Information on EC 2.7.9.1 - pyruvate, phosphate dikinase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
2.7.9.1
-
RECOMMENDED NAME
GeneOntology No.
pyruvate, phosphate dikinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
sequential mechanism for the addition of ATP and phosphate and a ping-pong mechanism for the addition of pyruvate and release of phosphoenolpyruvate
Arundinaria sp., Zea mays
-
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
mechanism
Arundinaria sp.
-
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
mechanism
Entamoeba histolytica, Gluconacetobacter xylinus
-
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
mechanism
-
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
mechanism
-
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
non-classical three-site tri ping-pong kinetics
-
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
non-classical three-site tri ping-pong kinetics
-
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
contains several structural domains. The catalytic histidine, the pyruvate binding site and the ATP binding site are located in different domains >#4# two-step bi bi uni uni mechanism <20>
-
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
increased activity results in an alternative gluconeogenic pathway
-
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
phospho group transfer
-
-
PATHWAY
KEGG Link
MetaCyc Link
C4 photosynthetic carbon assimilation cycle, NAD-ME type
-
C4 photosynthetic carbon assimilation cycle, NADP-ME type
-
C4 photosynthetic carbon assimilation cycle, PEPCK type
-
Carbon fixation in photosynthetic organisms
-
Carbon fixation pathways in prokaryotes
-
glutamine biosynthesis III
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Pyruvate metabolism
-
SYSTEMATIC NAME
IUBMB Comments
ATP:pyruvate, phosphate phosphotransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ATP:pyruvate, orthophosphate phosphotransferase
-
-
C4-PPDK
-
-
OsPPDKB
-
-
PPDK
-
-
-
-
PPDK
-
-
PPDK
Q2LIW1, Q2LIW2
-
PPDK
Q70WQ6
-
pyrophosphate-dependent pyruvate phosphate dikinase
-
-
pyruvate orthophosphate dikinase
-
-
pyruvate orthophosphate dikinase
-
-
pyruvate orthophosphate dikinase
P11155
-
pyruvate P1 dikinase
P11155
-
pyruvate phoshate dikinase
Q2LIW1, Q2LIW2
-
pyruvate phoshate dikinase
A2GU49
-
pyruvate phoshate dikinase
-
-
pyruvate phosphate dikinase
-
-
pyruvate phosphate dikinase
-
-
pyruvate phosphate dikinase
-
-
pyruvate phosphate dikinase
P37213
-
pyruvate phosphate dikinase
-
-
pyruvate phosphate dikinase
-
-
pyruvate phosphate dikinase
-
-
pyruvate Pi dikinase
-
-
pyruvate, orthophosphate dikinase
-
-
-
-
pyruvate, orthophosphate dikinase
-
-
pyruvate, orthophosphate dikinase
-
-
pyruvate, orthophosphate dikinase
-
-
pyruvate, phoshphate dikinase
Q70WQ6
-
pyruvate, Pi dikinase
-
-
-
-
pyruvate-inorganic phosphate dikinase
-
-
-
-
pyruvate-orthophosphate dikinase
-
-
pyruvate-phosphate dikinase
-
-
-
-
pyruvate-phosphate dikinase (phosphorylating)
-
-
-
-
pyruvate-phosphate ligase
-
-
-
-
pyruvate-Pi-dikinase
-
-
pyruvic-phosphate dikinase
-
-
-
-
pyruvic-phosphate ligase
-
-
-
-
ZnPPDK
-
-
CAS REGISTRY NUMBER
COMMENTARY
9027-40-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Arundinaria sp.
-
-
-
Manually annotated by BRENDA team
anendosymbiont, Wolbachia sp. subsp. Brugia malayi
-
-
Manually annotated by BRENDA team
Crithidia sp.
-
-
-
Manually annotated by BRENDA team
barnyard grass
-
-
Manually annotated by BRENDA team
recombinant enzyme expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
from isolate C2 derived from a patient in Southwest China
Uniprot
Manually annotated by BRENDA team
Gluconacetobacter xylinus
-
-
-
Manually annotated by BRENDA team
Kalanchoe hildebrandtii
-
-
-
Manually annotated by BRENDA team
Euryarchaea, Archaeabacteria
SwissProt
Manually annotated by BRENDA team
subsp. aerata
-
-
Manually annotated by BRENDA team
a bioenergy feedstock grass
-
-
Manually annotated by BRENDA team
Nopalxochia ackermannii
-
-
-
Manually annotated by BRENDA team
japonica variety Kitake of rice
-
-
Manually annotated by BRENDA team
rice
-
-
Manually annotated by BRENDA team
Crenarchaea, Archaeabacteria
SwissProt
Manually annotated by BRENDA team
strain S-1
-
-
Manually annotated by BRENDA team
Rhodospirillum rubrum S-1
strain S-1
-
-
Manually annotated by BRENDA team
Sedum prealtum
-
-
-
Manually annotated by BRENDA team
fragment 1; amitochondriate oxymonad, isolated from the hindgut of damp-wood termites
SwissProt
Manually annotated by BRENDA team
fragment 2; amitochondriate oxymonad, isolated from the hindgut of damp-wood termites
SwissProt
Manually annotated by BRENDA team
the entire gene consists of 2748 bp, GC content of 52.6%, protein of 915 amino acids corresponding to a theoretical molecular mass of 102.3 kDa, sequence signatures compared to other PPDK genes; hyperthermophilic crenarchaeote, Archaeabacteria, mass culture of Thermoproteus strain DSM 2078
SwissProt
Manually annotated by BRENDA team
fragment; parabasalia, isolated from hindgut of damp-wood termites
SwissProt
Manually annotated by BRENDA team
cv. Lerma Rojo
-
-
Manually annotated by BRENDA team
inbred line F2
SwissProt
Manually annotated by BRENDA team
L., var. Golden Cross Bantam T51
-
-
Manually annotated by BRENDA team
maize
-
-
Manually annotated by BRENDA team
recombinant enzyme expressed in Escherichia coli with a His-tag
SwissProt
Manually annotated by BRENDA team
var. Dekalb XL 81
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
the enzyme plays a controlling role in the phosphoenolpyruvate-regeneration phase of the C4 photosynthetic pathway
physiological function
-
C4-PPDK expression in rice promotes nitrogen absorption from the soil. In addition, the photosynthesis rate of some transgenic IR64 lines is also increased in the greenhouse
physiological function
-
enzyme overexpression during senescence can significantly accelerate nitrogen remobilization from leaves, and thereby increase rosette growth rate and the weight and nitrogen content of seeds
physiological function
-
Nicotiana tabacum lines harboring the enzyme construct are more tolerant to aluminium stress (treatment with 0.1 mM AlCl3 for 10 days). The overexpression of the enzyme can serve to protect roots against aluminium toxicity
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2',3'-dideoxyadenosine 5'-triphosphate + pyruvate + phosphate
?
show the reaction diagram
-
-
-
-
r
2'-dATP + pyruvate + phosphate
?
show the reaction diagram
-
-
-
-
r
3'-dATP + pyruvate + phosphate
?
show the reaction diagram
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
P11155
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
synthesis of ATP is not thermodynamically favorable in trophozoites of Entamoeba histolytica
-
-
?
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
the enzyme likely works in the direction of pyruvate production. PPDK is a central enzyme in the metabolism of glycosome by providing a link between glycolysis fatty acid oxidation and biosynthetic diphosphate-producing pathways. PPDK seems to replace diphosphatase in its classical thermodynamic role of displacing the equilibrium of diphosphate-producing reactions, as well as in its role of eliminating the toxic diphosphate
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
ordered steady-state mechanism, uni uni bi bi ping-pong mechanismsequential kinetic mechanism between AMP and pyrophosphate, phosphate is released before ATP
-
-
?
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
the Opaque-2 gene has regulatory function in metabolic pathways, mutation of Opaque-2 affects PPDK activity, overview
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
diphosphate released by DNA polymerase is converted to ATP by pyruvate phosphate dikinase, PPDK
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
PPDK catalyzes the reversible conversion of phosphoenolpyruvate, AMP, and phosphate to pyruvate and ATP, phosphoryl group transfer between PEP and His455, structure and mechanism, overview
-
-
r
ATP + PPDK central domain construct of residues 381-512 (Cent-I) + phosphate
?
show the reaction diagram
P22983
-
-
-
?
ATP + PPDK N-terminal domain construct of residues 1-340 (Tem-340) + phosphate
?
show the reaction diagram
P22983
-
-
-
?
ATP + PPDK N-terminal domain construct of residues 1-553 (Tem340-Cent-I) + phosphate
?
show the reaction diagram
P22983
-
-
-
?
ATP + pyruvate + arsenate
?
show the reaction diagram
Zea mays, Arundinaria sp.
-
-
-
-
ir
ATP + pyruvate + arsenate
?
show the reaction diagram
Gluconacetobacter xylinus
-
the rate of phosphoenolpyruvate formation in the presence of arsenate is 65% lower than that obtained with phosphate
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
P11155
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-, Q27662
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
P37213
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
Gluconacetobacter xylinus
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
Gluconacetobacter xylinus
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
P22983
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
Arundinaria sp.
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
Arundinaria sp.
