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Information on EC 2.7.1.40 - pyruvate kinase
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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
- insulin
- hepatocytes
- glycogen
- anemia
- pep
-
carboxykinase
-
hemolytic
- creatine
-
gluconeogenesis
- aldolase
- malate
- diabetes
- citrate
- carboxylase
- adenylate
- glucokinase
-
warburg
- glyceraldehyde-3-phosphate
-
gluconeogenic
- phosphoglycerate
- glucagon
- 6-phosphate
- enolase
- pentose
-
malic
- fructose-1,6-bisphosphate
- reticulocyte
- isocitrate
-
lipogenic
-
lipogenesis
- 2,6-bisphosphate
- 6-phosphogluconate
- triose
- g6pase
- 2,3-diphosphoglycerate
-
liver-type
-
1,6-bisphosphatase
-
glycogenolysis
-
splenectomy
- fructose-6-phosphate
- dikinase
-
triosephosphate
-
calprotectin
- diagnostics
- biofuel production
- drug development
- medicine
-
spherocytosis
- nutrition
-
reticulocytosis
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Synonyms
ATP/pyruvate O'-phosphotransferase, ATP:pyruvate 2-O-phosphotransferase, CTHBP, cytosolic thyroid hormone binding protein, EhPK, erythroid (R-type) pyruvate kinase, fluorokinase, hL-PYK, hPKM2, kinase, fluoro- (phosphorylating), 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CTHBP
-
-
-
-
cytosolic thyroid hormone binding protein
-
-
-
-
fluorokinase
-
-
-
-
kinase, fluoro- (phosphorylating)
-
-
-
-
kinase, pyruvate (phosphorylating)
-
-
-
-
L-PK
-
-
-
-
M1-PK
M2-PK
MRSA PK
PAE0819
phosphoenol transphosphorylase
-
-
-
-
phosphoenolpyruvate kinase
phosphoenolpyruvate: ADP phosphotransferase
PK-S
PK1
PKC
PKM1
PKM2
PYK
Pyk1
PykA
PykF
PyKII
pyruvate kinase
pyruvate kinase 1
pyruvate kinase isoenzyme M2
pyruvate kinase M2
pyruvate kinase muscle isozyme
-
-
-
-
pyruvate kinase type M2
pyruvate phosphotransferase
pyruvic kinase
-
-
-
-
R-type/L-type pyruvate kinase
-
-
-
-
red cell/liver pyruvate kinase
-
-
-
-
SSO0981
THBP1
-
-
-
-
VEG17
-
-
-
-
vegetative protein 17
-
-
-
-
phosphoenolpyruvate kinase
-
-
-
-
PKM2
-
-
pyruvate kinase M2
-
-
pyruvate phosphotransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + pyruvate = ADP + phosphoenolpyruvate
UTP, GTP, CTP, ITP and dATP can also act as donors, also phosphorylates hydroxylamine and fluoride in the presence of CO2
-
-
-
ATP + pyruvate = ADP + phosphoenolpyruvate
catalyzes the addition of a proton and the loss of a phosphoryl group which is transferred to ADP
-
ATP + pyruvate = ADP + phosphoenolpyruvate
allosteric enzyme: homotropic
-
ATP + pyruvate = ADP + phosphoenolpyruvate
allosteric enzyme: homotropic
-
ATP + pyruvate = ADP + phosphoenolpyruvate
allosteric enzyme: homotropic
-
ATP + pyruvate = ADP + phosphoenolpyruvate
sigmoidal saturation curves with substrate and metal ions
-
ATP + pyruvate = ADP + phosphoenolpyruvate
model for allosteric regulation
Musa cavendishii
-
ATP + pyruvate = ADP + phosphoenolpyruvate
sigmoidal kinetics with respect to phosphoenolpyruvate
ATP + pyruvate = ADP + phosphoenolpyruvate
allosteric enzyme
ATP + pyruvate = ADP + phosphoenolpyruvate
compulsory-ordered tri-bi mechanism
-
ATP + pyruvate = ADP + phosphoenolpyruvate
modeling of the catalytic mechanism, overview
-
ATP + pyruvate = ADP + phosphoenolpyruvate
the kinetic mechanism is random order with a rapid equilibrium
ATP + pyruvate = ADP + phosphoenolpyruvate
allosteric enzyme: homotropic
-
-
ATP + pyruvate = ADP + phosphoenolpyruvate
allosteric enzyme: homotropic
Mycolicibacterium smegmatis CDC 46
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
1-butanol autotrophic biosynthesis (engineered), anaerobic energy metabolism (invertebrates, cytosol), Bifidobacterium shunt, Entner-Doudoroff pathway I, Entner-Doudoroff pathway II (non-phosphorylative), Entner-Doudoroff pathway III (semi-phosphorylative), gluconeogenesis II (Methanobacterium thermoautotrophicum), glycerol degradation to butanol, glycolysis I (from glucose 6-phosphate), glycolysis II (from fructose 6-phosphate), glycolysis III (from glucose), glycolysis IV (plant cytosol), glycolysis V (Pyrococcus), heterolactic fermentation, mixed acid fermentation, photosynthetic 3-hydroxybutanoate biosynthesis (engineered), Rubisco shunt, superpathway of glucose and xylose degradation
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9001-59-6
-
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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
ATP + AKT1S1
ADP + phospho-AKT1S1
-
the enzyme phosphorylates Ser202 and Ser203 of AKT1S1
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
100% activity with ADP
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
4 phosphoenolpyruvate-binding sites/enzyme molecule
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
-
poor substrates: UDP, GDP
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
physiological role
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
Cardium tuberculatum
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
-
final regulatory point in catabolic Embden-Meyerhoff-Parnas pathway
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
probably involved in supplying additional carbon-skeletons for ammonium assimilation
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
