Information on EC 2.7.1.40 - pyruvate kinase

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The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.7.1.40
-
RECOMMENDED NAME
GeneOntology No.
pyruvate kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
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
show the reaction diagram
mechanism
-
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
catalyzes the addition of a proton and the loss of a phosphoryl group which is transferred to ADP
-
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
allosteric enzyme: homotropic
-
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
allosteric enzyme: homotropic
-
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
allosteric enzyme: homotropic
-
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
sigmoidal saturation curves with substrate and metal ions
-
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
model for allosteric regulation
Musa cavendishii
-
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
sigmoidal kinetics with respect to phosphoenolpyruvate
Q10208
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
hyperbolic kinetics
-
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
allosteric enzyme
P51181
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
allosteric enzyme
P51182, -
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
compulsory-ordered tri-bi mechanism
-
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
modeling of the catalytic mechanism, overview
-
ATP + pyruvate = ADP + phosphoenolpyruvate
show the reaction diagram
allosteric enzyme: homotropic
Halobacterium salinarum 9, Mycobacterium smegmatis CDC
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
1-butanol autotrophic biosynthesis
-
anaerobic energy metabolism (invertebrates, cytosol)
-
Bifidobacterium shunt
-
Biosynthesis of secondary metabolites
-
Entner-Doudoroff pathway II (non-phosphorylative)
-
Entner-Doudoroff pathway III (semi-phosphorylative)
-
gluconeogenesis II (Methanobacterium thermoautotrophicum)
-
glucose and xylose degradation
-
glycerol degradation to butanol
-
Glycolysis / Gluconeogenesis
-
glycolysis I (from glucose-6P)
-
glycolysis II (from fructose-6P)
-
glycolysis III (from glucose)
-
glycolysis IV (plant cytosol)
-
glycolysis V (Pyrococcus)
-
glycolysis VI (metazoan)
-
heterolactic fermentation
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
mixed acid fermentation
-
photosynthetic 3-hydroxybutyrate biosynthesis
-
Purine metabolism
-
Pyruvate metabolism
-
respiration (anaerobic)
-
Rubisco shunt
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ATP/pyruvate O'-phosphotransferase
-
-
ATP:pyruvate 2-O-phosphotransferase
-
-
CTHBP
-
-
-
-
cytosolic thyroid hormone binding protein
-
-
-
-
erythroid (R-type) pyruvate kinase
-
-
fluorokinase
-
-
-
-
hL-PYK
-
-
hPKM2
-
pyruvate kinase isoenzyme M2
kinase, fluoro- (phosphorylating)
-
-
-
-
kinase, pyruvate (phosphorylating)
-
-
-
-
L-PK
-
-
-
-
L-PYK
P30613
-
M1-PK
-
isozyme
M2 pyruvate kinase
-
-
M2 type phosphoenolpyruvate kinase
-
-
M2-PK
-
isozyme
M2-PK
-
M2 isoform of pyruvate kinase
M2-pyruvate kinase
-
-
M2-type pyruvate kinase
-
-
MRSA PK
Q6GG09
-
MRSA PK
Staphylococcus aureus RN4220
Q6GG09
-
-
phosphoenol transphosphorylase
-
-
-
-
phosphoenolpyruvate kinase
-
-
-
-
phosphoenolpyruvate kinase
O44006
-
phosphoenolpyruvate kinase
Eimeria tenella PaPt36
O44006
-
-
phosphoenolpyruvate kinase
-
-
phosphoenolpyruvate kinase
-
-
phosphoenolpyruvate kinase
-
-
phosphoenolpyruvate kinase
-
-
PK-alphabeta1
-
-
PK-alphabeta2
-
-
PK-M1
-
-
PK-M2
-
-
PK-S
-
-
PK-S
-
sperm-specific pyruvate kinase isoform
PK1
Q969A2
-
PK3
-
isoform
Pklr
-
-
PKM1
-
splice isoform of pyruvate kinase
PKM1
-
adult pyruvate kinase isoform
PKM2
-
less active isoenzyme
PKM2
-
splice isoform of pyruvate kinase
PKM2
P14618
-
PKM2
-
embryonic pyruvate kinase isoform
