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Information on EC 2.7.1.40 - pyruvate kinase and Organism(s) Plasmodium falciparum
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2.7.1.40 pyruvate kinaseIUBMB Comments
UTP, GTP, CTP, ITP and dATP can also act as donors. Also phosphorylates hydroxylamine and fluoride in the presence of CO2.
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Word Map
- 2.7.1.40
- hexokinase
-
phosphofructokinase
- erythrocyte
- fructose
- glucose-6-phosphate
- hepatocytes
- glycogen
- anemia
-
carboxykinase
-
gluconeogenesis
- aldolase
- pep
-
hemolytic
- malate
- citrate
- creatine
- glucokinase
- adenylate
- carboxylase
-
warburg
-
gluconeogenic
- enolase
- phosphoglycerate
- pentose
- 6-phosphate
-
malic
- glucagon
- glyceraldehyde-3-phosphate
- reticulocyte
-
lipogenesis
- 6-phosphogluconate
- fructose-1,6-bisphosphate
-
lipogenic
- 2,6-bisphosphate
- g6pase
-
1,6-bisphosphatase
-
liver-type
-
splenectomy
- hk2
- dikinase
-
glutaminolysis
-
calprotectin
- triose
- shikonin
- 2,3-diphosphoglycerate
- fructose-6-phosphate
-
glycogenolysis
- drug development
- medicine
- biofuel production
-
reticulocytosis
-
transfusion-dependent
-
spherocytosis
- nutrition
- diagnostics
The taxonomic range for the selected organisms is: Plasmodium falciparum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pyruvate kinase, m2-pk, pyruvate kinase m2, l-pk, pyk, tum2-pk, pyruvate kinase type m2, liver pyruvate kinase, pyruvate kinase m2 isoform, m2-pyruvate kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CTHBP
-
-
-
-
cytosolic thyroid hormone binding protein
-
-
-
-
fluorokinase
-
-
-
-
kinase, fluoro- (phosphorylating)
-
-
-
-
kinase, pyruvate (phosphorylating)
-
-
-
-
L-PK
-
-
-
-
phosphoenol transphosphorylase
-
-
-
-
phosphoenolpyruvate kinase
-
-
-
-
pyruvate kinase muscle isozyme
-
-
-
-
pyruvate phosphotransferase
-
-
-
-
pyruvic kinase
-
-
-
-
R-type/L-type pyruvate kinase
-
-
-
-
red cell/liver pyruvate kinase
-
-
-
-
THBP1
-
-
-
-
VEG17
-
-
-
-
vegetative protein 17
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:pyruvate 2-O-phosphotransferase
UTP, GTP, CTP, ITP and dATP can also act as donors. Also phosphorylates hydroxylamine and fluoride in the presence of CO2.
CAS REGISTRY NUMBER
COMMENTARY
9001-59-6
-
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
ADP + phosphoenolpyruvate
ATP + pyruvate
-
the enzyme is expressed during the intraerythrocytic-stage of its developlental cycle that may play important metabolic roles during infection
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
important role of pyruvate kinase during malarial infection
-
-
?
