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2',3'-dideoxyadenosine 5'-triphosphate + pyruvate + phosphate
?
-
-
-
-
r
2'-dAMP + phosphoenolpyruvate + diphosphate
2'-dATP + pyruvate + phosphate
-
-
-
-
?
2'-dATP + pyruvate + phosphate
?
-
-
-
-
r
3'-dATP + pyruvate + phosphate
?
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
ATP + PPDK central domain construct of residues 381-512 (Cent-I) + phosphate
?
-
-
-
?
ATP + PPDK N-terminal domain construct of residues 1-340 (Tem-340) + phosphate
?
-
-
-
?
ATP + PPDK N-terminal domain construct of residues 1-553 (Tem340-Cent-I) + phosphate
?
-
-
-
?
ATP + pyruvate + arsenate
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
additional information
?
-
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
synthesis of ATP is not thermodynamically favorable in trophozoites of Entamoeba histolytica
-
-
?
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
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
-
diphosphate released by DNA polymerase is converted to ATP by pyruvate phosphate dikinase, PPDK
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
the enzyme is dependent on AMP in the phosphotransfer networks
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
the enzyme is dependent on AMP in the phosphotransfer networks
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
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
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
?
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
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
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
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 + pyruvate + arsenate
?
Arundinaria sp.
-
-
-
-
ir
ATP + pyruvate + arsenate
?
-
the rate of phosphoenolpyruvate formation in the presence of arsenate is 65% lower than that obtained with phosphate
-
-
?
ATP + pyruvate + arsenate
?
-
-
-
-
ir
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
Arundinaria sp.
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
Arundinaria sp.
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
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
active site residues are Lys21, Arg91, Asp323, Glu325 and Gln337
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
essential enzyme of C4 photosynthetic pathway
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
structural asymmetries and nucleotide binding states in the enzyme dimer support an alternate binding change mechanism
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
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
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
permits the incorporation of pyruvate into carbohydrates in the light in Crassulacean acid metabolism
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
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
-
enzyme activity has implication in the regulation of gluconeogenesis and carbohydrate oxidation
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
key enzyme in the photosynthesis of C4 plants
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
key enzyme in the photosynthesis of C4 plants
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
specificity is strictly restricted to adenine nucleotides
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
Sedum prealtum
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
Sedum prealtum
-
permits the incorporation of pyruvate into carbohydrates in the light in Crassulacean acid metabolism
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
the enzyme is strictly and reversibly regulated by light
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
bidirectional activity, preference for catabolic reaction, DELTA G +9.9 kJ/mole
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
PPDK functions in the glycolytic direction with production of ATP in the glycosomes
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
PPDK functions in the glycolytic direction with production of ATP in the glycosomes
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
activity with UTP, GTP and CTP is 1-3% of the activity with ATP
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
HPO42- is the substrate
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
activity strictly and reversibly regulated by light
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
C4 acid cycle enzyme
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
loses activity below about 12°C 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
rate-limiting enzyme of C4 acid cycle
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
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
-
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
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
specificity is strictly restricted to adenine nucleotides
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
specificity is strictly restricted to adenine nucleotides
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
specificity is strictly restricted to adenine nucleotides
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
dAMP can replace ATP but with 20% of the activity
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
the enzyme forms phosphoenolpyruvate via two partial reactions: pyruvate phosphate dikinase + ATP + phosphate -> [pyruvate phosphate dikinase]-phosphate + AMP + diphosphate and [pyruvate phosphate dikinase]-phosphate + pyruvate -> phosphoenolpyruvate + pyruvate phosphate dikinase
-
-
r
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
?
-
-
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
?
-
-
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
?
-
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
?
-
-
the cytosolic PPDK functions in rice to modulate carbon metabolism during grain filling
-
-
?
additional information
?
-
diphosphate-dependent glycolysis
-
-
?
additional information
?
-
diphosphate-dependent glycolysis
-
-
?
additional information
?
-
-
diphosphate-dependent glycolysis
-
-
?
additional information
?
-
diphosphate-dependent glycolysis, pyruvate kinase (PK) replaced by pyrophosphate-dependent pyruvate phosphate dikinase (PPDK)
-
-
?
additional information
?
-
diphosphate-dependent glycolysis, pyruvate kinase (PK) replaced by pyrophosphate-dependent pyruvate phosphate dikinase (PPDK)
-
-
?
additional information
?
-
-
diphosphate-dependent glycolysis, pyruvate kinase (PK) replaced by pyrophosphate-dependent pyruvate phosphate dikinase (PPDK)
-
-
?
additional information
?
-
diphosphate-dependent glycolysis
-
-
?
additional information
?
-
-
diphosphate-dependent glycolysis
-
-
?
additional information
?
-
diphosphate-dependent glycolysis, pyruvate kinase (PK) replaced by pyrophosphate-dependent pyruvate phosphate dikinase (PPDK)
-
-
?
additional information
?
-
-
diphosphate-dependent glycolysis, pyruvate kinase (PK) replaced by pyrophosphate-dependent pyruvate phosphate dikinase (PPDK)
-
-
?
additional information
?
-
coupled assay method with lactate dehydrogenase
-
-
?
additional information
?
-
-
coupled assay method with lactate dehydrogenase
-
-
?
additional information
?
-
-
involved in C4 dicarboxylic acid pathway in plant
-
-
?
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
?
-
-
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
?
-
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
?
-
-
functions in glycolytic pathway
-
-
?
additional information
?
-
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
?
-
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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
additional information
?
-
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
synthesis of ATP is not thermodynamically favorable in trophozoites of Entamoeba histolytica
-
-
?
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
the enzyme is dependent on AMP in the phosphotransfer networks
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
the enzyme is dependent on AMP in the phosphotransfer networks
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
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
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
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
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
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
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
essential enzyme of C4 photosynthetic pathway
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
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
-
permits the incorporation of pyruvate into carbohydrates in the light in Crassulacean acid metabolism
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
enzyme activity has implication in the regulation of gluconeogenesis and carbohydrate oxidation
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
key enzyme in the photosynthesis of C4 plants
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
key enzyme in the photosynthesis of C4 plants
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
Sedum prealtum
-
permits the incorporation of pyruvate into carbohydrates in the light in Crassulacean acid metabolism
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
PPDK functions in the glycolytic direction with production of ATP in the glycosomes
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
PPDK functions in the glycolytic direction with production of ATP in the glycosomes
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
activity strictly and reversibly regulated by light
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
C4 acid cycle enzyme
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
loses activity below about 12°C 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
rate-limiting enzyme of C4 acid cycle
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
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
-
-
-
-
r
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
?
-
-
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
?
-
-
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
?
-
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
?
-
-
the cytosolic PPDK functions in rice to modulate carbon metabolism during grain filling
-
-
?
additional information
?
-
diphosphate-dependent glycolysis
-
-
?
additional information
?
-
diphosphate-dependent glycolysis
-
-
?
additional information
?