-
catalyzes the addition of a proton and the loss of a phosphoryl group which is transferred to ADP
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
-
no positive cooperativity for ADP
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
673438, 674082, 674499, 676298, 707450, 707493, 707838, 707871, 707908, 708196, 708214, 708378, 708661, 708734, 708759, 709010, 709228, 709286, 709379, 709464, 709909, 710022, 710034, 710047, 710048, 710210, 710648
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
as a function of increasing pH (pH 6.5-8.0), PYK's affinity for phosphoenolpyruvate decreases, while affinity for ATP slightly increases
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
involved in regulation of metabolism of an aerobic organism capable of net glucose synthesis
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
Musa cavendishii
-
ADP preferred substrate, UDP, IDP, GDP and CDP may also be used with lower effectivity
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
Mycolicibacterium smegmatis CDC 46
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
Mycolicibacterium smegmatis CDC 46
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
100% activity with ADP
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
rate-controlling enzyme of glycolytic flux
-
-
?
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
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
other nucleoside diphosphates can replace ADP with a different rank order of effectiveness for enzyme form I and II
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
641555, 641563, 641564, 641572, 661404, 661406, 674052, 675943, 706831, 707914, 708372, 709817, 710084
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
the enzyme catalyzes an important regulatory step in the glycolysis pathway, the main route that provides energy for brain function
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
the enzyme is essential for multicellular development: fruiting body formation is abolished in mutant strain and indole-induced spore formation is delayed
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
ADP preferred substrate, UDP, IDP, GDP and CDP may also be used with lower effectivity
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
the substrate binding order of the Thermofilum pendens enzyme is independent despite lacking an internal positive charge
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
-
isozyme M2-type acts as a ProTalpha kinase phosphorylating ProTalpha
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
-
in normal murine lymphocytes and in tumor cells M2-PK phosphorylates prothymosin alpha on a threonine
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
-
ProTalpha kinase activity
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
the enzyme catalyzes the final step of glycolysis
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
the enzyme catalyzes the final step of glycolysis
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
reaction at 25% the rate of ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
poor substrate
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
reaction with PKp-isozyme at 30%, with PKc-isozyme at 12% the rate of ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
Mycolicibacterium smegmatis CDC 46
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
dADP + phosphoenolpyruvate
dATP + pyruvate
-
23% activity compared to ADP
-
-
?
dADP + phosphoenolpyruvate
dATP + pyruvate
-
9.9% activity compared to ADP
-
-
?
dADP + phosphoenolpyruvate
dATP + pyruvate
-
26% activity compared to ADP
-
-
?
dCDP + phosphoenolpyruvate
dCTP + pyruvate
-
0.5% activity compared to ADP
-
-
?
dCDP + phosphoenolpyruvate
dCTP + pyruvate
-
0.082% activity compared to ADP
-
-
?
dCDP + phosphoenolpyruvate
dCTP + pyruvate
-
2.9% activity compared to ADP
-
-
?
dGDP + phosphoenolpyruvate
dGTP + pyruvate
-
10.2% activity compared to ADP
-
-
?
dGDP + phosphoenolpyruvate
dGTP + pyruvate
-
1.82% activity compared to ADP
-
-
?
dGDP + phosphoenolpyruvate
dGTP + pyruvate
-
44% activity compared to ADP
-
-
?
dTDP + phosphoenolpyruvate
dTTP + pyruvate
-
4.6% activity compared to ADP
-
-
?
dTDP + phosphoenolpyruvate
dTTP + pyruvate
-
0.035% activity compared to ADP
-
-
?
dTDP + phosphoenolpyruvate
dTTP + pyruvate
-
4.8% activity compared to ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
Cardium tuberculatum
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
reaction at 55% the rate of ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
reaction for PKc-isozyme at 71%, for PKp-isozyme at 39% the rate of ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
Cardium tuberculatum
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
reaction at 53% the rate of ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
reaction with PKp-isozyme at 20%, with PKc-isozyme at 89% the rate of ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
reaction at about 70% the rate of ADP, PKc-isozyme
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
reaction at about 31% the rate of ADP, PKp-isozyme
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
additional information
?