ProTalphaK
-
-
PYK
Bacillus subtilis 168
-
;
-
PYK
Brassica juncea Pusa Bold
-
-
-
PYK
Escherichia coli JM101, Escherichia coli K-12 W3110
-
-
-
Pyk1
Saccharomyces cerevisiae JT20454
-
-
-
PykA
Yersinia enterocolitica WA-314
-
-
-
PykF
Yersinia enterocolitica WA-314
-
-
-
pyruvate kinase
P14618
-
pyruvate kinase
Trichosporonoides megachiliensis
-
-
pyruvate kinase 1
-
-
pyruvate kinase 1
Saccharomyces cerevisiae JT20454
-
-
-
pyruvate kinase isoenzyme M2
-
-
pyruvate kinase isoenzyme M2
-
-
pyruvate kinase isozyme M1
-
-
pyruvate kinase isozyme type M2
-
-
pyruvate kinase M1
-
splice isoform of pyruvate kinase
pyruvate kinase M2
-
isozyme
pyruvate kinase M2
-
splice isoform of pyruvate kinase
pyruvate kinase M2
P14618
-
pyruvate kinase M2
-
-
pyruvate kinase muscle isozyme
-
-
-
-
pyruvate kinase type M2
-
-
pyruvate kinase type M2
-
-
pyruvate kinase type-II
-
-
pyruvate phosphotransferase
-
-
-
-
pyruvic kinase
-
-
-
-
R-type pyruvate kinase
-
-
R-type/L-type pyruvate kinase
-
-
-
-
red cell/liver pyruvate kinase
-
-
-
-
THBP1
-
-
-
-
TuM2-PK
-
-
tumor cell specific pyruvate kinase isozyme M2
-
-
tumour M2-PK
-
-
tumour M2-pyruvate kinase
-
-
VEG17
-
-
-
-
vegetative protein 17
-
-
-
-
vesicle-associated pyruvate kinase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-59-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Amaranthus sp.
-
-
-
Manually annotated by BRENDA team
American eel, kinase resembles mammalian M2-isozyme
-
-
Manually annotated by BRENDA team
Antarctic fish
-
-
-
Manually annotated by BRENDA team
strain 7324
-
-
Manually annotated by BRENDA team
Archaeoglobus fulgidus 7324
-
-
-
Manually annotated by BRENDA team
Archaeoglobus fulgidus 7324
strain 7324
-
-
Manually annotated by BRENDA team
Bacillus licheniformis A-5
A-5
-
-
Manually annotated by BRENDA team
strain ATCC 19213
-
-
Manually annotated by BRENDA team
strain ATCC 21616
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168
-
-
Manually annotated by BRENDA team
Brassica juncea Pusa Bold
-
-
-
Manually annotated by BRENDA team
PKc, cytosolic form
-
-
Manually annotated by BRENDA team
PKp, plastidic form
-
-
Manually annotated by BRENDA team
Busycotypus canaliculatum
-
-
-
Manually annotated by BRENDA team
Busycotypus canaliculatum
channelled whelk, gastropod mollusc
-
-
Manually annotated by BRENDA team
Cardium tuberculatum
cockle
-
-
Manually annotated by BRENDA team
Loenberg, ice-fish
-
-
Manually annotated by BRENDA team
Adriatic mollusc
-
-
Manually annotated by BRENDA team
chickpea
-
-
Manually annotated by BRENDA team
strain ATCC 13032 lysCfbr
-
-
Manually annotated by BRENDA team
sea bass, marine teleost
-
-
Manually annotated by BRENDA team
strain PaPt36
SwissProt
Manually annotated by BRENDA team
Eimeria tenella PaPt36
strain PaPt36
SwissProt
Manually annotated by BRENDA team
wild-type strain WG 096 (yA2, paba A1) and transformant 9/402
-
-
Manually annotated by BRENDA team
rumen ciliates
-
-
Manually annotated by BRENDA team
isoform M1
UniProt
Manually annotated by BRENDA team
isoform M2
UniProt
Manually annotated by BRENDA team
isozyme PK1; gene pykF
UniProt
Manually annotated by BRENDA team
isozyme PK2; gene pykA
UniProt
Manually annotated by BRENDA team
isozymes PykA and PykF encoded by genes pykA and pykF
-
-
Manually annotated by BRENDA team
strain JM101
-
-
Manually annotated by BRENDA team
strain K12 or B <45,60>
-
-
Manually annotated by BRENDA team
Escherichia coli JM101
strain JM101
-
-
Manually annotated by BRENDA team
Escherichia coli K-12 W3110
isozymes PykA and PykF encoded by genes pykA and pykF
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12 or B <45,60>
-
-
Manually annotated by BRENDA team
Abyssinian and Somali cat breeds
-
-
Manually annotated by BRENDA team
Abyssinian cat and Somali cat breeds
-
-
Manually annotated by BRENDA team
Gluconacetobacter xylinus
-
-
-
Manually annotated by BRENDA team
