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 hide
2.7.9.1
-
RECOMMENDED NAME
GeneOntology No.
pyruvate, phosphate dikinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
PATHWAY
BRENDA Link
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
-
-
L-glutamine biosynthesis III
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Pyruvate metabolism
-
-
C4 and CAM-carbon fixation
-
-
photosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:pyruvate, phosphate phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9027-40-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Arundinaria sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
anendosymbiont, Wolbachia sp. subsp. Brugia malayi
-
-
Manually annotated by BRENDA team
cv. World Beater
-
-
Manually annotated by BRENDA team
Crithidia sp.
-
-
-
Manually annotated by BRENDA team
barnyard grass
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Kalanchoe hildebrandtii
-
-
-
Manually annotated by BRENDA team
strain MHOM/GT/2001/U1103
UniProt
Manually annotated by BRENDA team
strain MHOM/GT/2001/U1103
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Euryarchaea, Archaeabacteria
SwissProt
Manually annotated by BRENDA team
a bioenergy feedstock grass
-
-
Manually annotated by BRENDA team
cv. W38
-
-
Manually annotated by BRENDA team
no activity in Prunus persica cv. Adriatica fruits
-
-
-
Manually annotated by BRENDA team
no activity in Solanum melongena cv. Black Enorma fruits
-
-
-
Manually annotated by BRENDA team
Nopalxochia ackermannii
-
-
-
Manually annotated by BRENDA team
cultivars 9311 and TXZ-25
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Crenarchaea, Archaeabacteria
SwissProt
Manually annotated by BRENDA team
strain S-1
-
-
Manually annotated by BRENDA team
strain S-1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Sedum prealtum
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Rhizobium
-
-
Manually annotated by BRENDA team
cv. Moneymaker
-
-
Manually annotated by BRENDA team
spinach
-
-
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
isolated from a patient with Chagas disease in acute phase
UniProt
Manually annotated by BRENDA team
isolated from a horse
-
-
Manually annotated by BRENDA team
isolated from a horse
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
ATP + PPDK central domain construct of residues 381-512 (Cent-I) + phosphate
?
show the reaction diagram
-
-
-
?
ATP + PPDK N-terminal domain construct of residues 1-340 (Tem-340) + phosphate
?
show the reaction diagram
-
-
-
?
ATP + PPDK N-terminal domain construct of residues 1-553 (Tem340-Cent-I) + phosphate
?
show the reaction diagram
-
-
-
?
ATP + pyruvate + arsenate
?
show the reaction diagram
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
show the reaction diagram
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na+
-
slight activation of the phosphoenol pyruvate formation
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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-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-(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-[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'-aminohexyl-5,7-dyhydroxyflavone
-
a potent competitive PPDK inhibitor with an IC50 value of 0.0016 mM
-
4'-aminopbutyl-5,7-dihydroxyflavone
-
displays selectivity for inhibition of PPDK versus other enzymes that utilize ATP and NAD+
-
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-[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
-
-
alpha-beta-methylene ATP
beta-gamma-methylene ATP
biphosphonate
-
mixed inhibition mechanism with respect to diphosphate
Bromoacetate
-
83% inhibition at 1 mM
Bromopyruvate
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
diphosphate
gamma(p-Arsenophenyl)-n-butyrate
ilimaquinone
Imidodiphosphate
-
competitive to diphosphate
iodoacetate
Methylene diphosphonate
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-ethylmaleimide