-
enzyme is confirmed by total proteome analysis of glycerol-grown cells
-
-
-
additional information
?
-
-
broad specificity for nucleoside diphosphates
-
-
-
additional information
?
-
-
allosteric enzyme: homotropic
-
-
-
additional information
?
-
-
pyruvate kinase M2 is a phosphotyrosine-binding protein
-
-
-
additional information
?
-
-
the SUMO-E3 ligase protein PIAS3 (inhibitor of activated STAT3) physically interacts with M2-PK and its isoenzyme M1-PK
-
-
-
additional information
?
-
mitogenic factor LPA, SUMO-E3 ligase, tumor endothelial marker-8, hepatitis C virus-NS5B RNA polymerase and HERC-1 via its HECT domain bind to isozyme PKM2
-
-
-
additional information
?
-
-
nuclear M2-PK participates in the phosphorylation of the epsilon-amino group of histone 1 by direct phosphate transfer from PEP without requiring ATP. M2-PK directly inters with different oncoproteins and components of the protein kinase cascade, such as HPV-16 E7, the tyrosine kinases pp60v-src, BCR-ABL, ETV6-NTRK3, FGFR-1, FLT3 and JAK-2, the serine/threonine kinase A-Raf, cytoplasmic promyelocytic leukemia tumor suppressor protein as well as phosphotyrosine peptides
-
-
-
additional information
?
-
-
the recombinant enzyme shows the following range in its substrate specificity: ADP>dADP>dGDP>dCDP>TDP
-
-
-
additional information
?
-
-
pyruvate kinase is a substrate of protein kinase A
-
-
-
additional information
?
-
-
pyruvate kinase is a substrate of protein kinase A
-
-
-
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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
ATP + AKT1S1
ADP + phospho-AKT1S1
-
the enzyme phosphorylates Ser202 and Ser203 of AKT1S1
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
physiological role
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
final regulatory point in catabolic Embden-Meyerhoff-Parnas pathway
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
-
probably involved in supplying additional carbon-skeletons for ammonium assimilation
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
involved in regulation of metabolism of an aerobic organism capable of net glucose synthesis
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
rate-controlling enzyme of glycolytic flux
-
-
?
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
-
the enzyme catalyzes an important regulatory step in the glycolysis pathway, the main route that provides energy for brain function
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
Q8GQS6
the enzyme is essential for multicellular development: fruiting body formation is abolished in mutant strain and indole-induced spore formation is delayed
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
-
in normal murine lymphocytes and in tumor cells M2-PK phosphorylates prothymosin alpha on a threonine
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
Q8ZYE0
the enzyme catalyzes the final step of glycolysis
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
Q8ZYE0
the enzyme catalyzes the final step of glycolysis
-
-
?
additional information
?
-
P14618
mitogenic factor LPA, SUMO-E3 ligase, tumor endothelial marker-8, hepatitis C virus-NS5B RNA polymerase and HERC-1 via its HECT domain bind to isozyme PKM2
-
-
-
additional information
?
-
-
nuclear M2-PK participates in the phosphorylation of the epsilon-amino group of histone 1 by direct phosphate transfer from PEP without requiring ATP. M2-PK directly inters with different oncoproteins and components of the protein kinase cascade, such as HPV-16 E7, the tyrosine kinases pp60v-src, BCR-ABL, ETV6-NTRK3, FGFR-1, FLT3 and JAK-2, the serine/threonine kinase A-Raf, cytoplasmic promyelocytic leukemia tumor suppressor protein as well as phosphotyrosine peptides
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
-
673438, 674082, 674499, 676298, 707274, 707450, 707493, 707838, 707871, 707908, 708196, 708214, 708378, 708661, 708734, 708759, 709010, 709228, 709286, 709379, 709464, 709909, 710022, 710034, 710047, 710048, 710210, 710648, 721787
ADP
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
-
multiphasical activation, at pH below physiological value, inhibits at physiological pH
Co2+
Cu2+
-
divalent cation required, at 1 mM Cu2+ activation results in 86% of the activity with Mg2+
divalent cation
Fe2+
-
the enzyme is dependent on Mn2+ ion for its activity. Fe2+ and Mg2+ show 70 and 20% of the Mn2+ activity, respectively. No activity is detected without metal or with Zn2+, Cu2+, Co2+, and Ni2+