-
-
diphosphate-dependent glycolysis
-
-
?
additional information
?
-
diphosphate-dependent glycolysis
-
-
?
additional information
?
-
-
diphosphate-dependent glycolysis
-
-
?
additional information
?
-
-
involved in C4 dicarboxylic acid pathway in plant
-
-
?
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
?
-
-
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
?
-
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
?
-
-
functions in glycolytic pathway
-
-
?
additional information
?
-
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
-
-
?
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(1-benzenesulfonyl-pyrrolidin-2-yl)-(3,5-dimethyl-4-p-tolylsulfanyl-pyrazol-1-yl)-methanone
-
(7-benzyl-3-methyl-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-ylsulfanyl)-acetic acid benzyl ester
-
2-(1-(3-dimethylaminopropyl)-5-methoxyindol-3-yl)-3-(1H-indol-3-yl)maleimide
i.e. Go 6983
-
2-(1-benzyl-1H-benzoimidazol-2-ylmethylsulfanyl)-3H-quinazolin-4-one
-
2-(1H-Benzoimidazol-2-ylsulfanyl)-N-(5-phenyl-[1,3,4]thiadiazol-2-yl)-acetamide
-
2-(1H-benzoimidazol-2-ylsulfanyl)-N-[4-(pyridin-2-ylsulfamoyl)-phenyl]-acetamide
-
2-(4-amino-1-isopropyl-1H-pyrazolo[3,4-d]pyrimidin-3-yl)-1H-indol-5-ol
-
-
2-(9-allyl-9H-1,3,4,9-tetraaza-fluoren-2-ylsulfanyl)-N-(5-methyl-isoxazol-3-yl)-butyramide
-
2-(9-benzyl-9H-1,3,4,9-tetraaza-fluoren-2-ylsulfanyl)-N-furan-2-ylmethyl-acetamide
-
2-benzylsulfanyl-N-[5-(3,4-dichloro-benzyl)-[1,3,4]thiadiazol-2-yl]-acetamide
-
2-Bromobutyrate
-
80% inhibition at 1 mM
2-Bromopropionate
-
74% inhibition at 1 mM
2-hydroxy-5-methoxy-3-[[(1R,2S,4aS,8aS)-1,2,4a-trimethyl-5-methylenedecahydro-1-naphthalenyl]methyl]-1,4-benzoquinone
-
-
2-[2-(1-benzyl-1H-benzoimidazol-2-ylsulfanylmethyl)-benzoimidazol-1-yl]-acetamide
-
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
-
3-Bromopropionate
-
66% inhibition at 1 mM
4'-aminobutyl-5,7-dihydroxyflavone
-
displays selectivity for inhibition of PPDK versus other enzymes that utilize ATP and NAD+
4'-aminohexyl-5,7-dihydroxyflavone
-
a potent competitive PPDK inhibitor with an IC50 value of 0.0016 mM
4'-aminopropyl-5,7-dihydroxyflavone
-
derivative specifically targets the ATP binding site and inhibits catalysis of only the PPDK + ATP + phosphate -> PPDK-P + AMP diphosphate partial reaction during single turnover experiments
4-chloro-N-[2-(1-phenyl-1H-tetrazol-5-ylsulfanyl)-acenaphthen-1-yl]-benzenesulfonamide
-
4-[4-hydroxy-5-oxo-2-(3-phenoxy-phenyl)-1-pyridin-3-ylmethyl-2,5-dihydro-1H-pyrrole-3-carbonyl]-N,N-dimethyl-benzenesulfonamide
-
5'-adenylimidodiphosphate
-
-
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
-
5-phenyl-2-[2-([1,2,4]triazolo[4,3-a]pyridin-3-ylsulfanyl)-acetylamino]-thiophene-3-carboxylic acid ethyl ester
-
6-(4-benzyl-5-phenyl-4H-[1,2,4]triazol-3-ylsulfanylmethyl)-N-phenyl-[1,3,5]triazine-2,4-diamine
-
6-bromoindirubin-3'-monoxime
-
-
6-[5-(2-chloro-phenyl)-4-phenyl-4H-[1,2,4]triazol-3-ylsulfanylmethyl]-N-phenyl-[1,3,5] triazine-2,4-diamine
-
adenosine 5'-mono-O-phosphorothiolate
-
-
biphosphonate
-
mixed inhibition mechanism with respect to diphosphate
Bromoacetate
-
83% inhibition at 1 mM
Co2+
-
at high concentration inhibits the phosphoenolpyruvate, pyruvate exchange reaction
D-glucose 1-phosphate
72% activity sustained, effector concentration 5 mM, 55°C
diethyldicarbonate
-
inactivates the enzyme by combination with histidyl residues, inhibition is reversed by hydroxylamine
Fe2+
-
competitive to Mg2+
gamma(p-Arsenophenyl)-n-butyrate
Imidodiphosphate
-
competitive to diphosphate
MgHPO4
-
competitive to HPO42-
Mn2+
-
at high concentration inhibits the phosphate, diphosphate exchange reaction
N-(3-cyano-4,5-diphenyl-furan-2-yl)-2-(1,3-dioxo-1,3-dihydro-isoindol-2-yl)-acetamide
-
N-(3-cyano-4,5-diphenyl-furan-2-yl)-4-(1,3-dioxo-1,3-dihydro-isoindol-2-yl)-butyramide
-
N-[4-(3-amino-1H-indazol-4-yl)phenyl]-N'-(2-fluoro-5-methylphenyl)urea
-
-
N-[5-(3-chloro-benzyl)-thiazol-2-yl]-3-[5-(2-methyl-cyclopropyl)-furan-2-yl]-propionamide
-
Phosphoglycolate
-
competitive to phosphoenolpyruvate
potassium fluoride
-
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
-
tetrasodium 1-hydroxyethylidene biphosphonate
-
-
tetrasodium 1-hydroxymethylidene biphosphonate
-
-
tetrasodium 1-hydroxynonane biphosphonate
-
-
UDP
55% activity of PPDK, effector concentration 5 mM, 55°C
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)
Z220582104
the specific to pyruvate phosphate dikinase inhibitor for leishmanicidal activities is active against free promastigotes and intracellular amastigotes. The inhibitor is well tolerated by the dividing cells and normal human lymphocytes and monocytes with no adverse effects on the growth kinetics or viability
-
[3-methyl-7-(3-methyl-benzyl)-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-ylsulfanyl]-acetic acid benzyl ester
-
5,5-dithiobis(2-nitrobenzoic acid)
-
-
5,5-dithiobis(2-nitrobenzoic acid)
-
-
ADP
Arundinaria sp.
