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Information on EC 2.7.9.1 - pyruvate, phosphate dikinase and Organism(s) Entamoeba histolytica and UniProt Accession P37213
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EC Tree
2.7.9.1 pyruvate, phosphate dikinaseSpecify your search results
Word Map
- 2.7.9.1
- phosphoenolpyruvate
- carboxylase
- maize
- pep
- mesophyll
-
nadp-malic
-
carboxykinase
- rubisco
- ribulose-1,5-bisphosphate
- nadp-me
- symbiosum
- flaveria
-
crassulacean
-
kranz
- glycosomal
-
adp-dependent
-
1,5-bisphosphate
-
pyrophosphorylated
- brownii
-
4.1.1.31
- pepcase
-
c4-like
- trinervia
-
swiveling
- miscanthus
- crystallinum
- drug development
- diagnostics
- pharmacology
- analysis
- agriculture
-
c4-type
- mesembryanthemum
The taxonomic range for the selected organisms is: Entamoeba histolytica
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pyruvate orthophosphate dikinase, pyruvate phosphate dikinase, pyruvate pi dikinase, ppdk1, pyruvate-phosphate dikinase, c4-ppdk, osppdkb, ppdk2, cytosolic pyruvate orthophosphate dikinase, cyppdk, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PPDK
pyruvate, orthophosphate dikinase
-
-
-
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pyruvate, Pi dikinase
-
-
-
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pyruvate-inorganic phosphate dikinase
-
-
-
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pyruvate-phosphate dikinase
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-
-
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pyruvate-phosphate dikinase (phosphorylating)
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-
-
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pyruvate-phosphate ligase
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-
-
-
pyruvic-phosphate dikinase
-
-
-
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pyruvic-phosphate ligase
-
-
-
-
PPDK
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:pyruvate, phosphate phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY
9027-40-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
synthesis of ATP is not thermodynamically favorable in trophozoites of Entamoeba histolytica
-
-
?
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
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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-[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
-
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
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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
-
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-[5-(3-chloro-benzyl)-thiazol-2-yl]-3-[5-(2-methyl-cyclopropyl)-furan-2-yl]-propionamide
-
phosphate
-
inhibits rate of ATP synthesis at saturating and equimolar concentrations of phosphoenolpyruvate, AMP and diphosphate. Product inhibition versus phosphoenolpyruvate is uncompetitive
[3-methyl-7-(3-methyl-benzyl)-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-ylsulfanyl]-acetic acid benzyl ester
-
additional information
-
in silico docking studies to pyruvate phosphate dikinase of Entamoeba histolytica, ID number, structure and IUPAC names of top scored ligands
-
additional information
in silico docking studies to pyruvate phosphate dikinase of Entamoeba histolytica, ID number, structure and IUPAC names of top scored ligands
-
additional information
-
ligand binding and docking analysis, overview
-
additional information
ligand binding and docking analysis, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
pyruvate phosphate dikinase is an excretory-secretory protein
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PPDK_ENTHI
885
0
98060
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
additional information
-
modeling of the three-dimensional structure of the PPDK protein in a homology-modeling approach
additional information
modeling of the three-dimensional structure of the PPDK protein in a homology-modeling approach
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% v/v glycerol, optimal storage condition, decay factor is 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged soluble enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of soluble His-tagged enzyme in Escherichia coli strain BL21(DE3)
the cloned sequence represents about 20% of the complete gene, and shows about 56% homology with enzymes from maize and Bacteroides symbiosus
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
the enzyme is a potential diagnostic marker for amoebic liver abscess. Development of a lateral flow dipstick (LFD) test using recombinant PPDK enzyme and evaluation for serodiagnosis of amoebic liver abscess, enzyme detection using mouse anti-human IgG4, directed against the parasite enzyme, conjugated to colloidal gold, overview
pharmacology
drug design, in silico studies on stereo chemical quality of PPDK protein structure, interaction studies to identify promising ligands to inhibit the function of PPDK, possibility of using proposed ligands as inhibitors for intestinal infections caused by Entamoeba histolytica in humans and for related pathogens, virtual screening of ligands to inhibit PPDK by docking studies using compound input libraries, phylogenetic trees of pathogens as further targets for in silico drug design to inhibit PPDK
drug development
PPDK is a good target in design of antiparasitic agents
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Reeves, R.E.
A new enzyme with the glycolytic function of pyruvate kinase
J. Biol. Chem.
243
3202-3204
1968
Entamoeba histolytica
Saavedra Lira, E.; Robinson, O.; Perez Montfort, R.
Partial nucleotide sequence of the enzyme pyruvate, orthophosphate dikinase of Entamoeba histolytica
Arch. Med. Res.
23
39-40
1992
Entamoeba histolytica
Cooper, R.A.; Kornberg, H.L.
Phosphoenolpyruvate synthetase and pyruvate, phosphate dikinase
The Enzymes, 3rd Ed. (Boyer,P. D. , Ed. )
10
631-649
1974
Komagataeibacter xylinus, Arundinaria sp., [Clostridium] symbiosum, Entamoeba histolytica, Propionibacterium freudenreichii subsp. shermanii
-
Goss, N.H.; Wood, H.G.
Covalent chemistry of pyruvate, orthophosphate dikinase
Methods Enzymol.
87
51-66
1982
Komagataeibacter xylinus, [Clostridium] symbiosum, Entamoeba histolytica, Propionibacterium freudenreichii subsp. shermanii
Saavedra-Lira, E.; Ramirez-Silva, L.; Perez-Montfort, R.
Expression and characterization of recombinant pyruvate phosphate dikinase from Entamoeba histolytica
Biochim. Biophys. Acta
1382
47-54
1998
Entamoeba histolytica
Saavedra, E.; Encalada, R.; Pineda, E.; Jasso-Chavez, R.; Moreno-Sanchez, R.
Glycolysis in Entamoeba histolytica. Biochemical characterization of recombinant glycolytic enzymes and flux control analysis
FEBS J.
272
1767-1783
2005
Entamoeba histolytica
Varela-Gomez, M.; Moreno-Sanchez, R.; Pardo, J.P.; Perez-Montfort, R.
Kinetic mechanism and metabolic role of pyruvate phosphate dikinase from Entamoeba histolytica
J. Biol. Chem.
279
54124-54130
2004
Entamoeba histolytica
Stephen, P.; Vijayan, R.; Bhat, A.; Subbarao, N.; Bamezai, R.N.
Molecular modeling on pyruvate phosphate dikinase of Entamoeba histolytica and in silico virtual screening for novel inhibitors
J. Comput. Aided Mol. Des.
22
647-660
2008
Entamoeba histolytica, Entamoeba histolytica (P37213)
Saidin, S.; Yunus, M.H.; Zakaria, N.D.; Razak, K.A.; Huat, L.B.; Othman, N.; Noordin, R.
Production of recombinant Entamoeba histolytica pyruvate phosphate dikinase and its application in a lateral flow dipstick test for amoebic liver abscess
BMC Infect. Dis.
14
182
2014
Entamoeba histolytica (P37213), Entamoeba histolytica
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