K+
Mg2+
Mn2+
monovalent cation
Na+
NH4+
Ni2+
-
divalent cation required, at 1 mM Ni2+ activation results in 2% of the activity with Mg2+
sulfate
each monomer in the asymmetric unit of CpPyK binds two sulfate ions at equivalent positions, one in the C-domain and the other at the interface of the A and C domains, binding structure, overview. The sulfate ion in the C-domain occupies a position corresponding to the 6-phosphate of the effector molecule in different PyKs
Tl+
-
wild-type enzyme and the three mutant enzymes T298S, T298C and T298A show no measurable activity in the presence of K+ or Tl+. Tl+ can activate wild-type enzyme to 85% the activity in the presence of K+. With T298S, T298, and T298A, Tl+ is 1.2-1.8fold better activator than is K+ based on the measured turnover number values
Zn2+
additional information
Ca2+
-
divalent cation required, at 1 mM Ca2+ activation results in 14% of the activity with Mg2+
Ca2+
-
divalent cation required, at 1 mM Ca2+ activation results in 7% of the activity with Mg2+
Ca2+
-
divalent cation required, at 1 mM Ca2+ activation results in 3% of the activity with Mg2+
Co2+
-
divalent cation required, at 1 mM Co2+ activation results in 170% of the activity with Mg2+
Co2+
-
divalent cation required, at 1 mM Co2+ activation results in 80% of the activity with Mn2+
Co2+
-
multiphasical activation, at pH below physiological value, inhibits at physiological pH
Co2+
-
divalent cation required, at 1 mM Co2+ activation results in 120% of the activity with Mg2+
divalent cation
-
requirement; requires both a divalent and a monovalent cation
divalent cation
-
requirement; requires both a divalent and a monovalent cation
divalent cation
-
requirement; requires both a divalent and a monovalent cation
K+
-
apparent Km-value: 0.48 mM; only together with activating divalent cation
K+
-
best activator at optimal conditions, in decreasing order of efficiency: K+, Rb+, Cs+, Na+, NH4+, Li+; requirement
K+
-
essential activator, in the presence of K+ the affinities for phosphoenolpyruvate, ADP, ADP-Cr2+, and oxalate are 2-6fold higher than in the absence of K+ when ADP cannot bind to the enzyme until phosphoenolpyruvate forms a competent active site
K+
-
in aqueous media, muscle pyruvate kinase is highly selective for K+ over Na+. Dimethylsulfoxide favors the partition of K+ and Na+ into the monovalent and divalent cation binding sites of the enzyme. The kinetics of the enzyme at subsaturating concentrations of activators show that K+ and Mg2+ exhibit high selectivity for their respective cation binding sites, whereas when Na+ substitutes K+, Na+ and Mg2+ bind with high affinity to their incorrect sites. The ratio of the affnities of Mg2+ and K+ for the monovalent cation binding site is close to 200. For Na+ and Mg2+ this ratio is approximately 20. The data suggest that K+ induces conformational changes that prevent the binding of Mg2+ to the monovalent cation binding site
K+
-
K+ is directly involved in the acquisition of the active conformation and movement of the B domain of the enzyme
K+
-
Km-value: 50 mM in the presence of fructose diphosphate; requirement
K+
-
wild-type enzyme and the three mutant enzymes T298S, T298C and T298A show no measurable activity in the presence of K+ or Tl+
Mg2+
-
apparent Km-value: 0,21 mM; fulfills absolute requirement for divalent cation
Mg2+
-
fulfills absolute requirement for divalent cation; requirement
Mg2+
-
the enzyme is dependent on Mn2+ ion for its activity. Fe2+ and Mg2+ show 70 and 20% of the Mn2+ activity, respectively. No activity is detected without metal or with Zn2+, Cu2+, Co2+, and Ni2+
Mg2+
Musa cavendishii
-
fulfills absolute requirement for divalent cation; Km-value 0.27 mM, hyperbolic saturation kinetics
Mg2+
-
kinetics of the enzyme at subsaturating concentrations of activators show that K+ and Mg2+ exhibit high selectivity for their respective cation binding sites, whereas when Na+ substitutes K+, Na+ and Mg2+ bind with high affinity to their incorrect sites. The ratio of the affinities of Mg2+ and K+ for the monovalent cation binding site is close to 200. For Na+ and Mg2+ this ratio is approximately 20
Mg2+
-
addition of Mg2+ protects the enzyme completely from the ferrous ion-mediated inactivation
Mg2+
-
positive homotropic interaction with phosphoenolpyruvate and Mg2+
Mg2+
-
fulfills absolute requirement for divalent cation; Km-value 0.45 mM for isozyme PKc, 1.6 mM for isozyme PKp; requirement