-
mediates a rapid but reversible inactivation in presence of a thiol
ADP
-
mediates a rapid but reversible inactivation in presence of a thiol
ADP
-
no inhibition up to 0.46 mM
alpha-beta-methylene ATP
-
competitive to ATP
alpha-beta-methylene ATP
-
competitive to ATP
AMP
-
-
AMP
-
phosphoenolpyruvate formation, competitive to ATP
AMP
-
non competitive with respect to ATP
AMP
-
competitive with respect to ATP
ATP
-
competitive to AMP
ATP
-
product inhibition versus phosphoenolpyruvate is noncompetitive
ATP
-
pyruvate formation, competitive to AMP
ATP
concentration 1 mM, 55°C, AMP-competitive inhibition as deduced from AMP saturation kinetics by using various ATP concentration ranging between 50-200 micromol
beta-gamma-methylene ATP
-
competitive to ATP
beta-gamma-methylene ATP
-
competitive to ATP
Bromopyruvate
-
competitive to phosphoenolpyruvate
Bromopyruvate
-
competitive to phosphoenolpyruvate
Bromopyruvate
-
irreversible inactivation
Ca2+
-
competitive to Mg2+
CTP
-
-
CTP
-
total inhibition of the forward reaction at 1 mM
dATP
-
-
dATP
-
40% inhibition at 1 mM
diphosphate
-
competitive to phosphate
diphosphate
-
non competitive to phosphate
diphosphate
-
competitive inhibitor
gamma(p-Arsenophenyl)-n-butyrate
Arundinaria sp.
-
-
gamma(p-Arsenophenyl)-n-butyrate
-
-
GMP
-
competitive to ATP
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
iodoacetate
-
-
iodoacetate
-
70% inhibition at 1 mM
ITP
-
-
ITP
-
total inhibition of the forward reaction at 1 mM
Methylene diphosphonate
-
competitive to diphosphate
Methylene diphosphonate
-
competitive to diphosphate
N-ethylmaleimide
-
-
oxalate
-
mixed mechanism with respect to phosphoenolpyruvate and diphosphate
oxalate
-
competitive to pyruvate
oxalate
-
competitive to pyruvate, oxalate binds to the phosphorylated form of the enzyme
p-chloromercuribenzoate
Arundinaria sp.
-
-
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
phosphate
-
competitive to diphosphate
phosphate
Arundinaria sp.
-
-
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
pyruvate
-
competitive to phosphoenolpyruvate
pyruvate
Arundinaria sp.
-
-
Sulfhydryl agents
-
-
-
additional information
-
phosphorylation of PPDK by AtRP1/2 is negated or greatly reduced when pyruvate is also included in the reaction mixture
-
additional information
-
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
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
-
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
-
not inhibited by iodoacetamide
-
additional information
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
-
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
-
response of the enzyme to energy charge
-
additional information
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 25°C), reversibility of RP activity by diphosphate-dependent reactivation assay described (1 mM diphosphate, at 25°C), SDS-PAGE and Western-Blot for detection of T456P-PPDK and RP
-
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 25°C), reversibility of RP activity by diphosphate-dependent reactivation assay described (1 mM diphosphate, at 25°C), SDS-PAGE and Western-Blot for detection of T456P-PPDK and RP
-
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
-
screening of substances that bind to the PPDK ATP-grasp domain active site reveals that flavone analogues are potent inhibitors of the Clostridium symbiosum PPDK. In silico modeling studies suggest that placement of a 36 carbon-tethered ammonium substituent at the 3'- or 4'-positions of 5,7-dihydroxyflavones result in favorable electrostatic interactions with the PPDK Mg-ATP binding site. Synthesis of polymethylene-tethered amine derivatives of 5,7-dihydroxyflavones
-
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0.28
2',3'-dideoxyadenosine 5'-triphosphate
-
pH 7, 25ºC
0.1
2'-dAMP
-
pH 6.8, 25ºC
0.35
2'-dATP
-
pH 7, 25ºC
0.25
3'-dATP
-
pH 7, 25ºC
0.02 - 0.5
phosphoenolpyruvate
additional information
additional information
-
0.0013
AMP
-
pH 7, 30ºC
0.0015
AMP
-
pH 6.8, 25ºC
0.0016
AMP
-
pH 6.5, 30ºC, pyruvate formation
0.0035
AMP
-
pH 6.8, 25ºC, phosphoenolpyruvate formation
0.004
AMP
Arundinaria sp.
-
pH 6.8, 25ºC
0.005
AMP
-
less than 0.005 mM ,pH 6.3, 25ºC
0.005
AMP
-
pH 5.8-6.4 (optimal pH), 37°C
0.006
AMP
-
pH 7.1, 30ºC, pyruvate formation
0.007
AMP
recombinant enzyme, pH 8.3, temperature not specified in the publication
0.009
AMP
-
pH 6.8, 25ºC, pyruvate-producing reaction, values for 7 mutant PPDK
0.004
ATP
-
pH 6.8, 25ºC
0.015
ATP
-
pH 7.5, 22ºC, phosphoenolpyruvate formation
0.042
ATP
-
pH 7.4, 25ºC, phosphoenolpyruvate formation
0.047
ATP
-
transgenic enzyme
0.049
ATP
-
transgenic enzyme
0.05
ATP
-
transgenic enzyme
0.081
ATP
-
pH 7, 25ºC, E279A mutant, phosphoenolpyruvate-producing reaction
0.082
ATP
-
pH 8.1, 25ºC, phosphoenolpyruvate formation
0.1
ATP
-
pH 6.8, 25ºC, pyruvate formation
0.19
ATP
-
pH 7, 25ºC, wild type and D280 mutant, phosphoenolpyruvate-producing reaction
0.2
ATP
-
pH 8, 30ºC, phosphoenolpyruvate formation
0.4
ATP
-
pH 8.2, 30ºC, phosphoenolpyruvate formation
0.41
ATP
-
pH 7, 25ºC, R135A mutant, phosphoenolpyruvate-producing reaction
0.017
diphosphate
recombinant enzyme, pH 8.3, temperature not specified in the publication
0.029
diphosphate
-
pH 7, 30ºC
0.04
diphosphate
Arundinaria sp.