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
Kalanchoe delagoensis, Sedum prealtum
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
P11155
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
P11155
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
the enzyme is strictly and reversibly regulated by light
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
activity with UTP, GTP and CTP is 1-3% of the activity with ATP
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
HPO42- is the substrate
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
Gluconacetobacter xylinus
-
GTP, CTP, ITP or TTP cannot replace ATP in the reaction with pyruvate
GDP, CMP and ADP cannot replace AMP in the reverse reaction
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
specificity is strictly restricted to adenine nucleotides
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
specificity is strictly restricted to adenine nucleotides
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
specificity is strictly restricted to adenine nucleotides
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
specificity is strictly restricted to adenine nucleotides
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
dAMP can replace ATP but with 20% of the activity
-
-
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
activity strictly and reversibly regulated by light
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
Kalanchoe delagoensis, Sedum prealtum
-
permits the incorporation of pyruvate into carbohydrates in the light in Crassulacean acid metabolism
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
the enzyme enables the organism to conserve the energy residing in the diphosphate resulting from protein and glycogen synthesis
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
Gluconacetobacter xylinus
-
enzyme activity has implication in the regulation of gluconeogenesis and carbohydrate oxidation
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
C4 acid cycle enzyme
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
loses activity below about 12C by dissociation of the tetramer, considered as one possible cause of the reduction of the photosynthetic rate of maize at low temperatures
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
P11155
rate-limiting enzyme of C4 acid cycle
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
P11155
C4 photosynthesis, late-stage accumulation of PPDK supports involvement in the starch-protein balance through restriction of ADP-glucose synthesis in dependence of diphosphate, role by influencing the balance of alanine-aromatic amino acid synthesis
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
Q70WQ6, -
bidirectional activity, preference for catabolic reaction, DELTA G +9.9 kJ/mole
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
different substrate concentrations for PPDK inhibition assay, pyruvate (40, 80, 160, 320, 480, and 720 micromol), ATP (20, 40, 60, 120, 240, and 480 micromol), and phosphate (0.3, 0.6, 1.2, 1.8, 2.7, and 4.32 mM)
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-, Q27662
PPDK catalyzes the generation of five ATP molecules from pyruvate by pyrophosphate-dependent glycolysis and offers a potential selective advantage
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
P37213
active site residues are Lys21, Arg91, Asp323, Glu325 and Gln337
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
Rhodospirillum rubrum S-1
-
-
-
-
additional information
?
-
-
involved in C4 dicarboxylic acid pathway in plant
-
-
-
additional information
?
-
-
functions in glycolytic pathway
-
-
-
additional information
?
-
-
the cytosolic PPDK functions in rice to modulate carbon metabolism during grain filling
-
-
-
additional information
?
-
P22983
central domain transports phosphoryl-groups between two distant catalytic sites located on the N-terminal and C-terminal sites, description of ability to catalyze the ATP/phosphate partial reaction by central domain and N-terminal domain of PPDK as independent recombinant proteins
-
-
-
additional information
?
-
Q2LIW1, Q2LIW2, -
diphosphate-dependent glycolysis
-
-
-
additional information
?
-
A2GU49, -
diphosphate-dependent glycolysis
-
-
-
additional information
?
-
Q2LIW1, Q2LIW2, -
diphosphate-dependent glycolysis, pyruvate kinase (PK) replaced by pyrophosphate-dependent pyruvate phosphate dikinase (PPDK)
-
-
-
additional information
?
-
A2GU49, -
diphosphate-dependent glycolysis, pyruvate kinase (PK) replaced by pyrophosphate-dependent pyruvate phosphate dikinase (PPDK)
-
-
-
additional information
?
-
-
differing functions of PPDK in C4 versus C3 plants, C4 PPDK regulatory proteins are involved in regulation of PPDK, mechanism, overview
-
-
-
additional information
?
-
-
differing functions of PPDK in C4 versus C3 plants, PPDK activity in C3 chloroplasts is light-regulated via reversible phosphorylation of an active-site Thr residue by the C3 PPDK regulatory proteins, most unusual bifunctional protein kinase /protein phosphatase, mechanism, overview. AtRP1 is chloroplast-targeted in predominant in greening and green tissues and organs, while AtRP2 is cytosol-localized mainly in seeds and pollen, overview
-
-
-
additional information
?
-
P37213
Entamoeba histolytica lacks Krebs cycle and oxidative phosphorylation enzymes, and adopts the exclusive way of ATP synthesis through glycolytic pathway. PPDK is the key enzyme essential for the glycolytic pathway in most common and perilous parasite Entamoeba histolytica
-
-
-
additional information
?
-
P11155
specific late-stage accumulation of the pyruvate orthophosphate dikinase, it plays a critical rolein the starch-protein balance through inorganic pyrophosphate-dependent restriction of ADP-glucose synthesis in addition to its usually reported influence on the alanine-aromatic amino acid synthesis balance, overview
-
-
-
additional information
?
-
-
the filarial parasite Brugia malayi lacks pyruvate kinase and instead utilizes the enzyme pyruvate phosphate dikinase, PPDK. The reversible reaction catalyzed by PPDK occurs in three steps, where the outcome depends on the organism glycolysis and ATP formation, or PEP synthesis
-
-
-
additional information
?
-
-
swiveling domain mechanism in pyruvate phosphate dikinase, upon detachment from the His domain, the two nucleotide-binding subdomains undergo a hinge motion that opens the active-site cleft, the nucleotide-binding domain undergoes a conformational transition upon binding of Mg2+, ATP, and phosphate, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
P11155
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
synthesis of ATP is not thermodynamically favorable in trophozoites of Entamoeba histolytica
-
-
?
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
the enzyme likely works in the direction of pyruvate production. PPDK is a central enzyme in the metabolism of glycosome by providing a link between glycolysis fatty acid oxidation and biosynthetic diphosphate-producing pathways. PPDK seems to replace diphosphatase in its classical thermodynamic role of displacing the equilibrium of diphosphate-producing reactions, as well as in its role of eliminating the toxic diphosphate
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
-
the Opaque-2 gene has regulatory function in metabolic pathways, mutation of Opaque-2 affects PPDK activity, overview
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
P37213
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
activity strictly and reversibly regulated by light
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
Kalanchoe delagoensis, Sedum prealtum
-
permits the incorporation of pyruvate into carbohydrates in the light in Crassulacean acid metabolism
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
the enzyme enables the organism to conserve the energy residing in the diphosphate resulting from protein and glycogen synthesis
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
Gluconacetobacter xylinus
-
enzyme activity has implication in the regulation of gluconeogenesis and carbohydrate oxidation
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
C4 acid cycle enzyme
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-
loses activity below about 12C by dissociation of the tetramer, considered as one possible cause of the reduction of the photosynthetic rate of maize at low temperatures
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
P11155
rate-limiting enzyme of C4 acid cycle
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
P11155
C4 photosynthesis, late-stage accumulation of PPDK supports involvement in the starch-protein balance through restriction of ADP-glucose synthesis in dependence of diphosphate, role by influencing the balance of alanine-aromatic amino acid synthesis
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
-, Q27662
PPDK catalyzes the generation of five ATP molecules from pyruvate by pyrophosphate-dependent glycolysis and offers a potential selective advantage
-
-
?
additional information
?
-
-
involved in C4 dicarboxylic acid pathway in plant
-
-
-
additional information
?
-
-
functions in glycolytic pathway
-
-
-
additional information
?
-
-
the cytosolic PPDK functions in rice to modulate carbon metabolism during grain filling
-
-
-
additional information
?
-
P22983
central domain transports phosphoryl-groups between two distant catalytic sites located on the N-terminal and C-terminal sites, description of ability to catalyze the ATP/phosphate partial reaction by central domain and N-terminal domain of PPDK as independent recombinant proteins
-
-
-
additional information
?
-
Q2LIW1, Q2LIW2, -
diphosphate-dependent glycolysis
-
-
-
additional information
?
-
A2GU49, -
diphosphate-dependent glycolysis
-
-
-
additional information
?
-
-
differing functions of PPDK in C4 versus C3 plants, C4 PPDK regulatory proteins are involved in regulation of PPDK, mechanism, overview
-
-
-
additional information
?
-
-
differing functions of PPDK in C4 versus C3 plants, PPDK activity in C3 chloroplasts is light-regulated via reversible phosphorylation of an active-site Thr residue by the C3 PPDK regulatory proteins, most unusual bifunctional protein kinase /protein phosphatase, mechanism, overview. AtRP1 is chloroplast-targeted in predominant in greening and green tissues and organs, while AtRP2 is cytosol-localized mainly in seeds and pollen, overview
-
-
-
additional information
?
-
P37213
Entamoeba histolytica lacks Krebs cycle and oxidative phosphorylation enzymes, and adopts the exclusive way of ATP synthesis through glycolytic pathway. PPDK is the key enzyme essential for the glycolytic pathway in most common and perilous parasite Entamoeba histolytica
-
-
-
additional information
?
-
P11155
specific late-stage accumulation of the pyruvate orthophosphate dikinase, it plays a critical rolein the starch-protein balance through inorganic pyrophosphate-dependent restriction of ADP-glucose synthesis in addition to its usually reported influence on the alanine-aromatic amino acid synthesis balance, overview
-
-
-
additional information
?