Mg2+
-
Km-value 2 mM in the presence of fructose diphosphate; requirement
Mg2+
-
positive cooperativity; requirement
Mg2+
although the maximum activity is 3.8-fold higher with Mg2+ than with Mn2+, the K0.5 for Mn2+ is 250fold lower than the K0.5 for Mg2+, with no significant change in the constants for the substrates. This finding shows that Mn2+ is the preferred divalent cation, consistent with the geochemistry of the Archaean ocean
Mn2+
-
divalent cation required, at 1 mM Mn2+ activation results in 160% of the activity with Mg2+
Mn2+
-
divalent cation required, at 1 mM Mn2+ activation results in 63% of the activity with Mg2+
Mn2+
-
activation; best activator; the activity of the sugar phosphate-activated enzyme is reduced to 50% if Mn2+ is omitted
Mn2+
-
fulfills absolute requirement for divalent cation; Km-value 0.05 mM for isozyme PKc, 0.5 mM for isozyme PKp; requirement
Mn2+
-
Mn2+-activated T298C behaves like Mn2+-activated wild type enzyme with a Vmax that is 20% of that for the wild type enzyme with or without D-fructose-1,6-bisphosphate
Mn2+
although the maximum activity is 3.8-fold higher with Mg2+ than with Mn2+, the K0.5 for Mn2+ is 250fold lower than the K0.5 for Mg2+, with no significant change in the constants for the substrates. This finding shows that Mn2+ is the preferred divalent cation, consistent with the geochemistry of the Archaean ocean
Mn2+
-
divalent cation required, at 1 mM Mn2+ activation results in 35% of the activity with Mg2+
monovalent cation
-
requirement; requires both a divalent and a monovalent cation
monovalent cation
-
requirement; requires both a divalent and a monovalent cation
monovalent cation
-
in decreasing order of efficiency: K+, Rb+, Cs+, Na+, NH4+, Li+
monovalent cation
-
requirement; requires both a divalent and a monovalent cation
monovalent cation
-
requirement; requires both a divalent and a monovalent cation
Na+
-
in decreasing order of efficiency: K+, Rb+, Cs+, Na+, NH4+, Li+
Na+
-
in aqueous media, muscle pyruvate kinase is highly selective for K+ over Na+. Dimethylsulfoxide favors the partition of K+ and Na+ into the monovalent and divalent cation binding sites of the enzyme. The kinetics of the enzyme at subsaturating concentrations of activators show that K+ and Mg2+ exhibit high selectivity for their respective cation binding sites, whereas when Na+ substitutes K+, Na+ and Mg2+ bind with high affinity to their incorrect sites. The ratio of the affnities of Mg2+ and K+ for the monovalent cation binding site is close to 200. For Na+ and Mg2+ this ratio is approximately 20. The data suggest that K+ induces conformational hanges that prevent the binding of Mg2+ to the monovalent cation binding site
NH4+
-
in decreasing order of efficiency: K+, Rb+, Cs+, Na+, NH4+, Li+
NH4+
-
can replace K+; only together with activating divalent cation; requirement
Zn2+
-
divalent cation required, at 1 mM Zn2+ activation results in 11% of the activity with Mg2+
Zn2+
-
divalent cation required, at 1 mM Zn2+ activation results in 6.5% of the activity with Mg2+
Zn2+
-
divalent cation required, at 1 mM Zn2 activation results in 2.5% of the activity with Mg2+
additional information
-
K-type allosteric properties only in the presence of Mg2+, not Mn2+
additional information
-
absolute requirement for a bivalent and a monovalent cation with Mg2+ and K+ fulfilling this
additional information
-
absolute requirement for a bivalent and a monovalent cation with Mg2+ and K+ fulfilling this
additional information
Busycotypus canaliculatum
-
interacting effects of various activators and inhibitors
additional information
-
no activation by Cu2+, Ni2+; no activation by Sr2+
additional information
-
activity is independent of free Mg2+ concentration in the range 4-20 mM
additional information
Musa cavendishii
-
absolute requirement for a bivalent and a monovalent cation with Mg2+ and K+ fulfilling this
additional information
-
no activation by Ba2+; no activation by Cu2+, Ni2+
additional information
-
interaction of three Trp residues, Tr157, Trp481, and Trp514, with activating cations, overview. The majority of changes in tryptophan fluorescence signal from PK induced by the binding of activating cations come from Trp157. Interactions with Mg2+ and K+ lead to more exposed tryptophan residues of PK while interactions with phosphoenolpyruvate and ADP decrease solvent accessibility of the tryptophan residues
additional information
-