-
-
0.04
diphosphate
-
pH 7.5, 22ºC, pyruvate formation
0.047
diphosphate
-
pH 7.0, 37°C
0.06
diphosphate
-
pH 6.5, 30ºC, pyruvate formation
0.062
diphosphate
-
pH 7.1, 30ºC, pyruvate formation
0.08
diphosphate
-
pH 6.7, 25ºC
0.089
diphosphate
-
pH 6.8, 25ºC, pyruvate-producing reaction, values for 7 mutant PPDK
0.091
diphosphate
-
pH 6.0, 37°C
0.1
diphosphate
-
pH 6.3, 25ºC
0.1
diphosphate
-
pH 5.8-6.4 (optimal pH), 37°C
0.0014
phosphate
-
-
0.134
phosphate
-
transgenic enzyme
0.138
phosphate
-
transgenic enzyme
0.256
phosphate
-
transgenic enzyme
0.38
phosphate
-
pH 8.1, 25ºC, phosphoenolpyruvate formation
0.43
phosphate
-
pH 8, 22ºC
0.5
phosphate
-
pH 8.3, 30ºC
0.56
phosphate
-
pH 8.1, 25ºC, phosphoenolpyruvate formation
0.6
phosphate
-
pH 6.8, 25ºC, pyruvate formation
0.8
phosphate
-
pH 6.7, 25ºC
0.8
phosphate
-
pH 8.2, 30ºC, phosphoenolpyruvate formation
0.83
phosphate
-
pH 8, 30ºC, phosphoenolpyruvate formation
1
phosphate
-
pH 6.8, 25ºC
1.5
phosphate
-
pH 7.5, 22ºC, phosphoenolpyruvate formation
1.8
phosphate
-
pH 7, 30ºC
0.02
phosphoenolpyruvate
-
pH 5.8-6.4 (optimal pH), 37°C
0.021
phosphoenolpyruvate
-
pH 6.3, 25ºC
0.024
phosphoenolpyruvate
-
-
0.024
phosphoenolpyruvate
-
pH 7.0, 37°C
0.027
phosphoenolpyruvate
-
pH 6.8, 25ºC, pyruvate-producing reaction, values for 7 mutant PPDK
0.03
phosphoenolpyruvate
-
pH 6.0, 37°C
0.033
phosphoenolpyruvate
-
pH 7, 30ºC
0.04
phosphoenolpyruvate
-
0.046
phosphoenolpyruvate
-
pH 7.4, 25ºC, pyruvate formation
0.1
phosphoenolpyruvate
-
pH 6.5, 30ºC, pyruvate formation
0.1
phosphoenolpyruvate
-
pH 6.7, 25ºC
0.13
phosphoenolpyruvate
-
pH 7.1, 30ºC, pyruvate formation
0.14
phosphoenolpyruvate
-
pH 7.5, 22ºC, pyruvate formation
0.16
phosphoenolpyruvate
-
pH 7.4, 25ºC, pyruvate formation
0.194
phosphoenolpyruvate
-
at pH 7.0 and 30°C
0.32
phosphoenolpyruvate
recombinant enzyme, pH 8.3, temperature not specified in the publication
0.5
phosphoenolpyruvate
55°C
0.025
pyruvate
-
pH 8, 22ºC
0.027
pyruvate
-
pH 8, 30ºC, phosphoenolpyruvate formation
0.032
pyruvate
-
transgenic enzyme
0.059
pyruvate
-
transgenic enzyme
0.065
pyruvate
-
transgenic enzyme
0.068
pyruvate
-
pH 7.0, 37°C
0.075
pyruvate
-
pH 7, 30ºC
0.08
pyruvate
-
pH 6.8, 25ºC, pyruvate formation
0.082
pyruvate
-
pH 8.1, 25ºC, phosphoenolpyruvate formation
0.092
pyruvate
-
pH 7.4, 25ºC, phosphoenolpyruvate formation
0.1
pyruvate
-
pH 6.8, 25ºC
0.1
pyruvate
-
pH 6.7, 25ºC
0.11
pyruvate
-
pH 8.3, 30ºC
0.11
pyruvate
Arundinaria sp.
-
pH 8.3, 30ºC
0.178
pyruvate
-
at pH 7.0 and 30°C
0.2
pyruvate
-
pH 8.2, 30ºC, phosphoenolpyruvate formation
0.25
pyruvate
-
pH 7.5, 22ºC, phosphoenolpyruvate formation
305
pyruvate
-
pH 6.0, 37°C
additional information
additional information
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additional information
additional information
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additional information
additional information
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additional information
additional information
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-
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additional information
additional information
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-
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additional information
additional information
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additional information
additional information
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-
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additional information
additional information
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-
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additional information
additional information
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-
-
additional information
additional information
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
-
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
-
kinetics at different temperature, the t1/2 for dephosphorylation of PPDK from chilling-acclimated Miscanthus x giganteus leaves increased to 2.3fold compared to warm-grown leaves, overview
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additional information
additional information
kinetics at different temperature, the t1/2 for dephosphorylation of PPDK from chilling-acclimated Miscanthus x giganteus leaves increased to 3.1fold compared to warm-grown leaves, overview
-
additional information
additional information
-
kinetics at different temperature, the t1/2 for dephosphorylation of PPDK from chilling-acclimated Miscanthus x giganteus leaves increased to 3.1fold compared to warm-grown leaves, overview
-
additional information
additional information
single-turnover reaction kinetics, mutant R219E/E271R/S261D
-
additional information
additional information
-
single-turnover reaction kinetics, mutant R219E/E271R/S261D
-
additional information
additional information
steady-state kinetics, progress curves of the reaction for both the native and recombinant PPDK show non-linearity with the activity increasing until a steady state is reached after a significant delay
-
additional information
additional information
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steady-state kinetics, progress curves of the reaction for both the native and recombinant PPDK show non-linearity with the activity increasing until a steady state is reached after a significant delay
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drug target
the pyruvate phosphate dikinase inhibitor Z220582104 is significantly leishmanicidal against the promastigotes and intracellular amastigotes. The study of pyruvate phosphate dikinase in parasitic organisms is significant because the enzyme is absent in the mammalian host which has different catalytic mechanisms for the glycolytic pathway
drug target
-
the pyruvate phosphate dikinase inhibitor Z220582104 is significantly leishmanicidal against the promastigotes and intracellular amastigotes. The study of pyruvate phosphate dikinase in parasitic organisms is significant because the enzyme is absent in the mammalian host which has different catalytic mechanisms for the glycolytic pathway
-
evolution
three-dimensional modeling of PPDKs from divergent organisms and comparion of the orientation of the phosphorylatable histidine residue within the central domain of PPDKs. These PPDKs are compared using a maximum-likelihood tree. For PPDK from anaerobic protozoans, the central domain tilt toward the N-terminal nucleotide-binding domain, indicating that this enzyme catalyzes ATP synthesis, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview. PPDK in anaerobic organisms is functionally adapted to generate energy more efficiently in an anaerobic environment
evolution
three-dimensional modeling of PPDKs from divergent organisms and comparion of the orientation of the phosphorylatable histidine residue within the central domain of PPDKs. These PPDKs are compared using a maximum-likelihood tree. For PPDK from Giardia, as well as from other anaerobic protozoans, the central domain tilt toward the N-terminal nucleotide-binding domain, indicating that this enzyme catalyzes ATP synthesis, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview. PPDK in anaerobic organisms, e.g. the enzyme from Giardia lamblia, is functionally adapted to generate energy more efficiently in an anaerobic environment
evolution
-
three-dimensional modeling of PPDKs from divergent organisms and comparion of the orientation of the phosphorylatable histidine residue within the central domain of PPDKs. These PPDKs are compared using a maximum-likelihood tree. Phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview
evolution
-
Trypanosoma evansi does not undergo stage-dependent differentiations, it occurs only as bloodstream forms, the metabolic pattern of this parasite is not identical to that of the bloodstream form of Trypanosoma brucei, modelling, overview