-
-
the filarial parasite Brugia malayi lacks pyruvate kinase and instead utilizes the enzyme pyruvate phosphate dikinase, PPDK. The reversible reaction catalyzed by PPDK occurs in three steps, where the outcome depends on the organism glycolysis and ATP formation, or PEP synthesis
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
AMP
-
reverse reaction
AMP
P37213
reverse reaction
AMP
-
forward reaction
AMP
-
forward reaction
AMP
-
reverse reaction
AMP
-
forward reaction
AMP
-
forward reaction
ATP
-
forward reaction
ATP
P37213
forward reaction
ATP
-
reverse reaction
ATP
-
reverse reaction
ATP
-
forward reaction
ATP
-
reverse reaction
ATP
-
reverse reaction
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
1 mM of this ion promotes pyruvate formation
K+
-
half-maximal activity with 20 mM potassium chloride at pH 6.8
K+
-
more than 20fold activation pH 7.4 and at pH 8.1
K+
O76283, -
not required for activity
K+
-
slight activation
Mg2+
-
1 mM of this ion promotes reaction in both directions
Mg2+
-
free Mg2+ is required to stabilize the oligomeric structure of the enzyme
Mg2+
Gluconacetobacter xylinus
-
-
Mg2+
-
free Mg2+ is required to stabilize the oligomeric structure of the enzyme
Mg2+
-
cannot be replaced by other divalent ions
Mg2+
O76283, -
required for activity
Mg2+
-
necessary for activity. Optimal concentration of 4.5 mM
Mg2+
-
activity increases with increasing Mg2+ concentrations, reaching a plateau at 2-4 mM. At higher concentrations the effect begins to reverse
Mg2+
-
binds together with phosphate and ATP to the active site located at the concave surface of the N-terminal domain
Mg2+
Q70WQ6, -
-
Mg2+
-
the enzyme requires Mg2+ for oligomerization
Mn2+
-
1 mM of this ion promotes pyruvate formation
Mn2+
-
free Mn2+ can replace free Mg2+
Mn2+
Gluconacetobacter xylinus
-
cannot replace Mg2+ in either the forward or the reverse reaction
Mn2+
-
not activation
Na+
-
slight activation of the phosphoenol pyruvate formation
NH4+
-
-
NH4+
-
at saturated concentration of NH4Cl pyruvate formation activity is increased 20fold
NH4+
-
more than 20fold activation at pH 7.4 and at pH 8.1
NH4+
-
required for enolization of pyruvate during the reaction
NH4+
O76283, -
not required for activity
NH4+
-
the enzyme requires NH4+ as a cofactor for optimal catalysis
Ni2+
-
1 mM of this ion promotes pyruvate formation
Rb+
-
25% of the activity relative to NH4+
Tl+
-
94% of the activity relative to NH4+
additional information
Q70WQ6, -
not depending on monovalent cations such as K+, Na+, NH4+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1-benzenesulfonyl-pyrrolidin-2-yl)-(3,5-dimethyl-4-p-tolylsulfanyl-pyrazol-1-yl)-methanone
P37213
-
(7-benzyl-3-methyl-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-ylsulfanyl)-acetic acid benzyl ester
P37213
-
2-(1-benzyl-1H-benzoimidazol-2-ylmethylsulfanyl)-3H-quinazolin-4-one
P37213
-
2-(1H-Benzoimidazol-2-ylsulfanyl)-N-(5-phenyl-[1,3,4]thiadiazol-2-yl)-acetamide
P37213
-
2-(1H-benzoimidazol-2-ylsulfanyl)-N-[4-(pyridin-2-ylsulfamoyl)-phenyl]-acetamide
P37213
-
2-(9-allyl-9H-1,3,4,9-tetraaza-fluoren-2-ylsulfanyl)-N-(5-methyl-isoxazol-3-yl)-butyramide
P37213
-
2-(9-benzyl-9H-1,3,4,9-tetraaza-fluoren-2-ylsulfanyl)-N-furan-2-ylmethyl-acetamide
P37213
-
2-benzylsulfanyl-N-[5-(3,4-dichloro-benzyl)-[1,3,4]thiadiazol-2-yl]-acetamide
P37213
-
2-Bromobutyrate
-
80% inhibition at 1 mM
2-Bromopropionate
-
74% inhibition at 1 mM
2-[2-(1-benzyl-1H-benzoimidazol-2-ylsulfanylmethyl)-benzoimidazol-1-yl]-acetamide
P37213
-
3-(2,6-dichloro-phenyl)-5-methyl-isoxazole-4-carboxylic acid 4-(6-amino-5-cyano-3-methyl-1,4-dihydro-pyrano[2,3-c]pyrazol-4-yl)-phenyl ester
P37213
-
3-Bromopropionate
-
66% inhibition at 1 mM
4-chloro-N-[2-(1-phenyl-1H-tetrazol-5-ylsulfanyl)-acenaphthen-1-yl]-benzenesulfonamide
P37213
-
4-[4-hydroxy-5-oxo-2-(3-phenoxy-phenyl)-1-pyridin-3-ylmethyl-2,5-dihydro-1H-pyrrole-3-carbonyl]-N,N-dimethyl-benzenesulfonamide
P37213
-
5'-adenylimidodiphosphate
-
-
5,5-dithiobis(2-nitrobenzoic acid)
-
-
5,5-dithiobis(2-nitrobenzoic acid)
-
-
5-benzyl-2-(4-chloro-phenyl)-3-(4-fluoro-phenyl)-tetrahydro-pyrrolo[3,4-d]isoxazole-4,6-dione
P37213
-
5-phenyl-2-[2-([1,2,4]triazolo[4,3-a]pyridin-3-ylsulfanyl)-acetylamino]-thiophene-3-carboxylic acid ethyl ester
P37213
-
6-(4-benzyl-5-phenyl-4H-[1,2,4]triazol-3-ylsulfanylmethyl)-N-phenyl-[1,3,5]triazine-2,4-diamine
P37213
-
6-[5-(2-chloro-phenyl)-4-phenyl-4H-[1,2,4]triazol-3-ylsulfanylmethyl]-N-phenyl-[1,3,5] triazine-2,4-diamine
P37213
-
adenosine 5'-mono-O-phosphorothiolate
-
-
ADP
Arundinaria sp., Zea mays
-
mediates a rapid but reversible inactivation in presence of a thiol
ADP
-
no inhibition up to 0.46 mM
AMP
Gluconacetobacter xylinus
-
phosphoenolpyruvate formation, competitive to ATP
AMP
Arundinaria sp., Zea mays
-
-
AMP
-
non competitive with respect to ATP
AMP
-
competitive with respect to ATP
ATP
Gluconacetobacter xylinus
-
pyruvate formation, competitive to AMP
ATP
-
competitive to AMP
ATP
-
product inhibition versus phosphoenolpyruvate is noncompetitive
ATP
Q70WQ6, -
concentration 1 mM, 55C, AMP-competitive inhibition as deduced from AMP saturation kinetics by using various ATP concentration ranging between 50-200 micromol
biphosphonate
-
mixed inhibition mechanism with respect to diphosphate
Bromoacetate
-
83% inhibition at 1 mM
Bromopyruvate
-
competitive to phosphoenolpyruvate
Bromopyruvate
-
irreversible inactivation
Co2+
-
at high concentration inhibits the phosphoenolpyruvate, pyruvate exchange reaction
CTP
-
total inhibition of the forward reaction at 1 mM
D-glucose 1-phosphate
Q70WQ6, -
72% activity sustained, effector concentration 5 mM, 55C
dATP
-
40% inhibition at 1 mM
diethyldicarbonate
-
inactivates the enzyme by combination with histidyl residues, inhibition is reversed by hydroxylamine
diphosphate
-
competitive to phosphate
diphosphate
-
non competitive to phosphate
diphosphate
-
competitive inhibitor
gamma(p-Arsenophenyl)-n-butyrate
Arundinaria sp., Zea mays
-
-
GMP
-
noncompetitive to ATP
ilimaquinone
-
uncompetitive/mixed type versus pyruvate and versus ATP, 48% inhibition of C4 acid cycle evolution. IC50: 0.292 mM
ilimaquinone
-
selectively toxic to C4 plants, isolated from a marine sponge, heterocyclic compound, 3 rings, 2-D structure shown
Imidodiphosphate
-
competitive to diphosphate
iodoacetate
-
70% inhibition at 1 mM
ITP
-
total inhibition of the forward reaction at 1 mM
Methylene diphosphonate
-
competitive to diphosphate
MgHPO4
-
competitive to HPO42-
N-(3-cyano-4,5-diphenyl-furan-2-yl)-2-(1,3-dioxo-1,3-dihydro-isoindol-2-yl)-acetamide
P37213
-
N-(3-cyano-4,5-diphenyl-furan-2-yl)-4-(1,3-dioxo-1,3-dihydro-isoindol-2-yl)-butyramide
P37213
-
N-[5-(3-chloro-benzyl)-thiazol-2-yl]-3-[5-(2-methyl-cyclopropyl)-furan-2-yl]-propionamide
P37213
-
oxalate
-
competitive to pyruvate, oxalate binds to the phosphorylated form of the enzyme
oxalate
-
competitive to pyruvate
oxalate
-
mixed mechanism with respect to phosphoenolpyruvate and diphosphate
p-chloromercuribenzoate
Arundinaria sp., Zea mays
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
Gluconacetobacter xylinus
-
-
p-hydroxymercuribenzoate
-
-
phosphate
Arundinaria sp., Zea mays
-
-
phosphate
-
competitive to diphosphate
phosphate
-
inhibits rate of ATP synthesis at saturating and equimolar concentrations of phosphoenolpyruvate, AMP and diphosphate. Product inhibition versus phosphoenolpyruvate is uncompetitive
phosphoenolpyruvate
-
competitive to pyruvate
phosphoenolpyruvate
-
competitive to pyruvate
Phosphoglycolate
-
competitive to phosphoenolpyruvate
potassium fluoride
Gluconacetobacter xylinus
-
inhibits reaction in both directions at 50 mM
PPDK regulatory protein
-
RP catalyzes reversible phosphorylation on T456 by RP, inactive form phoshorylated at T456, ADP-dependent, a catalytic His-phophorylation precedes phosphorylation at T456, pyruvate (2 mM) can inhibit inactivation by RP
-
pyruvate
Arundinaria sp., Zea mays
-