enzyme spectra in the absence and presence of activating cations, overview
additional information
-
1 mM Mg2+ does not shows significant activity. No activity is observed with Ca2+ and Zn2+
additional information
-
absolute requirement for a bivalent and a monovalent cation with Mg2+ and K+ fulfilling this
additional information
-
activity is independent of free Mg2+ concentration in the range 4-20 mM
additional information
-
absolute requirement for a bivalent and a monovalent cation with Mg2+ and K+ fulfilling this; no activation by Li+
additional information
the enzyme from Thermofilum pendens is K+-independent. Eukarya pyruvate kinases have glutamate at position 117 (numbered according to the rabbit muscle enzyme), whereas in Bacteria have either glutamate or lysine and in Archaea have other residues. Glutamate at this position makes pyruvate kinases K+-dependent, whereas lysine confers K+-independence because the positively charged residue substitutes for the monovalent cation charge. The enzyme from Thermofilum pendens has Val70 at the corresponding position
additional information
-
the enzyme from Thermofilum pendens is K+-independent. Eukarya pyruvate kinases have glutamate at position 117 (numbered according to the rabbit muscle enzyme), whereas in Bacteria have either glutamate or lysine and in Archaea have other residues. Glutamate at this position makes pyruvate kinases K+-dependent, whereas lysine confers K+-independence because the positively charged residue substitutes for the monovalent cation charge. The enzyme from Thermofilum pendens has Val70 at the corresponding position
additional information
-
1 mM Mg2+ does not shows significant activity. No activity is observed with Ca2+ and Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2'E)-2,2'-(1E,3E)-prop-1-en-1-yl-3-ylidenebis(1-butyl-5,6-dichloro-3-pentyl-2,3-dihydro-1H-benzimidazole)
-
86% inhibition at 0.03 mM
(2-[(1E)-1-[2-(5-bromo-2-hydroxybenzoyl)hydrazinylidene]ethyl]-1-methyl-1H-indol-6-yl)dibromanium
-
-
(2R,3S)-2-(3,4-diphenoxyphenyl)-3,5,7-triphenoxy-3,4-dihydro-2H-1-benzopyran
-
-
(5-bromo-2-hydroxyphenyl)([(E)-[1-(1-methyl-1H-indol-2-yl)ethylidene]amino]oxy)methanone
-
34% inhibition at 0.01 mM
(5-bromo-2-methoxyphenyl)([(E)-[1-(1-methyl-1H-indol-2-yl)ethylidene]amino]oxy)methanone
-
33% inhibition at 0.01 mM
(E)-5-bromo-2-hydroxy-N'-(1-(4,5,6-trifluoro-1Hindol-2-yl)ethylidene)benzohydrazide
-
-
(E)-5-bromo-2-hydroxy-N'-(1-(5-hydroxy-1H-indol-2-yl)ethylidene)benzohydrazide
-
-
(E)-5-bromo-2-hydroxy-N'-(1-(5-methoxy-1H-indol-2-yl)ethylidene)benzohydrazide
-
-
(E)-5-bromo-N'-(1-(4,5-difluoro-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
-
(E)-5-bromo-N'-(1-(5,6-difluoro-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
-
(E)-5-bromo-N'-(1-(5-bromo-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
-
(E)-5-bromo-N'-(1-(5-bromo-1H-indol-2-yl)propylidene)-2-hydroxybenzohydrazide
-
-
(E)-5-bromo-N'-(1-(5-chloro-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
-
(E)-5-bromo-N'-(1-(5-fluoro-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
-
(E)-5-bromo-N'-(1-(6-bromo-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
-
(E)-5-bromo-N'-(1-(7-fluoro-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
39% inhibition at 500 nM
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-2-hydroxy-5-chlorobenzohydrazide
-
36% inhibition at 0.001 mM
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-2-hydroxy-5-iodobenzohydrazide
-
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-3,5-dibromo-2-hydroxybenzohydrazide
-
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-3,5-dibromo-2-methoxybenzohydrazide
-
57% inhibition at 0.001 mM
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-4-bromo-2-hydroxybenzohydrazide
-
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-5-bromo-2-(prop-2-ynyloxy)benzohydrazide
-
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-5-bromo-2-hydroxy-4-methoxybenzohydrazide
-
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-5-bromo-2-hydroxybenzohydrazide
-
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-5-bromo-2-methoxybenzohydrazide
-
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)benzohydrazide
-
28% inhibition at 0.01 mM
(E)-N'-(1-(1H-indol-2-yl)ethylidene)picolinohydrazid
-
15% inhibition at 0.01 M
(E)-N'-(1-(1H-indol-2-yl)propylidene)-5-bromo-2-hydroxybenzohydrazide
-
crystal structure determination of the inhibitor compound