evolution
-
Trypanosoma evansi does not undergo stage-dependent differentiations, it occurs only as bloodstream forms, the metabolic pattern of this parasite is not identical to that of the bloodstream form of Trypanosoma brucei, modelling, overview
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malfunction
a reduction in PPDK activities due to high temperature (31°C) is observed during the middle and late grain filling periods, accompanied by downregulated cyPPDK mRNA and protein levels, leading to high temperature-induced chalkiness. Rice chalkiness due to high temperature during grain filling lower the grain quality. Temperature effects on the developmental regulation of PPDK activity are confirmed at transcription, translation and post-translational levels. Comparison of rice grain types at 24°C and 31°C of the two cultivars, overview
malfunction
deletion of the trypanosomal PPDK gene affects glycolysis. The rate of acetate production from glucose is 30% reduced in the DELTAppdk mutant, whereas threonine-derived acetate production is not affected. The DELTAppdk/DELTApepck double mutant, also lacking phosphoenolpyruvate carboxykinase, PEPCK, is incubated in glucose as the only carbon source and shows a 3.8fold reduction of the glycolytic rate compared with the DELTApepck mutant, as a consequence of the imbalanced glycosomal ATP/ADP ratio. Expressing the glycosomal phosphoglycerate kinase (PGKC) in the DELTAppdk/DELTApepck cell line restores the glycolytic flux, but expression of PGKC is lethal for procyclic trypanosomes, as a consequence of ATP depletion, due to glycosomal relocation of cytosolic ATP production. Comparison of glucose metabolism regulation of wild-type and mutant enzymes, the glucose metabolism is strongly impaired in the DELTAppdk/DELTApepck mutant, overview
malfunction
in gluconeogenic but not in rich media, growth of enzyme-deficient mutant DELTAppdK is severely impaired. In RAW 264.7 macrophages, the DELTAppdK mutant shows reduced multiplication, and studies with the DELTAppdK mutant confirm that it reaches the replicative niche. The mutant is attenuated in mice being cleared by week 10
malfunction
-
no difference in growth is observed between PPDK wild-type and null mutant parasite promastigotes, but the incorporation of precursors into storage compound mannogen changes in the mutant compared to wild-type
malfunction
an opaque phenotype results complete pyruvate phosphate dikinase knockout, including loss of vitreous endosperm character
malfunction
-
Brucella suis 513 attenuation occurrs only in the double phosphoenolpyruvate carboxykinase (PckA) / pyruvate phosphate dikinase (PpdK) mutant
malfunction
-
the maize transposable elements Mutator and Ds are used to generate multiple mutant alleles of pyruvate orthophosphate dikinase (PPDK). Loss-of-function mutants are seedling lethal, even when plants are grown under 2% CO2, and they show very low capacity for CO2 assimilation, indicating C4 photosynthesis is essential in maize. Loss of PPDK results in downregulation of gene expression of enzymes of theC4 cycle, the Calvin cycle, and components of photochemistry. The loss of PPDK does not change Kranz anatomy, indicating that this metabolic defect in the C4 cycle does not impinge on the morphological differentiation of C4 characters. However, sugar metabolism and nitrogen utilization are altered in the mutants
malfunction
the pdk1- mutation is seedling-lethal, indicating that C4 photosynthesis is essential in maize
malfunction
-
in gluconeogenic but not in rich media, growth of enzyme-deficient mutant DELTAppdK is severely impaired. In RAW 264.7 macrophages, the DELTAppdK mutant shows reduced multiplication, and studies with the DELTAppdK mutant confirm that it reaches the replicative niche. The mutant is attenuated in mice being cleared by week 10
-
malfunction
-
deletion of the trypanosomal PPDK gene affects glycolysis. The rate of acetate production from glucose is 30% reduced in the DELTAppdk mutant, whereas threonine-derived acetate production is not affected. The DELTAppdk/DELTApepck double mutant, also lacking phosphoenolpyruvate carboxykinase, PEPCK, is incubated in glucose as the only carbon source and shows a 3.8fold reduction of the glycolytic rate compared with the DELTApepck mutant, as a consequence of the imbalanced glycosomal ATP/ADP ratio. Expressing the glycosomal phosphoglycerate kinase (PGKC) in the DELTAppdk/DELTApepck cell line restores the glycolytic flux, but expression of PGKC is lethal for procyclic trypanosomes, as a consequence of ATP depletion, due to glycosomal relocation of cytosolic ATP production. Comparison of glucose metabolism regulation of wild-type and mutant enzymes, the glucose metabolism is strongly impaired in the DELTAppdk/DELTApepck mutant, overview
-
malfunction
-
no difference in growth is observed between PPDK wild-type and null mutant parasite promastigotes, but the incorporation of precursors into storage compound mannogen changes in the mutant compared to wild-type
-
malfunction
-
Brucella suis 513 attenuation occurrs only in the double phosphoenolpyruvate carboxykinase (PckA) / pyruvate phosphate dikinase (PpdK) mutant
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metabolism
-
the enzyme plays a controlling role in the phosphoenolpyruvate-regeneration phase of the C4 photosynthetic pathway
metabolism
-
despite the diminished activities of enzymes involved in the TCA cycle and in the electron transport chain, the ATP levels do not appear to be significantly affected in cells stressed by the presence of hydrogen peroxide and nitrosative stress. A phospho-transfer networks mediated by acetate kinase, adenylate kinase, and nucleoside diphosphate kinase are involved in maintaining ATP homeostasis in the oxidatively challenged cells. This phospho-relay machinery orchestrated by substrate-level phosphorylation is aided by the upregulation in the activities of such enzymes like phosphoenolpyruvate carboxylase, pyruvate orthophosphate dikinase, and phosphoenolpyruvate synthase. The enhanced production of phosphoenolpyruvate and pyruvate further fuel the synthesis of ATP. The phospho-transfer system enables the organism to generate ATP irrespective of the carbon source utilized, and this metabolic reconfiguration enables the organism to fulfill its ATP need in an O2-independent manner by utilizing an intricate phospho-wire module aimed at maximizing the energy potential of PEP with the participation of AMP. While PPDK helps synthesize ATP from of phosphoenolpyruvate in the presence of AMP and diphosphate, phosphoenolpyruvate synthase produces the high energy triphosphate with the participation of AMP and phosphate. These two enzymes are markedly increased in activity in the bacteria grown in the stressed conditions. The two AMP-utilizing enzymes provide a more effective route to ATP than the traditional ADP-dependent pyruvate kinase
metabolism
-
metabolic networks involved in its transformation into pyruvate, phosphoenolpyruvate (PEP) and ATP, overview. exposed to hydrogen peroxide in a mineral medium with glycerol as the sole carbon source, the microbe reconfigures its metabolism to generate ATP primarily via substrate-level phosphorylation. This alternative ATP-producing stratagem results in the synthesis of copious amounts of PEP and pyruvate. The production of these metabolites is mediated via the enhanced activities of such enzymes as pyruvatecarboxylase and phosphoenolpyruvate carboxylase. The high energy PEP is subsequentlyconverted into ATP with the aid of pyruvate phosphate dikinase, phosphoenolpyruvate synthase, and pyruvate kinase with the concomitant formation of pyruvate. The participation of the phosphotransfer enzymes like adenylate kinase and acetate kinase ensures the efficiency of this O2-independent energy-generating machinery. The increased activity of glycerol dehydrogenase in the stressed bacteria provides the necessary precursors to fuel this process. This H2O2-induced anaerobic life-style fortuitously evokes metabolic networks to an effective pathway that can be harnessed into the synthesis of ATP, PEP, and pyruvate