-
pyruvate
-
competitive to phosphoenolpyruvate
Sulfhydryl agents
-
-
-
tetrasodium 1-hydroxyethylidene biphosphonate
-
-
tetrasodium 1-hydroxymethylidene biphosphonate
-
-
tetrasodium 1-hydroxynonane biphosphonate
-
-
UDP
Q70WQ6, -
55% activity of PPDK, effector concentration 5 mM, 55C
unguinol
-
from fungal isolate F3000054, a mixed noncompetitive inhibitor of PPDK with respect to the substrates pyruvate and ATP and an uncompetitive inhibitor of PPDK with respect to phosphate. Unguinol has deleterious effects on a model C4 plant but no effect on a model C3 plant, effects in vivo, overview; mixed noncompetitive inhibition of PPDK with respect to the substrates pyruvate and ATP, uncompetitive with respect to phosphate, phytotoxic effects (bleaching) on C4 plants, no effect on a model C3 plant (Hordeum vulgare)
[3-methyl-7-(3-methyl-benzyl)-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-ylsulfanyl]-acetic acid benzyl ester
P37213
-
Mn2+
-
at high concentration inhibits the phosphate, diphosphate exchange reaction
additional information
-
no tested 5'-nucleoside monophosphate inhibits the reaction with AMP
-
additional information
-
not inhibited by iodoacetamide
-
additional information
-
not inhibited by iodoacetamide
-
additional information
-
response of the enzyme to energy charge
-
additional information
P11155
rapid screening method to detect specific inhibitors of pyruvate phosphate dikinase. Organic extracts of about 6500 marine macroscopic organisms are tested for inhibition. Approximately 70% of the PPDK selective extracts are from sponges (phylum Porifera). The remaining 30% of active extracts that preferentially inhibit PPDK include ascidians, cnidarians, echinoderms, mollusks, and red algae, with 25% of these preferentially inhibiting PPDK
-
additional information
-
extracts from several fungal isolates selectively inhibit PPDK; for PPDK inhibition assay 5 and 10 micrograms per ml of unguinol tested in the presence of different substrate concentrations, whole-plant phytotoxicity test (C4, C3),antimicrobial assays and anti-tumor cell assays described for unguinol, 2-D structure shown for further potential candidates to inhibit PPDK that are analogues of unguinol as acarogobien A, acarogobien B and guisinol
-
additional information
-
ADP-dependent inactivation assay of purified PPDK by bacterially-expressed RP described (47% inhibition of PPDK after 10min in presence of 2 mM ADP at 25C), reversibility of RP activity by diphosphate-dependent reactivation assay described (1 mM diphosphate, at 25C), SDS-PAGE and Western-Blot for detection of T456P-PPDK and RP
-
additional information
P37213
in silico docking studies to pyruvate phosphate dikinase of Entamoeba histolytica, ID number, structure and IUPAC names of top scored ligands; ligand binding and docking analysis, overview
-
additional information
Q70WQ6, -
inhibition by UDP and D-glucose 1-phosphate at rather high and unphysiological concentrations, no inhibitory effects by alpha-ketoglutarate (1 mM), potassium phosphate (5 mM), glyceraldehyde 3-phosphate (5 mM), 3-phosphoglycerate (5 mM), dihydroxyacetone phosphate (5 mM)
-
additional information
-
PPDK inactivation and protein degradation by posttranslational regulation during progressive seed development in rice, most abundant inactive forms of PPDK in endosperm of mature seeds
-
additional information
-
phosphorylation of PPDK by AtRP1/2 is negated or greatly reduced when pyruvate is also included in the reaction mixture
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
abscisic acid
-
induces production of the protein
Polyethylene glycol
-
induces production of the protein
thiols
-
required for activity in solution
mannitol
-
induces production of the protein
additional information
-
root submergence, gradual drying, cold and high salt treatment induces production of the protein. Expression induced by low-oxygen stress and water deficiency
-
additional information
-
the protein kinase/phosphatase RP catalyzes reversibly phosphorylation of T456, active form dephosphorylated at T456, diphosphate-forming dephosphorylation mechanism, assay at 25C
-
additional information
-
like the native PPDK of maize the activity of the cold-tolerant recombinant enzyme construct is regulated by the PPDK regulatory protein RP
-
additional information
Q70WQ6, -
neither inhibition nor activation of anabolic PPDK activity observed, kinetics of catabolic pathway
-
additional information
-
the enzyme is light-activated
-
additional information
-
PPDK is light-activated, activation kinetics at different temperatures, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.28
-
2',3'-dideoxyadenosine 5'-triphosphate
-
pH 7, 25C
0.1
-
2'-dAMP
-
pH 6.8, 25C
0.35
-
2'-dATP
-
pH 7, 25C
0.25
-
3'-dATP
-
pH 7, 25C
0.0013
-
AMP
-
pH 7, 30C
0.0016
-
AMP
Gluconacetobacter xylinus
-
pH 6.5, 30C, pyruvate formation
0.002
-
AMP
-
pH 6.0, 37C
0.0035
-
AMP
-
pH 6.8, 25C, phosphoenolpyruvate formation
0.004
-
AMP
Arundinaria sp.
-
pH 6.8, 25C
0.005
-
AMP
-
less than 0.005 mM ,pH 6.3, 25C
0.005
-
AMP
-
pH 5.8-6.4 (optimal pH), 37C
0.006
-
AMP
-
pH 7.1, 30C, pyruvate formation
0.0075
-
AMP
O76283, -
-
0.009
-
AMP
-
pH 6.8, 25C, pyruvate-producing reaction, values for 7 mutant PPDK
0.015
-
AMP
-
pH 6.7, 25C
0.02
-
AMP
-
pH 7.0, 37C
0.02
-
AMP
Q70WQ6, -
55C
0.009
-
ATP
-
pH 8.3, 30C
0.015
-
ATP
-
pH 7.5, 22C, phosphoenolpyruvate formation
0.023
-
ATP
-
pH 8, 22C
0.032
-
ATP
-
pH 7, 30C
0.036
-
ATP
-
pH 8, 22C
0.042
-
ATP
-
pH 7.4, 25C, phosphoenolpyruvate formation
0.047
-
ATP
-
transgenic enzyme
0.049
-
ATP
-
transgenic enzyme
0.05
-
ATP
-
pH 6.7, 25C
0.05
-
ATP
-
transgenic enzyme
0.081
-
ATP
-
pH 7, 25C, E279A mutant, phosphoenolpyruvate-producing reaction
0.082
-
ATP
-
pH 8.1, 25C, phosphoenolpyruvate formation
0.088
-
ATP
-
-
0.09
-
ATP
-
pH 8.3
0.095
-
ATP
-
-
0.1
-
ATP
-
pH 6.8, 25C, pyruvate formation
0.19
-
ATP
-
pH 7, 25C, wild type and D280 mutant, phosphoenolpyruvate-producing reaction
0.2
-
ATP
-
pH 8, 30C, phosphoenolpyruvate formation
0.284
-
ATP
-
pH 6.0, 37C
0.4
-
ATP
Gluconacetobacter xylinus
-
pH 8.2, 30C, phosphoenolpyruvate formation
0.41
-
ATP
-
pH 7, 25C, R135A mutant, phosphoenolpyruvate-producing reaction
0.6
-
ATP
O76283, -
-
8
-
ATP
Q70WQ6, -
KM/S50-value, 70C
0.029
-
diphosphate
-
-
0.029
-
diphosphate
-
pH 7, 30C
0.04
-
diphosphate
Arundinaria sp., Zea mays
-
-
0.04
-
diphosphate
-
pH 7.5, 22C, pyruvate formation
0.047
-
diphosphate
-
pH 7.0, 37C
0.05
-
diphosphate
O76283, -
-
0.06
-
diphosphate
Gluconacetobacter xylinus
-
pH 6.5, 30C, pyruvate formation
0.062
-
diphosphate
-
pH 7.1, 30C, pyruvate formation
0.08
-
diphosphate
-
pH 6.7, 25C
0.08
-
diphosphate
Q70WQ6, -
55C
0.089
-
diphosphate
-
pH 6.8, 25C, pyruvate-producing reaction, values for 7 mutant PPDK
0.091
-
diphosphate
-
pH 6.0, 37C
0.1
-
diphosphate
-
pH 6.3, 25C
0.1
-
diphosphate
-
pH 5.8-6.4 (optimal pH), 37C
0.0014
-
phosphate
-
-
0.118
-
phosphate
-
-
0.134
-
phosphate
-
transgenic enzyme
0.138
-
phosphate
-
transgenic enzyme
0.256
-
phosphate
-
transgenic enzyme
0.34
-
phosphate
-
-
0.38
-
phosphate
-
pH 8.1, 25C, phosphoenolpyruvate formation
0.408
-
phosphate
-
-
0.43
-
phosphate
-
pH 8, 22C
0.5
-
phosphate
-
pH 8.3, 30C
0.5
-
phosphate
O76283, -
-
0.56
-
phosphate
-
pH 8.1, 25C, phosphoenolpyruvate formation
0.6
-
phosphate
-
pH 6.8, 25C, pyruvate formation
0.8
-
phosphate
Gluconacetobacter xylinus
-
pH 8.2, 30C, phosphoenolpyruvate formation
0.8
-
phosphate
-
pH 6.7, 25C
0.83
-
phosphate
-
pH 8, 30C, phosphoenolpyruvate formation
1.5
-
phosphate
-
pH 7.5, 22C, phosphoenolpyruvate formation
1.8
-
phosphate
-
pH 7, 30C
0.02
-
phosphoenolpyruvate
-
pH 5.8-6.4 (optimal pH), 37C
0.021
-
phosphoenolpyruvate
-
pH 6.3, 25C
0.024
-
phosphoenolpyruvate
-
-
0.024
-
phosphoenolpyruvate
-
pH 7.0, 37C
0.027
-
phosphoenolpyruvate
-
pH 6.8, 25C, pyruvate-producing reaction, values for 7 mutant PPDK
0.03
-
phosphoenolpyruvate