Halobacterium salinarum 9
strain 9
-
-
Manually annotated by BRENDA team
four isozymes
UniProt
Manually annotated by BRENDA team
isoform M2
UniProt
Manually annotated by BRENDA team
isoform M2
-
-
Manually annotated by BRENDA team
isozyme L
UniProt
Manually annotated by BRENDA team
M2 isoform
-
-
Manually annotated by BRENDA team
patients with colorectal adenomas
-
-
Manually annotated by BRENDA team
type 1 diabetic patients with and without nephropathy
UniProt
Manually annotated by BRENDA team
African land tortoise
-
-
Manually annotated by BRENDA team
strain C10
-
-
Manually annotated by BRENDA team
Lactococcus lactis C10
strain C10
-
-
Manually annotated by BRENDA team
nordic krill, isoforms PK I and PK II
-
-
Manually annotated by BRENDA team
crustacean
-
-
Manually annotated by BRENDA team
green alga
-
-
Manually annotated by BRENDA team
dimorphic phycomycete
-
-
Manually annotated by BRENDA team
erythrocyte-specific pyruvate kinase gene PKLR
-
-
Manually annotated by BRENDA team
Musa cavendishii
banana
-
-
Manually annotated by BRENDA team
strain CDC 46
-
-
Manually annotated by BRENDA team
Mycobacterium smegmatis CDC
strain CDC 46
-
-
Manually annotated by BRENDA team
no activity in Clostridium thermocellum
-
-
-
Manually annotated by BRENDA team
coho salmon
-
-
Manually annotated by BRENDA team
chlorophyll-free mutant No. 20
-
-
Manually annotated by BRENDA team
Alaskan king crab
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
flounder
-
-
Manually annotated by BRENDA team
grass frog
-
-
Manually annotated by BRENDA team
adult albino; female Wistar
-
-
Manually annotated by BRENDA team
adult albino; male Donryu
-
-
Manually annotated by BRENDA team
fed with vitamin E-replete and -defcient diet
-
-
Manually annotated by BRENDA team
strain CBS 14
-
-
Manually annotated by BRENDA team
Rhodosporidium toruloides CBS 14
strain CBS 14
-
-
Manually annotated by BRENDA team
castor bean, var. Baker 296
-
-
Manually annotated by BRENDA team
cv. Hale
-
-
Manually annotated by BRENDA team
isoform Pka
-
-
Manually annotated by BRENDA team
Budweiser baker's yeast
-
-
Manually annotated by BRENDA team
diverse strains, overview. Gene CDC19, i.e. HTG2
-
-
Manually annotated by BRENDA team
isoform Pyk2p
-
-
Manually annotated by BRENDA team
strain JT20454
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae JT20454
strain JT20454
-
-
Manually annotated by BRENDA team
strain LT-2, highest activity in cells grown on glycolytic substrates, e.g. glucose, galactose, fructose or glycerol
-
-
Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium LT-2
strain LT-2, highest activity in cells grown on glycolytic substrates, e.g. glucose, galactose, fructose or glycerol
-
-
Manually annotated by BRENDA team
fission yeast
-
-
Manually annotated by BRENDA team
ruminal bacterium
Uniprot
Manually annotated by BRENDA team
Gilthead bream
-
-
Manually annotated by BRENDA team
a methicillin-resistant strain
-
-
Manually annotated by BRENDA team
a methicillin-resistant strain, gene pyk
UniProt
Manually annotated by BRENDA team
Staphylococcus aureus RN4220
a methicillin-resistant strain, gene pyk
UniProt
Manually annotated by BRENDA team
genes encoding pyruvate kinase and phosphofructokinase are cotranscribed and their expression is regulated at the transcriptional level in response to the sugars supplied
-
-
Manually annotated by BRENDA team
strain JC2
-
-
Manually annotated by BRENDA team
Streptococcus mutans JC2
strain JC2
-
-
Manually annotated by BRENDA team
M1 isozyme
-
-
Manually annotated by BRENDA team
cyanobacterium, strain PCC 6301
-
-
Manually annotated by BRENDA team
coleoptera, larvae
-
-
Manually annotated by BRENDA team
archaebacterium
-
-
Manually annotated by BRENDA team
Trichosporonoides megachiliensis
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
Trichosporonoides megachiliensis SN-G42
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