metabolism
-
phosphoenolpyruvate carboxylase (EC 4.1.1.31), NADP-malic enzyme (EC 1.1.1.40), and pyruvate, phosphate dikinase participate in Hatch-Slack pathway known as C4 photosynthesis. The enzymes are the key enzymes of C4 photosynthesis evolved to concentrate CO2 for the Calvin cycle especiallyin dry and hot areas
metabolism
-
the enzyme is involved in gluconeogenesis
metabolism
-
the enzyme is involved in gluconeogenesis
metabolism
-
the enzyme is involved in gluconeogenesis. In fruits from other plants than tomato, the bulk of any gluconeogenic flux proceeds via phosphoenolpyruvate carboxykinase, PEPCK
metabolism
-
the enzyme is involved in gluconeogenesis. In fruits from other plants than tomato, the bulk of any gluconeogenic flux proceeds via phosphoenolpyruvate carboxykinase, PEPCK, whereas in tomato both PEPCK and PPDK can potentially be utilised. The conversion of pyruvate/acetyl-CoA to malate by the glyoxylate cycle, for which glyoxysomal isocitrate lyase is necessary, is not a major pathway utilised by gluconeogenesis in fruits under normal conditions of growth
metabolism
the enzyme plays an important role in the central C metabolism between gluconeogenesis, glycolysis, and TCA cycle. Dysfunction of Brucella abortus fbp, glpX, ppdK, and mae but not of pckA or aceA homologues affects growth on gluconeogenic substrates in vitro
metabolism
-
the enzyme PPDK is an auxiliary enzyme of glycolytic metabolism present in glycosomes, modelling, overview
metabolism
-
the gluconeogenesis pathway in Leishmania parasites involves glycerol kinase, phosphoenolpyruvate carboxykinase, and pyruvate phosphate dikinase which allow the entry of glycerol, aspartate, and alanine into Leishmania mannogen, respectively. Contribution of these enzymes into gluconeogenesis differs between promastigotes and amastigotes, model of gluconeogenesis, overview
metabolism
-
Brucella suis 513 used pyruvate phosphate dikinase (PpdK) and phosphoenolpyruvate carboxykinase (PckA) for phosphoenolpyruvate synthesis in vitro
metabolism
enzyme in cellular energy metabolism
metabolism
-
in C4 photosynthesis, pyruvate orthophosphate dikinase catalyzes the regeneration of phosphoenolpyruvate in the carbon shuttle pathway
metabolism
key enzyme in the photosynthesis of C4 plants
metabolism
-
the enzyme plays an important role in the central C metabolism between gluconeogenesis, glycolysis, and TCA cycle. Dysfunction of Brucella abortus fbp, glpX, ppdK, and mae but not of pckA or aceA homologues affects growth on gluconeogenic substrates in vitro
-
metabolism
-
despite the diminished activities of enzymes involved in the TCA cycle and in the electron transport chain, the ATP levels do not appear to be significantly affected in cells stressed by the presence of hydrogen peroxide and nitrosative stress. A phospho-transfer networks mediated by acetate kinase, adenylate kinase, and nucleoside diphosphate kinase are involved in maintaining ATP homeostasis in the oxidatively challenged cells. This phospho-relay machinery orchestrated by substrate-level phosphorylation is aided by the upregulation in the activities of such enzymes like phosphoenolpyruvate carboxylase, pyruvate orthophosphate dikinase, and phosphoenolpyruvate synthase. The enhanced production of phosphoenolpyruvate and pyruvate further fuel the synthesis of ATP. The phospho-transfer system enables the organism to generate ATP irrespective of the carbon source utilized, and this metabolic reconfiguration enables the organism to fulfill its ATP need in an O2-independent manner by utilizing an intricate phospho-wire module aimed at maximizing the energy potential of PEP with the participation of AMP. While PPDK helps synthesize ATP from of phosphoenolpyruvate in the presence of AMP and diphosphate, phosphoenolpyruvate synthase produces the high energy triphosphate with the participation of AMP and phosphate. These two enzymes are markedly increased in activity in the bacteria grown in the stressed conditions. The two AMP-utilizing enzymes provide a more effective route to ATP than the traditional ADP-dependent pyruvate kinase
-
metabolism
-
metabolic networks involved in its transformation into pyruvate, phosphoenolpyruvate (PEP) and ATP, overview. exposed to hydrogen peroxide in a mineral medium with glycerol as the sole carbon source, the microbe reconfigures its metabolism to generate ATP primarily via substrate-level phosphorylation. This alternative ATP-producing stratagem results in the synthesis of copious amounts of PEP and pyruvate. The production of these metabolites is mediated via the enhanced activities of such enzymes as pyruvatecarboxylase and phosphoenolpyruvate carboxylase. The high energy PEP is subsequentlyconverted into ATP with the aid of pyruvate phosphate dikinase, phosphoenolpyruvate synthase, and pyruvate kinase with the concomitant formation of pyruvate. The participation of the phosphotransfer enzymes like adenylate kinase and acetate kinase ensures the efficiency of this O2-independent energy-generating machinery. The increased activity of glycerol dehydrogenase in the stressed bacteria provides the necessary precursors to fuel this process. This H2O2-induced anaerobic life-style fortuitously evokes metabolic networks to an effective pathway that can be harnessed into the synthesis of ATP, PEP, and pyruvate
-
metabolism
-
the gluconeogenesis pathway in Leishmania parasites involves glycerol kinase, phosphoenolpyruvate carboxykinase, and pyruvate phosphate dikinase which allow the entry of glycerol, aspartate, and alanine into Leishmania mannogen, respectively. Contribution of these enzymes into gluconeogenesis differs between promastigotes and amastigotes, model of gluconeogenesis, overview
-
metabolism
-
key enzyme in the photosynthesis of C4 plants
-
metabolism
-
the enzyme PPDK is an auxiliary enzyme of glycolytic metabolism present in glycosomes, modelling, overview
-
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
physiological function
a function of isozyme cyPPDK in rice is to modulate carbon metabolism during grain filling
physiological function
-
enzyme PPDK is involved in ATP homeostasis in Pseudomonas fluorescens, overview
physiological function
PPDK is the key enzyme of the C4 pathway, and its activity may limit the photosynthesis rate in maize leaves. The amount of PPDK (unphosphorylated) involved in C4 photosynthesis is strictly controlled by light intensity
physiological function
PPDK is the key enzyme of the C4 pathway, and its activity may limit the photosynthesis rate in maize leaves. The amount of PPDK (unphosphorylated) involved in C4 photosynthesis is strictly controlled by light intensity. Diverse regulatory pathways may work alone or in combination to fine-tune C4PPDK activity in response to changes in light
physiological function
-
PPDK regulatory protein (PDRP) regulates the phosphate-dependent activation and ADP-dependent inactivation of PPDK by reversible phosphorylation
physiological function
pyramiding expression of Zea mays genes encoding phosphoenolpyruvate carboxylase (PEPC) and pyruvate orthophosphate dikinase (PPDK) synergistically improve the photosynthetic characteristics of transgenic Triticum aestivum
physiological function