-
pH 6.0, 37C
0.033
-
phosphoenolpyruvate
-
pH 7, 30C
0.04
-
phosphoenolpyruvate
O76283, -
-
0.046
-
phosphoenolpyruvate
-
pH 7.4, 25C, pyruvate formation
0.1
-
phosphoenolpyruvate
Gluconacetobacter xylinus
-
pH 6.5, 30C, pyruvate formation
0.1
-
phosphoenolpyruvate
-
pH 6.7, 25C
0.13
-
phosphoenolpyruvate
-
pH 7.1, 30C, pyruvate formation
0.14
-
phosphoenolpyruvate
-
pH 7.5, 22C, pyruvate formation
0.16
-
phosphoenolpyruvate
-
pH 7.4, 25C, pyruvate formation
0.194
-
phosphoenolpyruvate
-
at pH 7.0 and 30C
0.5
-
phosphoenolpyruvate
Q70WQ6, -
55C
0.025
-
pyruvate
-
pH 8, 22C
0.027
-
pyruvate
-
pH 8, 30C, phosphoenolpyruvate formation
0.032
-
pyruvate
-
transgenic enzyme
0.059
-
pyruvate
-
transgenic enzyme
0.065
-
pyruvate
-
transgenic enzyme
0.067
-
pyruvate
-
-
0.068
-
pyruvate
-
pH 7.0, 37C
0.07
-
pyruvate
-
-
0.073
-
pyruvate
-
-
0.075
-
pyruvate
-
pH 7, 30C
0.08
-
pyruvate
-
pH 6.8, 25C, pyruvate formation
0.082
-
pyruvate
-
pH 8.1, 25C, phosphoenolpyruvate formation
0.092
-
pyruvate
-
pH 7.4, 25C, phosphoenolpyruvate formation
0.1
-
pyruvate
-
pH 6.7, 25C
0.11
-
pyruvate
Arundinaria sp., Zea mays
-
pH 8.3, 30C
0.158
-
pyruvate
-
-
0.178
-
pyruvate
-
at pH 7.0 and 30C
0.2
-
pyruvate
Gluconacetobacter xylinus
-
pH 8.2, 30C, phosphoenolpyruvate formation
0.25
-
pyruvate
-
pH 7.5, 22C, phosphoenolpyruvate formation
0.3
-
pyruvate
O76283, -
-
0.8
-
pyruvate
Q70WQ6, -
70C
305
-
pyruvate
-
pH 6.0, 37C
3.5
-
diphosphate
Q70WQ6, -
70C
additional information
-
additional information
-
-
-
additional information
-
additional information
Q70WQ6, -
reactions follow classical Michaelis Menten kinetics for pyruvate and phosphate, sigmoidal saturation curve observed with ATP, neither inhibition nor activation of the anabolic PPDK activity observed
-
additional information
-
additional information
-
single-turnover reaction kinetics, mutant R219E/E271R/S261D
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
53
-
phosphoenolpyruvate
-
pH 7.0, 37C
80
-
phosphoenolpyruvate
-
pH 5.8-6.4 (optimal pH)
87
-
phosphoenolpyruvate
-
pH 6.0, 37C
10
-
pyruvate
-
pH 6.0, 37C
15
-
pyruvate
-
pH 7.0, 37C
additional information
-
additional information
-
turnover reactions of ATP and phosphate using equal concentrations of central domain protein Cent-I (PPDK central domain construct of residues 381-512-I) and the N-terminal domain protein Tem-340 does not produce the expected products
-
additional information
-
additional information
Q70WQ6, -
assay overview, kinetics at 55C and 70C, anabolic and catabolic direction
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.07
-
5'-adenylimidodiphosphate
-
pH 6.8, 25C
0.32
-
adenosine
-
pH 6.8, 25C
0.31
-
adenosine 5'-mono-O-phosphorothiolate
-
pH 6.8, 25C
0.13
-
AMP
-
pH 8.1, 25C, phosphoenolpyruvate formation
0.2
-
AMP
Gluconacetobacter xylinus
-
pH 8.2, 30C, phosphoenolpyruvate formation
0.32
-
AMP
-
pH 8, 30C, phosphoenolpyruvate formation
0.036
-
ATP
-
pH 8, 22C
0.07
-
ATP
Q70WQ6, -
55C, AMP saturation kinetics with ATP concentration of 50-200 micromol
0.14
-
ATP
-
with phosphoenolpyruvate as varied substrate, Ki(slope)
0.22
-
ATP
Gluconacetobacter xylinus
-
pH 6.5, 30C, pyruvate formation
0.45
-
ATP
-
withAMP as varied substrate
0.6
-
ATP
-
pH 7.1, 30C, pyruvate formation
5.1
-
ATP
-
with diphosphate as varied substrate, Ki(slope)
15
-
ATP
-
with diphosphate as varied substrate, Ki(intercept)
17
-
ATP
-
with phosphoenolpyruvate as varied substrate, Ki(intercept)
0.32
-
diphosphate
-
pH 8.1, 25C, phosphoenolpyruvate formation
0.36
-
diphosphate
-
pH 8, 30C, phosphoenolpyruvate formation
0.55
-
diphosphate
-
pH 7, 30C
0.001
-
oxalate
-
pH 7, 30C, less than 0.001 mM
0.025
-
oxalate
-
pH 7.5, 25C
6
-
phosphate
-
pH 7.1, 30C, pyruvate formation
7.2
-
phosphate
-
with phosphoenolpyruvate as varied substrate
23
-
phosphate
-
with diphosphate as varied substrate, Ki(slope)
44
-
phosphate
-
with AMP as varied substrate, Ki(slope)
46
-
phosphate
-
with diphosphate as varied substrate, Ki(intercept)
88
-
phosphate
-
with AMP as varied substrate, Ki(intercept)
0.15
-
phosphoenolpyruvate
-
pH 8.1, 25C, phosphoenolpyruvate formation
2
-
phosphoenolpyruvate
-
pH 8, 30C, phosphoenolpyruvate formation
0.4
-
pyruvate
-
with diphosphate as varied substrate, Ki(intercept)
0.76
-
pyruvate
-
pH 7.1, 30C, pyruvate formation
2.3
-
pyruvate
-
with diphosphate as varied substrate, Ki(slope)
22.6
-
pyruvate
-
with AMP as varied substrate
1.2
-
tetrasodium 1-hydroxyethylidene biphosphonate
-
pH 6.3, 25C
11
-
tetrasodium 1-hydroxymethylidene biphosphonate
-
pH 6.3, 25C
4.3
-
tetrasodium 1-hydroxynonane biphosphonate
-
pH 6.3, 25C
8.7
-
GMP
-
pH 6.8, 25C
additional information
-
additional information
-
inhibition kinetics for unguinol on PPDK
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.29
-
ilimaquinone
-
-
0.292
-
ilimaquinone
-
uncompetitive/mixed type versus pyruvate and versus ATP, 48% inhibition of C4 acid cycle evolution. IC50: 0.292 mM
0.04
-
unguinol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.043
-
-
T456F mutant
0.067
-
-
inactive enzyme obtained from dark-grown plants
0.24
-
-
T456Y mutant
0.88
-
Gluconacetobacter xylinus
-
-
1.2
-
-
measured at 30C
2.5
-
O76283, -
catalysis of both the pyruvate and the phosphoenolpyruvate formation
2.91
-
-
after activation by phosphate of an enzyme obtained from dark-grown plants
4.1
-
-
-
4.5
-
-
-
12
-
-
recombinant enzyme
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
enzyme activity per g of fresh tissue
additional information
-
-
enzyme activity per g of fresh tissue; relationship between developmental stage and activity
additional information
-
-
-
additional information
-
-
activities measured using a firefly luciferase-luciferin reaction
additional information
-
-
specific activity of PPDK in plants transformed with the construct showing 17 amino acid substitutions inversely correlates with amount of enzyme in leaves, PPDK activity becomes constant when the amount is above 5 mg/g fresh weight, enzyme contents estimated by Western blot, spectrometric assay at 25C, two transformants retained 70% of activity after 180 min indicating a comparable cold-tolerance like Flaveria brownii plants, further effect of cold-tolerant PPDK on photosynthetic rate estimated by measurement of CO2 uptake at leaf temperatures of 30C, 20C, 13C, and 8C, increase by 23% at 8C shown, no effects at higher temperatures
additional information
-
Q70WQ6, -
the maximal specific activity of the catabolic reaction is approximately 2fold higher if compared to the anabolic reaction, indicated by lower Km-values for reaction compounds of the catabolic reaction, kinetics at 55C and 70C shown, neither inhibition nor activation of anabolic PPDK activity observed
additional information
-
-
activity and amounts of PPDK downregulated during seed development in rice, tissue-specificy, immunoblot analysis of different seed fractions of rice, SDS-PAGE, spectrophotometric assay of PPDK acitivity, kinetics
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.8
6.4
-
reaction with AMP, phosphoenolpyruvate and diphosphate
6
-
-
ATP formation
6.4
6.7
-
pyruvate formation
6.4
-
-
reverse reaction, pyruvate formation
6.5
7
-
both directions of reaction
6.5
7.5
-
phosphoenolpyruvate formation
6.5
-
Gluconacetobacter xylinus
-
pyruvate formation
6.8
7
-
assay at
6.8
-
-
activity assay
6.9
-
-
pyruvate formation
7
7.8
-
phosphoenolpyruvate formation
7
-
-
reaction with pyruvate, ATP and phosphate
7
-
-
the pyruvate-forming reaction is strongly favoured at pH 7.0
7.1
-
-
pyruvate formation
7.2
7.8
-
forward reaction, phosphoenolpyruvate formation
7.2
8
-
forward reaction, phosphoenolpyruvate formation
7.75
-
-
pyrosequencing by utilizing pyruvate phosphate dikinase, expressed onto bacterial magnetic particles, PPDK-BacMPs
8
-
-
phosphoenolpyruvate formation
8
-
-
assay at, at pH 7.5 and pH 7.0 without ADP and AMP the enzyme activity is 61% and 38% of the activity at pH 8 respectively
