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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
- glycogen
- hepatocytes
- anemia
-
carboxykinase
-
hemolytic
- aldolase
- pep
-
gluconeogenesis
- malate
- citrate
- creatine
- adenylate
- glucokinase
- carboxylase
-
warburg
-
gluconeogenic
- phosphoglycerate
- pentose
- 6-phosphate
- enolase
- glucagon
-
malic
- glyceraldehyde-3-phosphate
- reticulocyte
-
lipogenesis
-
lipogenic
- fructose-1,6-bisphosphate
- 6-phosphogluconate
- 2,6-bisphosphate
- fructose-6-phosphate
-
glycogenolysis
- g6pase
-
splenectomy
-
calprotectin
-
liver-type
- triose
- dikinase
- shikonin
- hk2
- 2,3-diphosphoglycerate
-
glutaminolysis
-
1,6-bisphosphatase
- medicine
-
spherocytosis
-
transfusion-dependent
- diagnostics
- nutrition
-
reticulocytosis
- biofuel production
- drug development
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ATP/pyruvate O'-phosphotransferase, ATP:pyruvate 2-O-phosphotransferase, CPK, CPK1, cPK2, cPK3, cPK4, cPK5, CTHBP, cytosolic pyruvate kinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CTHBP
-
-
-
-
cytosolic thyroid hormone binding protein
-
-
-
-
fluorokinase
-
-
-
-
hPKM2
K+-dependent PK
K+-independent PK
kinase, fluoro- (phosphorylating)
-
-
-
-
kinase, pyruvate (phosphorylating)
-
-
-
-
L-PK
-
-
-
-
M1-PK
M1-PYK
M2-PK
MRSA PK
NCgl2008
NCgl2809
PAE0819
phosphoenol transphosphorylase
-
-
-
-
phosphoenolpyruvate kinase
phosphoenolpyruvate: ADP phosphotransferase
PK-S
PK1
PKC
PKM1
PKM2
PYK
Pyk1
Pyk2
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
-
-
-
-
Rv1617
SSO0981
TCIL3000_10_12020
TcoPYK
THBP1
-
-
-
-
VcIIPK
VcIPK
VC_0485
VC_2008
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
compulsory-ordered tri-bi mechanism
-
ATP + pyruvate = ADP + phosphoenolpyruvate
model for allosteric regulation
Musa cavendishii
-
ATP + pyruvate = ADP + phosphoenolpyruvate
allosteric enzyme
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 kinetics with respect to phosphoenolpyruvate
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
sigmoidal saturation curves with substrate and metal ions
-
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
Mycolicibacterium smegmatis CDC 46
-
-
ATP + pyruvate = ADP + phosphoenolpyruvate
allosteric enzyme: homotropic
-
-
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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, 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
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
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
-
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
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
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
-
-
641553, 673438, 674082, 674499, 676298, 707450, 707493, 707838, 707871, 707908, 708196, 708214, 708378, 708661, 708734, 708759, 709228, 709286, 709379, 709464, 709909, 710022, 710034, 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
-
-
-
?
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
-
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
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
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
-
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
-
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
?
-
-
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
?
-
-
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
?
-
direct physical binding through protein-protein interaction between PHD3 and PKM2 is observed. Homology three-dimensional model of PHD3/PKM2 complex
-
-
-
additional information
?
-
PKM2 during in vitro reconstitution potentially interacts with histone H3 of the 5'-FAM labelled nucleosome octamer core and forms a stable complex. PKM2 phosphorylates histone H3 at T11
-
-
-
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
-
-
-
?
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
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
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
-
-
-
?
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
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
-
-
-
?
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
the enzyme catalyzes the final step of glycolysis
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
the enzyme catalyzes the final step of glycolysis
-
-
?
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
?
-
-
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
?
-
direct physical binding through protein-protein interaction between PHD3 and PKM2 is observed. Homology three-dimensional model of PHD3/PKM2 complex
-
-
-
additional information
?
-
PKM2 during in vitro reconstitution potentially interacts with histone H3 of the 5'-FAM labelled nucleosome octamer core and forms a stable complex. PKM2 phosphorylates histone H3 at T11
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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+
Cs+
activates, at saturating concentrations of PEP3-, ADP-Mg complex and free Mg2+, the Km for Cs+ is 13.5 mM
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+
Rb+
activates, at saturating concentrations of PEP3-, ADP-Mg complex and free Mg2+, the Km for Rb+ is 5.9 mM
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+
-
multiphasical activation, at pH below physiological value, inhibits at physiological pH
Co2+
-
divalent cation required, at 1 mM Co2+ activation results in 80% of the activity with Mn2+
Co2+
-
divalent cation required, at 1 mM Co2+ activation results in 120% of the activity with Mg2+
K+
-
best activator at optimal conditions, in decreasing order of efficiency: K+, Rb+, Cs+, Na+, NH4+, Li+
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+
-
wild-type enzyme and the three mutant enzymes T298S, T298C and T298A show no measurable activity in the presence of K+ or Tl+
K+
-
activates, torpid PK is significantly more sensitive to KCl with a Ka that is 69% less than the corresponding Ka from the euthermic animal
K+
K117 isozyme requires K+, at saturating concentrations of PEP3-, ADP-Mg complex and free Mg2+, the Km for K+ is 8.5 mM
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+
-
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+
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
Mg2+
-
required, no difference between euthermic and torpid PK responses to MgCl2
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+
-
the activity of the sugar phosphate-activated enzyme is reduced to 50% if Mn2+ is omitted
Mn2+