvate, phosphate dikinase] phosphate + phosphate
[pyruvate, phosphate dikinase] + diphosphate
show the reaction diagram
[pyruvate,phosphate dikinase]phosphate + phosphate
pyruvate,phosphate dikinase + diphosphate
show the reaction diagram
[pyruvate,Pi dikinase]phosphate + phosphate
pyruvate,Pi dikinase + diphosphate
show the reaction diagram
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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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
[pyruvate, phosphate dikinase] phosphate + phosphate
[pyruvate, phosphate dikinase] + diphosphate
show the reaction diagram
additional information
?
-
Q195N6
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 hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-nitro-5-thiocyanatobenzoate
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ADP-beta-S
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competitive to substrate [pyruvate,Pi dikinase]phosphate (phosphorylated at a Thr residue)
CDP
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Cibacron blue
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competitive to substrate [pyruvate,Pi dikinase]phosphate (phosphorylated at a Thr residue)
diphosphate
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competitive to substrate [pyruvate,Pi dikinase]phosphate (phosphorylated at a Thr residue)
GDP
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Phenylglyoxal
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pyridoxal 5'-phosphate
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pyruvate,Pi dikinase phosphorylated at a His residue
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competitive to substrate [pyruvate,Pi dikinase]phosphate (phosphorylated at a Thr residue)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65 - 0.67
phosphate
0.0007
[pyruvate,Pi dikinase]phosphate
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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 hide
LITERATURE
IMAGE
0.085
ADP
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pH 8.3, temperature not specified in the publication
0.08
ADP-beta-S
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Ki-value below 0.08 mM, pH 8.3, temperature not specified in the publication
0.4
AMP
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pH 8.3, temperature not specified in the publication
0.005
Cibacron blue
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pH 8.3, temperature not specified in the publication
0.16
diphosphate
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pH 8.3, temperature not specified in the publication
1.7
pyridoxal 5'-phosphate
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pH 8.3, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
dephosphorylation assay at
8.1
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broad optimum pH 7.8-8.4, 68% activity at pH 7.2
8.3
kinase assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
asay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
additional information
green tissues
Manually annotated by BRENDA team
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
48000
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2 * 48000, SDS-PAGE, gel filtration, pH 7.0-7.5; 4 * 48000, SDS-PAGE, gel filtration, pH 8.3
180000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homotetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
the enzyme contains a transit peptide cleavage site
side-chain modification
N-terminal acetylation of nucleus-encoded chloroplast proteins in the cytosol, e.g. of isozyme C4 chloroplast PPDK, is required for proper chloroplast characteristics, such as the stability and/or import competence of organellar precursor proteins
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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+)
partially purified
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partially purified, ammonium sulfate precipitation, dye ligand chromatography (Blue-Sepharose, agarose-blue dextran), gel filtration
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partially purified, ammonium sulfate precipitation, dye-ligand chromatography (Blue Sepharose), gel filtration, anion exchange chromatography
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recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) RIL by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tagged and GFP-fusion proteins expressed in Escherichia coli BL21(DE3)
His-tagged protein expressed in Escherichia coli NM522
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recombinant overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) RIL
recombinant overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) RIL
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G525A
site-directed mutagenesis of a C4PPDK phosphorylation site
G525P
site-directed mutagenesis of a C4PPDK phosphorylation site
H529A
site-directed mutagenesis of a C4PPDK phosphorylation site
S506A
site-directed mutagenesis of a C4PPDK phosphorylation site
S528A
site-directed mutagenesis of a C4PPDK phosphorylation site
S528C
site-directed mutagenesis of a C4PPDK phosphorylation site
S528D
site-directed mutagenesis of a C4PPDK phosphorylation site
S528T
site-directed mutagenesis of a C4PPDK phosphorylation site
S528Y
site-directed mutagenesis of a C4PPDK phosphorylation site
T309A
site-directed mutagenesis of a C4PPDK phosphorylation site
T527A
site-directed mutagenesis of a C4PPDK phosphorylation site
T527D
site-directed mutagenesis of a C4PPDK phosphorylation site
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