8
-
-
assay at
8.2
-
Gluconacetobacter xylinus
-
phosphoenolpyruvate formation
8.2
-
-
phosphoenolpyruvate formation
8.3
-
Arundinaria sp.
-
phosphoenolpyruvate formation
8.3
-
-
the competency of the enzyme in catalyzing its phosphoenolpyruvate-forming reaction at pH 7.0 is dramatically reduced, having only 6% of the rate at pH 8.3
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
9.5
-
pyruvate phosphate dikinase, expressed onto bacterial magnetic particles, PPDK-BacMPs, shows stable enzymatic activity
7
8.3
-
the competency of the enzyme in catalyzing its phosphoenolpyruvate-forming reaction at pH 7.0 is dramatically reduced, having only 6% of the rate at pH 8.3
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at
25
-
-
assay at
30
-
-
assay at
30
-
Gluconacetobacter xylinus
-
assay at
37
-
-
activity assay; pyrosequencing by utilizing pyruvate phosphate dikinase, expressed onto bacterial magnetic particles, PPDK-BacMPs
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
45
-
pyruvate phosphate dikinase, expressed onto bacterial magnetic particles, PPDK-BacMPs, shows stable enzymatic activity
additional information
-
-
cold tolerance of recombinant maize plants estimated, crude leaf extracts placed on ice to measure residual PPDK activities, PPDK extracted from untransformed maize looses 90% of its activity after 20 min, a retained PPDK activity 70% of after 180 min in two transformants corresponds to a cold-tolerance shown for Flaveria brownii plants
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.2
-
P11155
isoelectric focusing (pH range from 4 to 7), cytosolic CyPPDK 2
5.3
-
P11155
isoelectric focusing (pH range from 4 to 7), cytosolic CyPPDK 2
5.4
-
P11155
isoelectric focusing (pH range from 4 to 7), cytosolic CyPPDK 2
8.25
-
O76283, -
calculated
8.9
-
-
calculated
additional information
-
P11155
annotation of different isoforms of one of the two cytosolic isoforms of PPDK of maize
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
cytosolic mRNA of OsPPDKB is induced in the reproductive organs after pollination, and greatly increases until about 10 days after fertilization. This mRNA is localized mainly in the endosperm, aleurone, and scutellum of the developing kernel
Manually annotated by BRENDA team
-
cytosolic mRNA of OsPPDKB is induced in the reproductive organs after pollination, and greatly increases until about 10 days after fertilization. This mRNA is localized mainly in the endosperm, aleurone, and scutellum of the developing kernel
Manually annotated by BRENDA team
P11155
proteomic study of maize endosperm development, PPDK is important, overview; time course analysis of seven developmental stages of maize, 4-40 days after pollination, significant PPDK accumulation at 21 days after pollination
Manually annotated by BRENDA team
-
transcriptomic, proteomic and metabolic analysis of maize endosperm development, PPDK is important, overview
Manually annotated by BRENDA team
-
cytosolic mRNA of OsPPDKB is induced in the reproductive organs after pollination, and greatly increases until about 10 days after fertilization. This mRNA is localized mainly in the endosperm, aleurone, and scutellum of the developing kernel
Manually annotated by BRENDA team
Arundinaria sp.
-
-
Manually annotated by BRENDA team
-
dark-treated
Manually annotated by BRENDA team
-
; maize PPDK of leaves used for inhibitor studies
Manually annotated by BRENDA team
-
maize inbred line A188, recombinant cold tolerant PPDK protein, 3'-part of Flaveria brownii (Asteraceae) PPDK fused to maize PPDK, exon-intron boundaries unaffected, in one of the constructs 17 amino acid positions altered, amounts of recombinant PPDK estimated by western blot and densitometry calculated on the basis of leaf fresh weight, wide range among individual plants
Manually annotated by BRENDA team
-
the cytosolic isoform accumulates preferentially in the veins
Manually annotated by BRENDA team
-
cytosolic mRNA of OsPPDKB is induced in the reproductive organs after pollination, and greatly increases until about 10 days after fertilization. This mRNA is localized mainly in the endosperm, aleurone, and scutellum of the developing kernel
Manually annotated by BRENDA team
-
green immature seeds
Manually annotated by BRENDA team
-
variety Kitake of rice, early cellularization stages of syncitial-endosperm during seed development, separated analysis of pericarp, embryo and aleurone and seed embryo, regulatory phosphorylation of PPDK in the non-green seed embryo and in green outer pericarp layer, no regulatory phosphorylation of PPDK in the endosperm and aleurone layer, pool of inactive PPDK in mature seed most abundant, immunoblot analysis, PPDK assay, inhibition assay
Manually annotated by BRENDA team
additional information
-
optimization of plant culture conditions, the unusual C4 species shows high productivity in cold climates, high activity at 14C, while PPDK is the key limiting factor for C4 photosynthesis at low temperature in other plants, e.g. Zea mays, overview
Manually annotated by BRENDA team
additional information
-
enzyme activity at different climates, cold climates at 14C and warm climates at 25C, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Alluaudia procera, Crassula arborescens, Kalanchoe hildebrandtii, Lithops sp., Nopalxochia ackermannii, Sansevieria trifasciata
-
intracellular localization of PPDK investigated in 22 malic enzyme-crassulacean acid metabolism species
Manually annotated by BRENDA team
-
C4 chloroplasts
Manually annotated by BRENDA team
-
the chloroplastic form accumulates in both mesophyll and veinal cells
Manually annotated by BRENDA team
Alluaudia procera, Crassula arborescens, Kalanchoe hildebrandtii, Lithops sp., Nopalxochia ackermannii, Sansevieria trifasciata
-
intracellular localization of PPDK investigated in 22 malic enzyme-crassulacean acid metabolism species
Manually annotated by BRENDA team
-
cytosolic mRNA of OsPPDKB is induced in the reproductive organs after pollination, and greatly increases until about 10 days after fertilization
Manually annotated by BRENDA team
P11155
seven isoforms of cytosolic PPDK of maize identified by proteomics, distinguished by deduced molecular mass, isoelectric point and slight differences in primary peptide sequence, in silico prediction of subcellular destination
Manually annotated by BRENDA team
-
the cytosolic isoform accumulates preferentially in the veins
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
96300
-
-, Q39734
calculated
96600
-
-
calculated
99280
-
P11155
cytosolic CyPPDK 2
100000
-
-
antibody recognition
100000
-
O76283, -
antibody recognition
100000
-
-
calculated
102300
-
Q70WQ6, -
theoretical weight calculated from sequence
104900
-
P11155
cytosolic CyPPDK 2
105100
-
P11155
cytosolic CyPPDK 2
105700
-
P11155
cytosolic CyPPDK 2
150000
160000
-
equilibrium sedimentation and gel filtration
169300
-
-
sucrose density gradient sedimentation
170000
-
-
gel filtration
195000
-
-
gel filtration
198400
-
-
gel electrophoresis
246800
-
-
HPLC gel filtration
250000
-
Q70WQ6, -
native protein, gelfiltration
320000
-
-
gel filtration on Sephadex G-200
330000
-
-
gel filtration on Sephrose 6B
370000
-
-
gel filtration on Sepharose 6B
370000
-
-
gel filtration, dark-treated inactive enzyme form
385000
-
-
gel filtration
387000
-
-
sedimentation analysis
additional information
-
-
mass spectral determination of Cent-I recombinant protein (residues 381-512 of the native PPDK), native molecular weight determined by gel filtration chromatography is 13438
additional information
-
P11155
different isoforms of one of the two cytosolic isoforms of PPDK of maize distinguished by pI value, molecular mass and altered amino acid positions in identified peptides by isoelectric focusing, 2-D electrophoresis and liquid chromatography
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 94000, SDS-PAGE
?