strain K-100
-
-
Manually annotated by BRENDA team
Trypanoplasma borreli K-100
strain K-100
-
-
Manually annotated by BRENDA team
mung bean
-
-
Manually annotated by BRENDA team
dimorphic yeast
Uniprot
Manually annotated by BRENDA team
isozymes PykA and PykF encoded by genes pykA and pykF
-
-
Manually annotated by BRENDA team
Yersinia enterocolitica WA-314
isozymes PykA and PykF encoded by genes pykA and pykF
-
-
Manually annotated by BRENDA team
strain ATCC 31821
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
Q6GG09
significant evolutionary distance existing between the type I and type II isoenzymes in Gram-negative bacteria
evolution
Staphylococcus aureus RN4220
-
significant evolutionary distance existing between the type I and type II isoenzymes in Gram-negative bacteria
-
malfunction
-
FcepsilonRI-mediated inhibition of M2-type PK is required for mast cell degranulation
malfunction
-
M2-PK inhibition rescues cells from glucose starvation-induced apoptotic cell death by increasing the metabolic activity
malfunction
-
the pyruvate kinase-deficient co-isogenic mouse strain CBAPk-1slc is protected against Babesia rodhaini infection
malfunction
-
pyruvate kinase-deficient Escherichia coli exhibits increased plasmid copy number and cyclic AMP levels
malfunction
-
erythrocytes from individuals with pyruvate kinase deficiency are resistant to invasion by Plasmodium falciparum parasites, and erythrocytes infected with ring-stage parasites are preferentially cleared by macrophages in vitro
malfunction
-
pyruvate kinase deficiency provides protection against infection and replication of Plasmodium falciparum in human erythrocytes
malfunction
Q6GG09
the catalytic activities of the C-terminally truncated mutant toward both phophoenolpyruvate and ADP are profoundly decreased compared to those of wild-type enzyme
malfunction
P30613
human liver pyruvate kinase shows reduced affinity for phosphoenolpyruvate several days after cell lysis because Cys436 is oxidized, an effect of aging. The side chain of residue 436 is energetically coupled to phosphoenolpyruvate binding, overview
malfunction
-
missense mutations of M2-PK are described in the lymphocytes of an Indian Bloom syndrome patient. Inhibition of M2-PK isdirectly linked with the initiation of mast cell degranulation
malfunction
-
consequence of PKM2 inhibition is a reduced glycolytic flux, which can be reflected by the rates of cellular glucose consumption and lactate production
malfunction
-
the absence of extracellular serine and glycine has a pronounced inhibitory effect on pyruvate kinase activity
malfunction
P14618
PKM2 inhibition accumulates all upstream glycolytic intermediates as an anabolic feed for synthesis of lipids and nucleic acids. Downregulation of the enzyme activity by either phosphorylation or dissociation into dimer blocks the pyruvate production and leads in turn to an accumulation of the synthetic precursors to activate nucleic acid and lipid biosynthesis, required for cell division. The reduced cellular ATP amount as a result of PKM2 inactivation possibly activates TIGAR protein through AMPK-p53 pathway
malfunction
Escherichia coli JM101
-
pyruvate kinase-deficient Escherichia coli exhibits increased plasmid copy number and cyclic AMP levels
-
malfunction
Staphylococcus aureus RN4220
-
the catalytic activities of the C-terminally truncated mutant toward both phophoenolpyruvate and ADP are profoundly decreased compared to those of wild-type enzyme
-
metabolism
-
the embryonic pyruvate kinase isoform PKM2 is almost universally re-expressed in cancer and promotes aerobic glycolysis, whereas the adult isoform PKM1 promotes oxidative phosphorylation
metabolism
C6KTA4
type-II pyruvate kinase is involved in fatty acid type-II biosynthesis
metabolism
-