pyruvate phosphate dikinase (PPDK) is a diphosphate-dependent enzyme, which reversibly catalyzes conversion of phosphoenolpyruvate, diphosphate, and AMP into pyruvate, phosphate, and ATP. In trypanosomes, enzyme PPDK works in the glycolytic direction and participates in the maintenance of the glycosomal ATP/ADP balance. The glycosomal PPDK provides a metabolic flexibility by producing 2 ATP per phosphoenolpyruvate consumed. Role of enzyme PPDK in acetate production
physiological function
pyruvate phosphate dikinase is an auxiliary enzyme of glycolysis located in the glycosomes
physiological function
-
pyruvate phosphate dikinase reversibly catalyzes the interconversion of phosphoenolpyruvate and pyruvic acid, leading to catabolism and adenosine triphosphate (ATP) synthesis or gluconeogenesis and ATP consumption. The orientation of the phosphorylatable histidine residue within the central domain of PPDK determines whether this enzyme promotes catabolism or gluconeogenesis
physiological function
pyruvate phosphate dikinase reversibly catalyzes the interconversion of phosphoenolpyruvate and pyruvic acid, leading to catabolism and adenosine triphosphate (ATP) synthesis or gluconeogenesis and ATP consumption. The orientation of the phosphorylatable histidine residue within the central domain of PPDK determines whether this enzyme promotes catabolism or gluconeogenesis
physiological function
pyruvate phosphate dikinase reversibly catalyzes the interconversion of phosphoenolpyruvate and pyruvic acid, leading to catabolism and adenosine triphosphate (ATP) synthesis or gluconeogenesis and ATP consumption. The orientation of the phosphorylatable histidine residue within the central domain of PPDK determines whether this enzyme promotes catabolism or gluconeogenesis
physiological function
the diphosphate-dependent pyruvate phosphate dikinase, that converts phosphoenolpyruvate, diphosphate, and AMP into pyruvate, phosphate, and ATP, is the first enzyme of one branch of a two-branched glycolytic auxiliary system in glycosomes, thus contributing to the ATP/ADP balance within the glycosomes. During growth of epimastigotes in batch culture an apparent decrease in the specific activity of PPDK is observed
physiological function
-
the enzyme plays an important role in the maintenance of the ATP/ADP balance in glycosomes in this life-cycle stage of the parasite, as well as contributes in part to its glycolytic flux
physiological function
-
the enzyme PPDK is involved in the entry of alanine into the essential gluconeogenesis pathway in amastigotes. The majority of alanine enters into the pathway via decarboxylation of pyruvate in promastigotes. Also L-lactate, an abundant glucogenic precursor in mammals, is used by Leishmania amastigotes to synthesize mannogen, entering the pathway through PPDK
physiological function
-
Brucella suis biovar 5 depends on phosphoenolpyruvate carboxykinase and pyruvate phosphate dikinase for full virulence in laboratory models
physiological function
essential enzyme of C4 photosynthesis in plants
physiological function
essential enzyme of C4 photosynthetic pathway
physiological function
pyruvate phosphate dikinase modulates endosperm metabolism, potentially through reversible adjustments to energy charge
physiological function
the enzyme facilitates the survival of Manihot esculenta plants in response to abiotic stress
physiological function
the enzyme plays an important role in starch metabolism and structure in rice endosperm
physiological function
-
pyruvate phosphate dikinase (PPDK) is a diphosphate-dependent enzyme, which reversibly catalyzes conversion of phosphoenolpyruvate, diphosphate, and AMP into pyruvate, phosphate, and ATP. In trypanosomes, enzyme PPDK works in the glycolytic direction and participates in the maintenance of the glycosomal ATP/ADP balance. The glycosomal PPDK provides a metabolic flexibility by producing 2 ATP per phosphoenolpyruvate consumed. Role of enzyme PPDK in acetate production
-
physiological function
-
enzyme PPDK is involved in ATP homeostasis in Pseudomonas fluorescens, overview
-
physiological function
-
the enzyme PPDK is involved in the entry of alanine into the essential gluconeogenesis pathway in amastigotes. The majority of alanine enters into the pathway via decarboxylation of pyruvate in promastigotes. Also L-lactate, an abundant glucogenic precursor in mammals, is used by Leishmania amastigotes to synthesize mannogen, entering the pathway through PPDK
-
physiological function
-
pyruvate phosphate dikinase is an auxiliary enzyme of glycolysis located in the glycosomes
-
physiological function
-
Brucella suis biovar 5 depends on phosphoenolpyruvate carboxykinase and pyruvate phosphate dikinase for full virulence in laboratory models
-
physiological function
-
the enzyme facilitates the survival of Manihot esculenta plants in response to abiotic stress
-
physiological function
-
the enzyme plays an important role in the maintenance of the ATP/ADP balance in glycosomes in this life-cycle stage of the parasite, as well as contributes in part to its glycolytic flux
-
additional information
PPDK activities are insensitive to variation in PPDK levels, suggesting the rapid phosphorylation mechanism of this protein. The phosphorylation rate of the enzyme is increased at higher temperature of 31°C compared to control at 24°C
additional information
-
role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis
additional information
role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis
additional information
role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis
additional information
-
role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis
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S101F
-
a C to T single nucleotide polymorphism (SNP) in exon 2 of the gene encoding cytosolic pyruvate phosphate dikinase results in a change of serine to phenylalanine acid at amino acid position 101. The gene is named FLOURY ENDOSPERM 4-5 (FLO4-5). Co-segregation between the floury phenotype and the flo4-5 is observed. PPDK is expressed at considerably higher levels in the flo4-5 mutant than in the wild type during the grain filling stage
G525A
site-directed mutagenesis, the mutant shows no phosphorylation signal
G525P
site-directed mutagenesis, the mutant shows no phosphorylation signal
H529A
site-directed mutagenesis
S506A
site-directed mutagenesis
S528A
site-directed mutagenesis
S528C
site-directed mutagenesis, the mutant shows a phosphorylation signal only slightly weaker than the wild-type enzyme due to the tighter binding of S528 to G525 compared to C528
S528D
site-directed mutagenesis
S528T
site-directed mutagenesis, the mutant shows no phosphorylation signal
S528Y
site-directed mutagenesis, the mutant shows no phosphorylation signal
T309A
site-directed mutagenesis
T456S
-
111% activity with respect to wild type
T456V
-
98% activity with respect to wild type
T527A
site-directed mutagenesis
T527D
site-directed mutagenesis
R135A
-
partial activity, 15 mutant enzymes studied
R219E/E271R/S262D
site-directed mutagensis, comparison of mutant to wild-type enzyme structure
T456F
-
-
T456F
-
1% activity with respect to wild type
T456Y
-
-
T456Y
-
6% activity with respect to wild type
additional information
construction of an enzyme deletion mutant DELTAppdK from strain 2308, and of a double deletion mutant DELTApckADELTAppdK, also lacking phosphoenolpyruvate carboxykinase, both show a reduced growth phenotype, overview. But albeit impaired in growth, the DELTAppdK is still able to reach the replicative intracellular niche, but BABDELTAppdK fails to reach the chronic steady phase typical of virulent brucellae
additional information
-
construction of an enzyme deletion mutant DELTAppdK from strain 2308, and of a double deletion mutant DELTApckADELTAppdK, also lacking phosphoenolpyruvate carboxykinase, both show a reduced growth phenotype, overview. But albeit impaired in growth, the DELTAppdK is still able to reach the replicative intracellular niche, but BABDELTAppdK fails to reach the chronic steady phase typical of virulent brucellae
