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

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The expected taxonomic range for this enzyme is: Magnoliophyta

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
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
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Manually annotated by BRENDA team
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,Pi dikinase]phosphate + phosphate
pyruvate,Pi dikinase + diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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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
8.1
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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
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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
180000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homotetramer
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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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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