pyruvate kinase is a critical protein catalyzing the final step of glycolysis, which involves the transfer of a phosphoryl group from phosphoenolpyruvate to ADP, producing pyruvate and ATP
metabolism
-
pyruvate kinase is a crucial regulatory enzyme involved in glycolysis
metabolism
-
phosphoenolpyruvate enters the aromatic amino acids biosynthesis, metabolic flux distribution and Pyk activity in wild-type strain W3110 and in modified strains VH33, VH34 and VH35, overview
metabolism
-
low pyruvate kinase activity can drive serine and glycine biosynthesis, important link between key metabolic processes observed in cancer, namely preferential PKM2 expression, aerobic glycolysis and serine biosynthesis
metabolism
-
CDC19 or HTG2 is involved in the phenotype of high-temperature growth
metabolism
-
pyruvate kinase catalyzes the final step in glycolysis converting phosphoenolpyruvate to pyruvate, it is a central metabolic regulator
metabolism
-
in the absence of serine, an allosteric activator of PKM2, glycolytic efflux to lactate is significantly reduced in PKM2-expressing cells. This inhibition of PKM2 results in the accumulation of glycolytic intermediates that feed into serine synthesis. the GCN2-ATF4, general control nonderepressible 2 kinase-activating transcription factor 4, pathway collaborates with PKM2-dependent alterations in glycolytic metabolism to coordinate serine synthesis
metabolism
P14618
pyruvate kinase catalyzes the last but rate-limiting step of glycolysis
metabolism
Brassica juncea Pusa Bold
-
pyruvate kinase is a crucial regulatory enzyme involved in glycolysis
-
physiological function
Trichosporonoides megachiliensis
-
part of citric acid cycle
physiological function
-
suppressor of cytokine signaling 3 interacts with M2-PK to decrease ATP production causing dendritic cell dysfunction
physiological function
-
M2-PK is a metabolic sensor which regulates cell proliferation, cell growth and apoptotic cell death in a glucose supply-dependent manner
physiological function
-
pyruvate kinase and annexin I expressed by nerve growth factor contributes to granule formation containing TNF-alpha as well as other mediators in mast cells, which play a major role in allergic diseases via a TrkA/ERK pathway
physiological function
-
Oct-4-mediated transcriptional activity is positively regulated by PKM2
physiological function
-
PKM1 expression reduces the tumorigenicity of lung cancer cells, the M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth, the switch to the M2 isoform of pyruvate kinase in tumour cells is necessary to cause the metabolic phenotype known as the Warburg effect, PKM2 knockdown is rescued by expression of PKM1 in vitro
physiological function
-
vesicle-associated pyruvate kinase can support vesicular glutamate and other neurotransmitter uptake in the presence of its substrates
physiological function
Q3S1N4
pyruvate kinase plays a crucial role in the regulation of pyruvate levels as well as the level of the alternative oxidase in heterotrophic plant tissue
physiological function
-
PKM2 enhances the use of glycolytic intermediates for macromolecular biosynthesis and tumor growth, PKM2 can clearly contribute to the development of aerobic glycolysis and the Warburg effect
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
-
PYK plays a central role in a number of proliferative and infectious diseases
physiological function
Q6GG09
the C-terminal domain is not required for substrate binding or allosteric regulation observed in the holoenzyme, the kinetic efficiency of the truncated enzyme is decreased by 24 and 16fold, in ligand-free state, toward phophoenolpyruvate and ADP, respectively, but is restored by 3fold in AMP-bound state. The C-terminal domain (Gly473-Leu585) plays a substantial role in enzyme activity and comformational stability, and the C-terminal domain is involved in maintaining the specificity of allosteric regulation
physiological function
-