additional information
-
construction of an enzyme deletion mutant DELTAppdK from strain 2308, and of a double deletion mutant DELTApckADELTAppdK, also lacking phosphoenolpyruvate carboxykinase, both show a reduced growth phenotype, overview. But albeit impaired in growth, the DELTAppdK is still able to reach the replicative intracellular niche, but BABDELTAppdK fails to reach the chronic steady phase typical of virulent brucellae
-
additional information
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
-
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
-
generation of a DELTAppdk null mutant by recombinant homologous gene replacement with hygromycin B and phleomycin resistance markers. No difference in growth is observed between PPDK wild-type and null mutant parasite promastigotes, but the incorporation of precursors into storage compound mannogen changes in the mutant compared to wild-type, DELTAppdk promastigotes are able to incorporate 14C label into mannogen when they are incubated with alanine, glycerol, and aspartate. The label incorporation in wild-type and DELTAppdk promastigotes incubated with alanine is 98.6% and 78.9%, respectively
additional information
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generation of a DELTAppdk null mutant by recombinant homologous gene replacement with hygromycin B and phleomycin resistance markers. No difference in growth is observed between PPDK wild-type and null mutant parasite promastigotes, but the incorporation of precursors into storage compound mannogen changes in the mutant compared to wild-type, DELTAppdk promastigotes are able to incorporate 14C label into mannogen when they are incubated with alanine, glycerol, and aspartate. The label incorporation in wild-type and DELTAppdk promastigotes incubated with alanine is 98.6% and 78.9%, respectively
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additional information
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development of a bioluminescent assay method for diphosphate, detection applied to single-nucleotide polymorphism analysis using one-base extension reaction, overview
additional information
construction of a PPDK deletion mutant, DELTAppdk, and a DELTAppdk/DELTApepck double deletion mutant
additional information
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construction of a PPDK deletion mutant, DELTAppdk, and a DELTAppdk/DELTApepck double deletion mutant
additional information
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construction of a PPDK deletion mutant, DELTAppdk, and a DELTAppdk/DELTApepck double deletion mutant
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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
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direct pleiotropic effects of Opaque-2 mutation on PPDK, mechanism, epistatic relationship between PPDK and Opaque-2, detailed overview
additional information
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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
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25 kDa C-terminal and 35 kDa N-terminal deletion mutants expressed in Escherichia coli
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78% of homology with maize enzyme
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codon-optimized coding regions of PPDK from Flaveria trinervia stripped of the chloroplast transport sequence are cloned into the multiple cloning site of a pET-16b vector (Novagen) containing a His10 tag and coding for a Tobacco Etch Virus protease cleavage site. Escherichia coli BL21 (DE3) cells are transformed with this plasmid
Escherichia coli, strains DH5alpha and BL21-CodonPLUS(DE3)-RIL
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 a baculovirus system
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expressed in Arabidopsis thaliana, found exclusively in chloroplasts of transgenic Arabidopsis plants
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expressed in Escherichia coli
expressed in Nicotiana tabacum
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expressed in Oryza sativa subsp. indica cultivar IR64
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expression in Escherichia coli
expression of mutant enzyme R219E/E271R/S262D in Escherichia coli strain JM101
gene C4ppdkZm1, quantitative real-time PCR enzyme expression analysis, recombinant expression of tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (RIL)
gene CyppdkZm2, quantitative real-time PCR enzyme expression analysis
gene ppdK, expression analysis
gene PPDK, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview
gene ppdk, recombinant expression of His-tagged enzyme in Escherichia coli strain TG-1
gene ppdk, Triticum aestivum cv. Zhoumai19 immature embryosare transfected by particle bombardment with chimeric genes containing pepc or ppdk cDNA and the bialaphos resistance gene under the control of the Cauliflower mosaic virus 35S promoter. Three types of transgenic lines containing 1. pepc cDNA (PC lines), 2. ppdk cDNA (PK lines), or 3. both genes (PKC lines) are obtained through callus differentiation, phosphinthricine resistance screening, plantlet regeneration, and molecular detection. Quantitative real-time PCR enzyme expression analysis. Net photosynthetic rates of mutants are increased compared to controls
gene ppdk2 or ppdk1, recombinant His-tagged enzyme expression in Escherichia coli
genomic analysis of the glycolytic/gluconeogenic pathway, optimization of C-terminally His-tagged PPDK expression in Escherichia coli as soluble protein, overview
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heterologous expression in Escherichia coli strain BL21 (DE3)
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
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into the vector pUMP16M13
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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
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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
recombinant expression of soluble His-tagged enzyme in Escherichia coli strain BL21(DE3)
single copy gene LmxM11.1000, the LmxPPDK ORF is subcloned into pX63NeoRI, recombinant expression of N-terminally His6-tagged enzyme
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the 5' flanking sequence of PPDK is fused to the uidA reporter gene and stably transfected tobacco (Nicotiana benthamiana Domin)
the cloned sequence represents about 20% of the complete gene, and shows about 56% homology with enzymes from maize and Bacteroides symbiosus
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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
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expressed in Escherichia coli
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expressed in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli
gene PPDK, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview
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gene PPDK, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview
gene PPDK, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview
quantitative expression analysis of the enzyme during endosperm development, expression profiles, overview
quantitative expression analysis of the enzyme during endosperm development, expression profiles, overview
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quantitative real-time reverse transcription (RT)-PCR expression analysis during transfer of plants from 25C to 14C growth temperature
quantitative real-time reverse transcription (RT)-PCR expression analysis during transfer of plants from 25C to 14C growth temperature
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