N-[5-(3-chloro-benzyl)-thiazol-2-yl]-3-[5-(2-methyl-cyclopropyl)-furan-2-yl]-propionamide
-
-
oxalate
p-chloromercuribenzoate
p-hydroxymercuribenzoate
phosphate
phosphoenolpyruvate
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
-
pyruvate
Sulfhydryl agents
-
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)
[3-methyl-7-(3-methyl-benzyl)-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-ylsulfanyl]-acetic acid benzyl ester
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
abscisic acid
-
induces production of the protein
ammonium
activates up to 2.6fold
mannitol
-
induces production of the protein
Polyethylene glycol
-
induces production of the protein
thiols
-
required for activity in solution
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.0013 - 0.02
AMP
0.004 - 8
ATP
0.017 - 3.5
diphosphate
0.0014 - 1.8
phosphate
0.02 - 0.5
phosphoenolpyruvate
0.025 - 305
pyruvate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
AMP
Trypanosoma cruzi
Q9GN79
recombinant enzyme, pH 8.3, temperature not specified in the publication
0.14
diphosphate
Trypanosoma cruzi
Q9GN79
recombinant enzyme, pH 8.3, temperature not specified in the publication
0.11 - 87
phosphoenolpyruvate
10 - 15
pyruvate
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016
4'-aminohexyl-5,7-dyhydroxyflavone
-
pH and temperature not specified in the publication
-
0.07
5'-adenylimidodiphosphate
-
pH 6.8, 25ºC
0.32
adenosine
-
pH 6.8, 25ºC
0.31
adenosine 5'-mono-O-phosphorothiolate
-
pH 6.8, 25ºC
0.13 - 0.32
AMP
0.036 - 17
ATP
0.32 - 0.55
diphosphate
8.7
GMP
-
pH 6.8, 25ºC
0.001 - 0.025
oxalate
6 - 88
phosphate
0.15 - 2
phosphoenolpyruvate
0.4 - 22.6
pyruvate
1.2
tetrasodium 1-hydroxyethylidene biphosphonate
-
pH 6.3, 25ºC
11
tetrasodium 1-hydroxymethylidene biphosphonate
-
pH 6.3, 25ºC
4.3
tetrasodium 1-hydroxynonane biphosphonate
-
pH 6.3, 25ºC
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29 - 0.292
ilimaquinone
0.04
unguinol
Zea mays
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0006
-
leaf enzyme extract, pH and temperature not specified in the publication
0.005
native enzyme in purified glycosomes, pH 8.3, temperature not specified in the publication
0.016
-
purified glycosomes, pH 7.2, 28°C
0.043
-
T456F mutant
0.067
-
inactive enzyme obtained from dark-grown plants
0.1 - 0.19
-
leaf enzyme extract, pH and temperature not specified in the publication
0.2
purified recombinant enzyme, pH 8.3, temperature not specified in the publication
0.24
-
T456Y mutant
1.2
-
measured at 30ºC
2.5
-
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
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
-
pyruvate formation
6.5 - 7
-
both directions of reaction
6.5 - 7.5
-
phosphoenolpyruvate formation
6.8 - 7
-
assay at
6.9
-
pyruvate formation
7 - 7.8
-
phosphoenolpyruvate formation
7.1
-
pyruvate formation
7.2 - 7.8
-
forward reaction, phosphoenolpyruvate formation
7.2 - 8
-
forward reaction, phosphoenolpyruvate formation
7.2
-
assay at
7.3
reverse reaction optimum
7.75
-
pyrosequencing by utilizing pyruvate phosphate dikinase, expressed onto bacterial magnetic particles, PPDK-BacMPs
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at
28
-
assay at
37
-
activity assay; pyrosequencing by utilizing pyruvate phosphate dikinase, expressed onto bacterial magnetic particles, PPDK-BacMPs
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
isoelectric focusing (pH range from 4 to 7), cytosolic CyPPDK 2
5.3
isoelectric focusing (pH range from 4 to 7), cytosolic CyPPDK 2
5.4
isoelectric focusing (pH range from 4 to 7), cytosolic CyPPDK 2
8.25
-
calculated
8.9
-
calculated
additional information
annotation of different isoforms of one of the two cytosolic isoforms of PPDK of maize
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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
-
the cytosolic isoform accumulates preferentially in the veins
Manually annotated by BRENDA team
-
-
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
additional information