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
ADP + phosphoenolpyruvate
ATP + pyruvate
-
the enzyme is expressed during the intraerythrocytic-stage of its developlental cycle that may play important metabolic roles during infection
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
oxalate
the binding of glucose 6-phosphate and oxalate, which potentially lock the enzyme in its active state, increase the thermal stability of the enzyme
citrate
citrate at 2 mM inhibits GST-tagged PfPYK activity by over 90%, citrate slightly decreases the affinity for the PEP substrate, with no obvious change in the apparent kcat
additional information
no effects by fructose 1,6-bisphosphate or fructose 2,6-bisphosphate on the enzyme activity
-
additional information
-
no effects by fructose 1,6-bisphosphate or fructose 2,6-bisphosphate on the enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glucose 6-phosphate
G6P, an activator increasing the apparent maximal velocity of isozyme PYK-I, 1.5fold activation at 5 mM without affecting the affinity and cooperativity towards the PEP substrate. The binding of glucose 6-phosphate and oxalate, which potentially lock the enzyme in its active state, increase the thermal stability of the enzyme. PfPYK might be a V-type allosteric enzyme with respect to G6P. In silico docking of the activator G6P to the canonical effector site, the phosphate group of G6P forms a number of favorable interactions with the PO4-2 motif
additional information
-
enzyme is not affected by fructose-1,6-bisphosphate and glucose 6-phosphate
-
additional information
no effects by fructose 1,6-bisphosphate or fructose 2,6-bisphosphate on the enzyme activity
-
additional information
-
no effects by fructose 1,6-bisphosphate or fructose 2,6-bisphosphate on the enzyme activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00039
ADP
in presence of inhibitor suramin, pH and temperature not specified in the publication
additional information
additional information
allosteric mechanism and structural changes, overview
-
additional information
additional information
-
allosteric mechanism and structural changes, overview
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
type-II pyruvate kinase is involved in fatty acid type-II biosynthesis
additional information
additional information
comparisons of isozyme PYK-I structures in the active R-state and inactive T-state reveal a rock-and-lock allosteric mechanism regulated by rigid-body rotations of each subunit in the tetramer. It is likely that the GST-tag on the recombinant enzyme partially hinders or affects conformational changes occurring in the PfPYK-I tetramer, which are crucial for allosteric regulation. Structure-function analysis, overview
additional information
-
comparisons of isozyme PYK-I structures in the active R-state and inactive T-state reveal a rock-and-lock allosteric mechanism regulated by rigid-body rotations of each subunit in the tetramer. It is likely that the GST-tag on the recombinant enzyme partially hinders or affects conformational changes occurring in the PfPYK-I tetramer, which are crucial for allosteric regulation. Structure-function analysis, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified isozyme PYK-I in complex with substrate analogue oxalate, activator glucose 6-phosphate, and product ATP, hanging drop vapour diffusion method, mixing of 0.001 ml of protein solution and 500 nl of 20 mM ligand solution, with 0.0015 ml of reservoir solution containing 12% PEG 8000, 10-20% glycerol, 50 mM TEA, pH 7.2, 100 mM KCl, and 50 mM MgCl2, and equilibration against 1 ml of reservoir solution, X-ray diffraction structure determination and analysis, molecular replacement using the structure obtained from the deposited T-state PfPYK (PDB ID 3KHD) as template, molecular modelling
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the binding of glucose 6-phosphate and oxalate, which potentially lock the enzyme in its active state, increase the thermal stability of the enzyme
additional information
-
the binding of glucose 6-phosphate and oxalate, which potentially lock the enzyme in its active state, increase the thermal stability of the enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PF3D7_1037100, sequence comparisons, recombinant expression of GST-tagged enzyme in Escherichia coli. It is likely that the GST-tag partially hinders or affects conformational changes occurring in the PfPYK-I tetramer, which are crucial for allosteric regulation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chan, M.; Sim, T.S.
Functional analysis, overexpression, and kinetic characterization of pyruvate kinase from Plasmodium falciparum
Biochem. Biophys. Res. Commun.
326
188-196
2005
Plasmodium falciparum
Maeda, T.; Saito, T.; Harb, O.S.; Roos, D.S.; Takeo, S.; Suzuki, H.; Tsuboi, T.; Takeuchi, T.; Asai, T.
Pyruvate kinase type-II isozyme in Plasmodium falciparum localizes to the apicoplast
Parasitol. Int.
58
101-105
2009
Plasmodium falciparum (C6KTA4), Plasmodium falciparum
Zhong, W.; Li, K.; Cai, Q.; Guo, J.; Yuan, M.; Wong, Y.H.; Walkinshaw, M.D.; Fothergill-Gilmore, L.A.; Michels, P.A.M.; Dedon, P.C.; Lescar, J.
Pyruvate kinase from Plasmodium falciparum structural and kinetic insights into the allosteric mechanism
Biochem. Biophys. Res. Commun.
532
370-376
2020
Plasmodium falciparum (C6KTA4), Plasmodium falciparum
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