(E)-N'-[1-(1H-indol-2-yl)ethylidene]-2-hydroxy-3,5-diisopropylbenzohydrazide
-
40% inhibition at 0.01 mM
(E)-N'-[1-(1H-indol-2-yl)ethylidene]-5-bromo-2-ethoxybenzohydrazide
-
-
(E/Z)-N'-((1H-indol-2-yl)(phenyl)methylene)-5-bromo-2-hydroxybenzohydrazide
-
-
(Z)-N'-(1-(1H-indol-2-yl)-2,2-dimethylpropylidene)-5-bromo-2-hydroxybenzohydrazide
-
crystal structure determination of the inhibitor compound
2,4-dihydroxy-N'-[(E)-(2-hydroxy-6,7,8,9-tetrahydrodibenzo[b,d]furan-1-yl)methylidene]benzohydrazide
-
-
2-hydroxy-5-iodo-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
-
2-tetradecylglycidic acid
-
in mice treated with 2-tetradecylglycidic acid, hepatic pyruvate kinase mRNA levels are significantly decreased, whereas pyruvate dehydrogenase kinase isozyme 4 expression is 30fold increased
2-[(1E)-1-[2-[(5-bromo-2-methoxyphenyl)(dioxido-l6-sulfanylidene)methyl]hydrazinylidene]ethyl]-1H-indole
-
12% inhibition at 0.01 mM
2-[(1E)-1-[2-[(5-bromo-2-methoxyphenyl)(dioxido-l6-sulfanylidene)methyl]hydrazinylidene]ethyl]-4,5-difluoro-1H-indole
-
11% inhibition at 0.01 mM
3-(2,5-dimethylphenoxy)-1,2-benzothiazole 1,1-dioxide
-
a saccharin derivative, potent inhibitor, but a labile compound
3-hydroxy-N'-[(1E)-1-(1H-indol-2-yl)ethylidene]naphthalene-2-carbohydrazide
-
-
3-hydroxy-N'-[(1E)-1-(4,5,6-trifluoro-1-methyl-1H-indol-2-yl)ethylidene]naphthalene-2-carbohydrazide
-
-
3-hydroxy-N'-[(1E)-1-(4,5,6-trifluoro-1-methyl-1H-indol-2-yl)propylidene]naphthalene-2-carbohydrazide
-
-
3-hydroxy-N'-[(1E)-1-(4,5,6-trifluoro-1H-indol-2-yl)propylidene]naphthalene-2-carbohydrazide
-
-
3-[(2,5-dimethylphenyl)sulfanyl]-1,2-benzothiazole 1,1-dioxide
-
a stable sulfur derivative of 3-(2,5-dimethylphenoxy)-1,2-benzothiazole 1,1-dioxide
4-amino-2-methylnaphthalen-1-ol
-
i.e. vitamin K5, shows a significantly stronger potency to inhibit isozyme PKM2 than to inhibit isozymes PKM1 and PKL
4-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
611% inhibition at 500 nM
4-hydroxy-N'-(7-hydroxy-2,3-dihydro-8H-[1,4]dioxino[2,3-f]indol-8-yl)phthalazine-1-carbohydrazide
-
-
4-hydroxy-N'-[(1E)-1-(1H-indol-2-yl)ethylidene]-1,10-biphenyl-3-carbohydrazide
-
20% inhibition at 0.01 mM
4-[(1,1-dioxo-1,2-benzothiazol-3-yl)sulfanyl]benzoic acid
-
irreversible inhibitor, a saccharin derivative, reacts with an active-site lysine residue (Lys335), forming a covalent bond and sterically hindering the binding of ADP/ATP, covalent inhibitor mechanism, overview. Inhibition of LmPYK by the compound is time-dependent
4-[(4-[3-[(1-hydroxy-2-methylpropan-2-yl)sulfamoyl]-4-methylphenyl]phthalazin-1-yl)amino]-N-methylbenzamide
-
-
5-(2,5-dimethyl-1H-pyrrol-1-yl)-2-hydroxybenzoic acid
-
81% inhibition at 0.03 mM
5-bromo-2-(ethoxymethoxy)-N'-((1E)-1-(1H-indol-2-yl)ethylidene)benzohydrazide
-
-
5-bromo-2-hydroxy-4-methoxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
-
5-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-benzimidazol-2-yl)ethylidene]benzohydrazide
-
-
5-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
-
5-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)propylidene]benzohydrazide
-
-
5-bromo-2-hydroxy-N'-[(1E)-1-(1H-indol-2-yl)ethylidene]benzohydrazide
-
-
5-bromo-2-hydroxy-N'-[(1E)-1-(1H-indol-2-yl)propylidene]benzohydrazide
-
-
5-bromo-2-hydroxy-N'-[(1E)-1-(4,5,6-trifluoro-1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
-
5-bromo-2-hydroxy-N'-[(1E)-1-(5-hydroxy-1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
-
5-bromo-2-hydroxy-N'-[(1E)-1-(5-iodo-1H-indol-2-yl)ethylidene]benzohydrazide
-
-
5-bromo-2-hydroxy-N'-[(1E)-1-(5-methoxy-1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
54% inhibition at 0.001 mM
5-bromo-2-hydroxy-N'-[(1E)-1-[5-(trifluoromethyl)-1Hindol-2-yl]ethylidene]benzohydrazide
-
46% inhibition at 0.01 mM
5-bromo-2-hydroxy-N'-[(3E)-5-methyl-2-methylidene-1,2-dihydro-3H-indol-3-ylidene]benzohydrazide
-
-
5-bromo-2-hydroxy-N'-[(E)-(1-methyl-1H-indol-2-yl)(phenyl)methylidene]benzohydrazide
-
-
5-bromo-2-hydroxy-N'-[(E)-(1-methyl-1H-indol-2-yl)methylidene]benzohydrazide
-
-
5-bromo-N'-[(1E)-1-(1H-indol-2-yl)ethylidene]-2-methoxy-N-methylbenzohydrazide
-
33% inhibition at 0.001 mM
5-bromo-N'-[(1E)-1-(2,4-dihydroxyphenyl)ethylidene]-2-hydroxybenzohydrazide
-
-
5-bromo-N'-[(1E)-1-(4,5-difluoro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
-
5-bromo-N'-[(1E)-1-(5,6-difluoro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
-
5-bromo-N'-[(1E)-1-(5,6-difluoro-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
