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
2.7.4.27
-
RECOMMENDED NAME
GeneOntology No.
[pyruvate, phosphate dikinase]-phosphate phosphotransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AtRP1
O49562
-
bifunctional regulatory protein of pyruvate,orthophosphate dikinase
-
-
PDRP1
-
-
gene name
-
PPDK regulatory protein
-
-
PPDK regulatory protein
-
bifunctional serine/threonine kinase-phosphatase
pyruvate, orthophosphate dikinase regulatory protein
-
-
pyruvate, orthophosphate dikinase regulatory protein 1
O49562
bifunctional protein kinase/protein phosphatase
pyruvate,orthophosphate dikinase regulatory protein
-
-
pyruvate,Pi dikinase regulatory protein
-
-
pyruvate,Pi dikinase regulatory protein
-
bifunctional, catalyses phosphorylation and dephosphorylation of pyruvate,Pi dikinase
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
cv. Dekalb XL81
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[pyruvate, phosphate dikinase]phosphate + phosphate
pyruvate, phosphate dikinase + diphosphate
show the reaction diagram
-, O49562
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
show the reaction diagram
-
Thr residue phosphorylated (inactive)
active
-
?
[pyruvate, phosphate dikinase]phosphate + phosphate
pyruvate, phosphate dikinase + diphosphate
show the reaction diagram
-
Thr456 and His458 phosphorylated (inactive)
His458 phosphorylated (active)
-
?
[pyruvate,phosphate dikinase]phosphate + phosphate
pyruvate,phosphate dikinase + diphosphate
show the reaction diagram
-
His458 and Thr456 phosphorylated (inactive)
His458 phosphorylated (active)
-
?
[pyruvate,phosphate dikinase]phosphate + phosphate
pyruvate,phosphate dikinase + diphosphate
show the reaction diagram
-
Thr residue phosphorylated (inactive)
active
-
ir
[pyruvate,phosphate dikinase]phosphate + phosphate
pyruvate,phosphate dikinase + diphosphate
show the reaction diagram
-
Thr456 phosphorylated (inactive)
active
-
?
[pyruvate,Pi dikinase]phosphate + phosphate
pyruvate,Pi dikinase + diphosphate
show the reaction diagram
-
a His residue and a Thr residue phosphorylated (inactive)
one His residue phosphorylated (active)
-
?
[pyruvate,Pi dikinase]phosphate + phosphate
pyruvate,Pi dikinase + diphosphate
show the reaction diagram
-
phosphorylated at a Thr residue, inactive, additionally catalytically phosphorylated substrate (at His residue) is a much poorer substrate
active
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-nitro-5-thiocyanatobenzoate
-
-
ADP
-
competitive to substrate [pyruvate,Pi dikinase]phosphate (phosphorylated at a Thr residue)
ADP-beta-S
-
competitive to substrate [pyruvate,Pi dikinase]phosphate (phosphorylated at a Thr residue)
AMP
-
competitive to phosphate
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)
Phenylglyoxal
-
-
pyridoxal 5'-phosphate
-
-
pyruvate,Pi dikinase phosphorylated at a His residue
-
competitive to substrate [pyruvate,Pi dikinase]phosphate (phosphorylated at a Thr residue)
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.65
-
phosphate
-
pH 8.3, temperature not specified in the publication
0.67
-
phosphate
-
pH 8.3., 30°C
0.0007
-
[pyruvate,Pi dikinase]phosphate
-
phosphorylated at a Thr residue, pH 8.3, temperature not specified in the publication
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.085
-
ADP
-
pH 8.3, temperature not specified in the publication
0.08
-
ADP-beta-S
-
Ki-value below 0.08 mM, pH 8.3, temperature not specified in the publication
0.4
-
AMP
-
pH 8.3, temperature not specified in the publication
0.005
-
Cibacron blue
-
pH 8.3, temperature not specified in the publication
0.16
-
diphosphate
-
pH 8.3, temperature not specified in the publication
1.7
-
pyridoxal 5'-phosphate
-
pH 8.3, 30°C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.1
-
-
broad optimum pH 7.8-8.4, 68% activity at pH 7.2
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
O49562
green tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
mesophyll-chloroplast stroma
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
90000
-
-
gel filtration, pH 7.0-7.5
90000
-
-
pH 7.5, gel filtration
180000
-
-
gel filtration, pH 8.3
180000
-
-
pH 8.3, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 40000, SDS-PAGE
?
-
x * 45000, SDS-PAGE
homodimer
-
2 * 48000, SDS-PAGE, gel filtration, pH 7.0-7.5
homodimer
-
90000 at pH 7.5
homotetramer
-
4 * 48000, SDS-PAGE, gel filtration, pH 8.3
homotetramer
-
180000 at pH 8.3
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stabilized at 25°C by phosphate, ATP, Blue Dextran and Cibacron blue
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
immobilized metal ion affinity chromatography (Ni2+)
O49562
ammonium sulfate precipitation, dye ligand chromatography (agarose-Blue Dextran), gel filtration
-
immobilized metal ion affinity chromatography (Ni2+)
-
partially purified
-
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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
His-tagged and GFP-fusion proteins expressed in Escherichia coli BL21(DE3)
O49562
His-tagged protein expressed in Escherichia coli NM522
-