required role of the active site in allosteric regulation involving substrate binding, requirement for monovalent and divalent cations, overview
physiological function
-
acquisition of ProTalpha kinase activity by M2 isozyme seems to be due to the phosphorylation of serine and threonine residues, which, besides being essential for its catalytic activity, induces a trimeric association of ProTalpha kinase. Cytosolic phosphorylation of ProTaalpha, which then migrates to the nucleus, where it influences chromatin activity
physiological function
-
pyruvate kinase is a glycolytic enzyme catalyzing the ATP regenerating dephosphorylation of phosphoenolpyruvate to pyruvate. Pyruvate kinase is responsible for net ATP production within the glycolytic sequence. Besides its role as glycolytic enzyme M2-PK may also function as protein kinase. In tumor metabolism the quaternary structure of M2-PK (tetramer:dimer ratio) determines whether glucose is used for glycolytic energy regeneration (highly active tetrameric form, Warburg effect) or synthesis of cell building blocks (nearly inactive dimeric form) which are both prerequisites for cells with a high proliferation rate. In tumor cells the nearly inactive dimeric form of M2-PK is predominant due to direct interactions with different oncoproteins. Besides its key functions in tumor metabolism, M2-PK may also react as protein kinase as well as co activator of transcription factors. The mTOR/HIF-1a/c-myc/M2-PK cascade may be one explanation for the increased aerobic glycolysis in tumor cells first described by Otto Warburg, overview. Nuclear translocation of M2-PK by the somatostatin analogue TT232, H2O2 or UV light are linked to the induction of caspase independent apoptosis. M2-PK binds to the mast cell IgE receptor FcepsilonRI and plays a crucial role in responses to allergens
physiological function
-
pyruvate kinase is a glycolytic enzyme catalyzing the ATP regenerating dephosphorylation of phosphoenolpyruvate to pyruvate. Pyruvate kinase is responsible for net ATP production within the glycolytic sequence. Besides its role as glycolytic enzyme M2-PK may also function as protein kinase
physiological function
-
the expression of the M2 isozyme of pyruvate kinase plays an important role in the anabolic metabolism of cancer cells
physiological function
-
the Warburg effect, a metabolic change, originates from a shift in the expression of alternative spliced isoforms of the glycolytic enzyme pyruvate kinase, from PKM1 to PKM2. While PKM1 is constitutively active, PKM2 is switched from an inactive dimer form to an active tetramer form by small molecule activators. Activation of PKM2 may counter the abnormal cellular metabolism in cancer cells, and consequently decreased cellular proliferation
physiological function
-
pyruvate kinase isozyme PKM2 is a rate-limiting enzyme of aerobic glycolysis in cancer cells and plays important roles in cancer metabolism and growth. Vitamin K3/vitamin K5-enhanced toxicity of doxorubicin is associated with pyruvate kinase activity
physiological function
-
pyruvate kinase triggers a metabolic feedback loop that controls redox metabolism in respiring cells. Low PYK activity activates yeast respiration, the central metabolism is self-adapting to synchronize redox metabolism when respiration is activated. A metabolic feedback loop is responsible for preventing an increase in reactive oxygen species upon respiration activation. Low PYK enzyme activity causes accumulation of phosphoenolpyruvate, which in turn inhibits triose phosphate isomerase, an enzyme of upper glycolysis. This inhibition of triose phosphate isomerase increases metabolite content of the pentose phosphate pathway, a catabolic pathway closely connected to glycolysis. The PYK-PEP-TPI feedback loop protects cells from ROS-induced damage during respiration, metabolic mechanism, overview
physiological function
-