-
x * 103900, deduced from nucleotide sequence
?
-
x * 92700, SDS-PAGE
?
-
x * 94000, SDS-PAGE
?
-
x * 98000, SDS-PAGE
?
-
x * 95000 immunoblot analysis
?
-
x * 96000, recombinant His-tagged PPDK, SDS-PAGE
?
-
x * 94000, SDS-PAGE
?
-
x * 94000, SDS-PAGE
?
Rhodospirillum rubrum S-1
-
x * 92700, SDS-PAGE
-
dimer
-
2 * 75000, SDS-PAGE
dimer
-
2 * 94000, SDS-PAGE
dimer
-
2 * 97600, analytical ultracentrifugation and gel filtration
hexamer
-
6 * 58000, SDS-PAGE
homodimer
-
x * 96000, PPDK of Clostridium symbiosum, three consecutive structural domains connected by helical linkers, X-ray crystal structure
homodimer
Q70WQ6, -
x * 100000, SDS-PAGE, homomeric dimer, calculated from theoretical weight and chromatography, more similar to bacterial PPDKs (dimer) than protists or plants (tetramer)
homotetramer
-
4 * 95000, the enzyme is maximally active as a homotetramer and is inactive in the dimeric and monomeric forms
tetramer
-
4 * 94000, SDS-PAGE
tetramer
-
4 * 94800, gel filtration
tetramer
-
molecular filtration
tetramer
-
4 * 95000, dissociates into largely inactive dimers and tetramers when subjected to cold temperatures in vitro
tetramer
-
4 * 100000, SDS-PAGE
monomer
-
1 * 13438, recombinant protein of the central domain of PPDK (Cent-I protein), mass spectrometry, chromatography
additional information
-
multilayered structure of Cent-I protein in solution, chain structure of Cent-I in solution closely related to X-ray structure of native PPDK, three-dimensional structure calculated by different methods, topology of secondary structure indicated
additional information
P37213
modeling of the three-dimensional structure of the PPDK protein in a homology-modeling approach
additional information
-
phosphomonomer of about 95000 Dalton in rice as reference, SDS-PAGE, immunoblot
additional information
-
PPDK contains a His445-containing domain, which is positioned close to the nucleotide binding domain and does not contact the PEP/pyruvate-binding domain, the enzyme shows two conformations and swivel motion of the His domain, upon detachment from the His domain, the two nucleotide-binding subdomains undergo a hinge motion that opens the active-site cleft, structure analysis, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
PPDK activity in C3 chloroplasts is light-regulated via reversible phosphorylation of an active-site Thr residue by the PPDK regulatory protein, i.e. C3 RP, a most unusual bifunctional protein kinase /protein phosphatase, overview
phosphoprotein
-
phosphorylation/dephosphorylation by the PPDK regulatory protein RP at T456, RP-reaction described as PPDK-T456 + ADP = PPDK-T456P + AMP and PPDK-T456P + phophate = PPDK-T456 + diphosphate
phosphoprotein
-
PPDK activity in C4 chloroplasts is light-regulated via reversible phosphorylation of an active-site Thr residue by the PPDK regulatory protein, i.e. C4 RP, a most unusual bifunctional protein kinase /protein phosphatase, overview
phosphoprotein
-
the PPDK regulatory protein catalyses this light-dependent regulation of the enzyme by reversible phosphorylation of the active-site Thr456 residue
phosphoprotein
-
phosphorylation and dephosphorylation of the enzyme by PPDK regulatory protein (RP) lead to inactivation and activation, respectively. Isoform RP2 is able to catalyse the dephosphorylation of the enzyme, although at a slower rate than isoformRP1
additional information
-
during seed development posttranslational down-regulation of PPDK in activity and amount by regulatory threonyl-phosphorylation PPDK regulatory protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
method description
-
PPDK, mutant R219E/E271R/S262D, hanging drop vapour diffusion method at 30C, using a protein solution containing 28 mg/ml protein in 20 mM imidazole, pH 6.5, 0.1 mM EDTA, 100 mM KCl, and 1 mM DTT. The reservoir solution contains 50% saturated ammonium sulfate and 0.1 M Na-HEPES, pH 7.0, mixing of equal volumes of protein solution and reservoir solution, structure determination and analysis of two different enzyme conformations at 1.94 A resolution, modeling
-
X-ray crystal structure mentioned, the central domain faces the C-terminal domain and positions the phosphorylated His residue for phosphoryl transfer to pyruvate thereby forming phosphoenolpyruvate and regenerating the unphosphorylated H455, native structure determined by NMR
-
crystals sensitive to temperature
-
hanging-drop vapour diffusion method, crystal strcuture with and without phosphoenolpyruvate, determined at 2.3 A resolution
-
method description
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
Arundinaria sp., Zea mays
-
rapid inactivation, activity is recovered by re-warming to 20-30C
0
-
-
20 min, about 70% loss of activity
0
-
-, Q39735
5 min 50% loss of activity
0
-
-, Q39734
20 min 82-87% loss of activity
0
-
-
10 min 50% loss of activity
0
-
-
45 min, 0.6 mg protein/ml, 78% loss of activity. 2.4 mg protein/ml, 29% loss of activity. Partial protection against cold inactivation with 10 mM MgCl2, 4 mM phosphoenolpyruvate, 1.52 mM glycerol, 0.48 mM proline, 0.23 mM betain, 0.40 mM sorbitol, 0.73 mM trehalose. Pyruvate has no effect
2
-
-
activity in vivo decreases more than 30% when exposed 90 min
4
-
-
dissociates in dimers when subjected to gel filtration at 4C or at 22C but in the presence of EDTA
4
-
-
dissociates in dimers when subjected to gel filtration at 4C or at 22C but in the presence of EDTA; does not dissociate when subjected to gel filtration al 4C or 22C or in the presence of EDTA
4
-
-
-
10
-
-
30 min, about 40% loss of activity
10
-
-
inactive below 10C
12
-
-
loses activity below at about 12C by dissociation of the tetramer, considered as one possible cause of the reduction of the photosynthetic rate of maize at low temperatures
20
40
-
stable for at least 30 min
24
-
-
45 min, 0.6 mg protein/ml, 18% loss of activity. 2.4 mg protein/ml, no inhibition
50
-
-
irreversible denaturation
additional information
-
-
rapid inactivation at 0C
additional information
-
Sedum prealtum
-
-
additional information
-
-
cold inactivation follows first order kinetics, this inactivation is protected by pyruvate, phosphoenolpyruvate and polyols, e.g. sucrose and glycerol
additional information
-
-
cold labile, reactivation by several min incubation at 22C
additional information
-
-
up to 70% of activity of PPDK retained after incubation of transformed leaf extracts for 180 min on ice, 5fold increased amounts of recombinant enzyme by using a construct with seventeen amino acid substitutions, PPDK extracted from untransformed maize lost 90% of its activity after 20 min, in recombinant plants the photosynthetic rate (CO2 uptake) at 8C significantly increased by 23%, no obvious effect at higher temperatures
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
central domain protein Cent-I, 4.3 kcal/mol (delta G) for unfolding at 25C in buffer at pH 7.0
-
does not require thiol compounds to maintain stability during storage or assay
-
freezing and thawing inactivates
-
slowly inactivates when kept at 4C
-
sensitive to dilution, particularly at concentrations below 0.3 mg/ml, stable to freezing and thawing
-
glycerol protects both the day-form and night-form in vitro
-
Mg2+ stabilizes the oligomeric structure of the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C, as a precipitate in a 66% saturated solution of (NH4)2SO4
Arundinaria sp.