-
5-bromo-N'-[(1E)-1-(5-bromo-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
-
5-bromo-N'-[(1E)-1-(5-bromo-1-methyl-1H-indol-2-yl)propylidene]-2-hydroxybenzohydrazide
-
-
5-bromo-N'-[(1E)-1-(5-chloro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
-
5-bromo-N'-[(1E)-1-(5-fluoro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
-
5-bromo-N'-[(1E)-1-(6-bromo-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
-
5-bromo-N'-[(1E)-1-(6-chloro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
-
5-bromo-N'-[(1E)-1-(6-fluoro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
-
5-bromo-N'-[(1E)-1-(6-fluoro-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
-
5-bromo-N'-[(3E)-5-bromo-2-methylidene-1,2-dihydro-3H-indol-3-ylidene]-2-hydroxybenzohydrazide
-
-
A-Raf protein
proteins known for cellular growth and proliferation such as A-Raf and PML protein are known to downregulate PKM2 activity by interacting with it
-
Antibody
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to bovine type L-kinase leading to partial inactivation of type K-kinase, not type M-kinase, to bovine, chicken and salmon type M-kinases leading partial inactivation of type K-kinase, to bovine type M-kinase leading to partial inactivation of type M-kinase
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ascorbate
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treatment of rabbit muscle pyruvate kinase with 10 mM ascorbate causes an inactivation with the cleavage of peptide bond. The inactivation or fragmentation of the enzyme is prevented by addition of Mg2+, catalase, and mannitol, but ADP and PEP the substrates do not show any effect
Ba2+
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in decreasing order of inhibitory efficiency: Ni2+, Zn2+, Cu2+, Ca2+, Ba2+
cumene hydroperoxide
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1% residual activity after treatment with 17 mM cumene hydroperoxide at 50°C and pH 7 for 2 h
D-Fructose 1-phosphate
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allosteric inhibitor with a 40% reduction in the Vmax
D-glucose 1-phosphate
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allosteric inhibitor with a 40% reduction in the Vmax
EGMVLPTVWQPANWMCRLSN
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peptide aptamer placed within thioredoxin A. Aptamer specifically binds to M2 pyruvate kinase and shifts the isoenzyme into its low affinity dimeric conformation
EGQLRHWGWAWSLASQNFSI
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peptide aptamer placed within thioredoxin A. Aptamer specifically binds to M2 pyruvate kinase and shifts the isoenzyme into its low affinity dimeric conformation
FeSO4
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treatment of rabbit muscle pyruvate kinase with 0.02 mM FeSO4 causes an inactivation with the cleavage of peptide bond. The inactivation or fragmentation of the enzyme is prevented by addition of Mg2+, catalase, and mannitol, but ADP and PEP the substrates do not show any effect
glyoxylate
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5 mM, 79% of activity remaining; 5 mM, 83% of activity remaining
human papillomavirus-16 E7
causes dissociation of PKM2 tetramer into inactive dimer
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iso-citrate
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10 mM, 70% of activity remaining; 10 mM, 75% of activity remaining
menadione
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i.e. vitamin K3, shows a significantly stronger potency to inhibit isozyme PKM2 than to inhibit isozymes PKM1 and PKL
N'-[(1E)-1-(1,3-benzothiazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
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N'-[(1E)-1-(1,3-benzoxazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
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26% inhibition at 500 nM
N'-[(1E)-1-(1-benzothiophen-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
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N'-[(1E)-1-(1H-benzimidazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
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N'-[(1E)-1-(2,4-dihydroxyphenyl)ethylidene]-3-(5,6-dimethyl-1,3-dihydro-2H-isoindol-2-yl)benzohydrazide
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N'-[(1E)-1-(5-bromo-1-methyl-1H-indol-2-yl)ethylidene]-3-hydroxynaphthalene-2-carbohydrazide
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