-
-20C, 50% v/v glycerol, optimal storage condition, decay factor is 3 months
-
22C, Tris-HCl buffer, pH 7.9, 5 mM imidazole, 50 mM NaCl, 2 weeks
-
retains 85% of activity after two weeks at room temperature
Gluconacetobacter xylinus
-
0C, as a precipitate in a 66% saturated solution of (NH4)2SO4
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
using hydroxyapatite, Sephadex G-200 and DEAE column chromatography
-
partial, using Sephadex G-25 and DEAE column chromatography
-
soluble recombinant His-tagged PPDK from Escherichia coli by nickel affinity chromatography
-
partial, using ammonium sulfate precipitation, and chromatography on DEAE-cellulose and Bio-Gel
-
recombinant proteins of the central domain (Cent-I) and of the N-terminus (Tem-340, residues 1-340 of the native PPDK)
-
two deletion mutants purified by a method that includes DEAE-cellulose and Sephadex G-200 chromatography
-
partial by a method that includes Sephadex G-25 chromatography
-
method that includes metal affinity chromatography
-
partial, using ammonium sulfate precipitation and chromatography on DEAE-cellulose
Gluconacetobacter xylinus
-
partial, using Sephadex G-25 and DEAE column chromatography
-
partial, using Sephadex G-25 column chromatography
-
partial, using ammonium sulfate precipitation and chromatography on DEAE-cellulose and Sephadex G-200
-
partial, using ammonium sulfate precipitation and chromatography on DEAE-cellulose and hydroxyapatite
-
partial, using Sephadex G-25 column chromatography
Sedum prealtum
-
recombinant protein, heat precipitation at 90C for 20 min, ion exchange chromatography
Q70WQ6, -
partial, using Sephadex G-25 and DEAE column chromatography
-
isolation of an inactive enzyme form dark-grown leaves
-
maize PPDK of leaves expressed for inhibitor studies in Escherichia coli with a His-tag and purified on a Ni-affinity column
-
method that includes successive chromatography through DE-52, hydroxyapatite, Sephadex G-200 and Blue agarose
-
partial
-
partial, using Sephadex-G200 and Hypatite C chromatography
-
recombinant maize PPDK used for inactivation/activation assay by the PPDK regulatory protein RP
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
genomic analysis of the glycolytic/gluconeogenic pathway, optimization of C-terminally His-tagged PPDK expression in Escherichia coli as soluble protein, overview
-
25 kDa C-terminal and 35 kDa N-terminal deletion mutants expressed in Escherichia coli
-
expressed in Escherichia coli
-
expression of mutant enzyme R219E/E271R/S262D in Escherichia coli strain JM101
-
phylogenetic analysis
P37213
the cloned sequence represents about 20% of the complete gene, and shows about 56% homology with enzymes from maize and Bacteroides symbiosus
-
expressed in Escherichia coli
-, Q39735
high levels of expression in Zea mays by using a double intron cassette and a chimeric cDNA made from Flaveria bidentis and Flaveria brownii with a maximum content of 1 mg/g fresh weight. In leaves of transgenic maize, PPDK molecules produced from the transgene are detected in cold-tolerant homotetramers or in heterotetramers of intermediate cold susceptibility formed with the internal PPDK
-
expressed in Escherichia coli
-, Q39734
introduction of a cold-tolerant PPDK cDNA isolated from Flaveria brownii into maize by Agrobacterium-mediated transformation. Higher levels of expression by using a double intron cassette and a chimeric cDNA made from Flaveria bidentis and Flaveria brownii with a maximum content of 1 mg/g fresh weight. In leaves of transgenic maize, PPDK molecules produced from the transgene are detected in cold-tolerant homotetramers or in heterotetramers of intermediate cold susceptibility formed with the internal PPDK
-
78% of homology with maize enzyme
-
expressed in a baculovirus system
-
expressed in Nicotiana tabacum
-
into the vector pUMP16M13
-
quantitative real-time reverse transcription (RT)-PCR expression analysis during transfer of plants from 25C to 14C growth temperature
-
Escherichia coli; Escherichia coli
Q2LIW1, Q2LIW2, -
Escherichia coli, strains DH5alpha and BL21-CodonPLUS(DE3)-RIL
Q70WQ6, -
expressed in Escherichia coli
A2GU49, -
expressed in Escherichia coli
O76283, -
; expressed in Escherichia coli
-
Escherichia coli, three constructs, one construct consisting of the 3'-part of Flaveria brownii (Asteraceae) of cold tolerant PPDK fused to maize PPDK (15th exon), another construct includes a set of point mutations to substitute all of the 17 residues that differ between the 3'-parts of maize and Flaveria brownii PPDK, respectively, the whole genomic sequence of the maize PPDK gene is included as a control, transformation of constructs into maize inbred line A188 by Agrobacterium tumefaciens (strain LBA4404), individual range of variation in the amount of PPDK among regenerated plants, crude leaf extracts of some transformed plants produce a large amount of cold tolerant recombinant enzyme and reveal a greatly improved cold tolerance especially by using the construct altered at 17 amino acid positions
-
expressed in Arabidopsis thaliana, found exclusively in chloroplasts of transgenic Arabidopsis plants
-
expressed in Escherichia coli
-
expressed in Oryza sativa subsp. indica cultivar IR64
-
quantitative expression analysis of the enzyme during endosperm development, expression profiles, overview
-
quantitative real-time reverse transcription (RT)-PCR expression analysis during transfer of plants from 25C to 14C growth temperature
-
to improve the cold stability of the enzyme, a cold-tolerant PPDK cDNA isolated from Flaveria brownii is introduced into maize by Agrobacterium-mediated transformation. Higher levels of expression are ontained by using a double intron cassette and a chimeric cDNA made from Flaveria bidentis and Flaveria brownii with a maximum content of 1 mg/g fresh weight. In leaves of transgenic maize, PPDK molecules produced from the transgene are detected in cold-tolerant homotetramers or in heterotetramers of intermediate cold susceptibility formed with the internal PPDK. A significant improvement in the cold stability of PPDK can be achieved when a suffcient quantity of cold-tolerant subunits is expressed in transgenic maize leaves
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
both the cytosolic and chloroplastic isoforms of pyruvate, orthophosphate dikinase are up-regulated in naturally senescing leaves
-
in the C4 pathway, enzyme activity is strictly regulated in an up/down manner by the level of incident light
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D280A
-
partial activity
R135A
-
partial activity, 15 mutant enzymes studied
T456D
-
no activity
T456E
-
no activity
T456F
-
-
T456F
-
1% activity with respect to wild type
T456S
-
111% activity with respect to wild type
T456V
-
98% activity with respect to wild type
T456Y
-
-
T456Y
-
6% activity with respect to wild type
E279A
-
partial activity
additional information
-
35 kDa C-terminal deletion mutant catalyzes the formation of a diphosphorylenzyme intermediate and diphosphate, but not the subsequent formation of phosphoenolpyruvate. A 25 kDa N-terminal deletion mutant catalyzes the second partial reaction but not the first one
R219E/E271R/S262D
-
site-directed mutagensis, comparison of mutant to wild-type enzyme structure
additional information
-, Q27662
application of ribozyme-mediated cleavage of the PPDK transcript to decrease PPDK transcript levels to 20% of normal level with an accompanying decrease in PPDK enzyme activity and decreased ATP levels to 3% of normal levels. Extracellular cleavage of PPDK mRNA by PPDK antisense RNA containing hammerhead ribozyme, overview
additional information
-
development of a bioluminescent assay method for diphosphate, detection applied to single-nucleotide polymorphism analysis using one-base extension reaction, overview
H458N
-
no activity
additional information
-
point mutations introduced into exons 15, 16, 17, 18, and 19 of the maize PPDK gene to generate a construct altered at 17 amino acid positions at the C-terminus that mimicks the 3'-part of PPDK of Flaveria brownii (Asteraceae) encoding the C-terminal part of PPDK responsible for cold tolerance, two other constructs represent a fusion protein of the 3'-part of PPDK of Flaveria brownii (Asteraceae) and maize PPDK, a further construct of maize PPDK serves as a control
additional information
-
direct pleiotropic effects of Opaque-2 mutation on PPDK, mechanism, epistatic relationship between PPDK and Opaque-2, detailed overview
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
percent decrease of fluorescence intensity (304 nm) for conversion of native protein (0 M urea) to fully denaturation (6 M urea) calculated (23.5%), DELTA G for unfolding of Cent-I (PPDK central domain construct of residues 381-512) in solvent determined (4.3 kcal/mol)
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
-
the enzyme is a good target for anti-parasite drug design
drug development
P37213
PPDK is a good target in design of antiparasitic agents
pharmacology
P37213
drug design, in silico studies on stereo chemical quality of PPDK protein structure, interaction studies to identify promising ligands to inhibit the function of PPDK, possibility of using proposed ligands as inhibitors for intestinal infections caused by Entamoeba histolytica in humans and for related pathogens, virtual screening of ligands to inhibit PPDK by docking studies using compound input libraries, phylogenetic trees of pathogens as further targets for in silico drug design to inhibit PPDK
drug development
-, Q27662
PPDK is not found in vertebrates, so specific inhibitors may be useful for treatment of infections caused by anaerobic protists that depend on pyrophosphate-dependent glycolysis
analysis
-
PPDK is useful in DNA analysis, method development, overview
analysis
-
pyruvate phosphate dikinase, expressed onto bacterial magnetic particles, PPDK-BacMPs, is utilized in pyrosequencing
agriculture
-
PPDK function during early cereal seed development, seed metabolism
agriculture
-
modification of the cold sensitivity of a C4 photosynthetic enzyme by employing cereal transformation technology. A significant improvement in the cold stability of PPDK can be achieved when a suffcient quantity of cold-tolerant subunits is expressed in transgenic maize leaves
agriculture
-
to improve the cold stability of the PPDK enzyme, studies on cold tolerance in plants
drug development
-
the enzyme is a potential herbicide target in C4 plants