catalytic allosteric mechanism, overview
physiological function
-
the enzyme uses a rock and lock model allosteric mechanism, intersubunit interactions on the A-A and C-C interfaces strongly influence the allosteric effect whereas mutations affecting the intrasubunit A-C interface are less sensitive, overview. Conformational changes coupled with effector binding correlate with loss of flexibility and increase in thermal stability providing a general mechanism for allosteric control
physiological function
-
phosphoenolpyruvate is a key central metabolism intermediate that participates in glucose transport, as precursor in several biosynthetic pathways and it is involved in allosteric regulation of glycolytic enzymes
physiological function
-, Q5CSM7
pyruvate kinase of Cryptosporidium parvum is exceptional among known enzymes of protozoan origin in that it exhibits no allosteric property in the presence of commonly known effector molecules, mainly phosphosugars, due to blockage of the effector binding site by a sulfate ion, overview
physiological function
-
PKM2-expressing cells can maintain mammalian target of rapamycin complex 1 activity and proliferate in serine-depleted medium, but PKM1-expressing cells cannot. Pyruvate kinase M2 promotes de novo serine synthesis to sustain mTORC1 activity and cell proliferation upon serine depletion, mTOR is a key molecular sensor for nutrient availability and a regulator of cell growth and proliferation. PKM2 confers rsistance to proliferation arrest under serine starvation, tumor cells use serine-dependent regulation of PKM2 and GCN2 to modulate the flux of glycolytic intermediates in support of cell proliferation, overview
physiological function
P14618
tetrameric isozyme PKM2 is an allosterically regulated isoform and intrinsically designed to downregulate its activity by subunit dissociation from tetramer to dimer, which results in partial inhibition of glycolysis at the last step. Reassociation of PKM2 into active tetramer replenishes the normal catabolism as a feedback after cell division. PKM2 is a metabolic regulator, involvement of this enzyme in a variety of pathways, protein-protein interactions, and nuclear transport suggests its potential to perform multiple nonglycolytic functions with diverse implications, overview. Downregulation of the enzyme activity by either phosphorylation or dissociation into dimer blocks the pyruvate production and leads in turn to an accumulation of the synthetic precursors to activate nucleic acid and lipid biosynthesis, required for cell division PKM2 saves the cell from nutritional stress-dependent apoptosis during cell division process
physiological function
Escherichia coli K-12 W3110
-
phosphoenolpyruvate is a key central metabolism intermediate that participates in glucose transport, as precursor in several biosynthetic pathways and it is involved in allosteric regulation of glycolytic enzymes
-
physiological function
Staphylococcus aureus RN4220
-
the C-terminal domain is not required for substrate binding or allosteric regulation observed in the holoenzyme, the kinetic efficiency of the truncated enzyme is decreased by 24 and 16fold, in ligand-free state, toward phophoenolpyruvate and ADP, respectively, but is restored by 3fold in AMP-bound state. The C-terminal domain (Gly473-Leu585) plays a substantial role in enzyme activity and comformational stability, and the C-terminal domain is involved in maintaining the specificity of allosteric regulation
-
metabolism
Escherichia coli K-12 W3110
-
phosphoenolpyruvate enters the aromatic amino acids biosynthesis, metabolic flux distribution and Pyk activity in wild-type strain W3110 and in modified strains VH33, VH34 and VH35, overview
-
additional information
Q6GG09
the C-terminally truncated enzyme exhibits high affinity toward both phophoenolpyruvate and ADP and exhibits hyperbolic kinetics toward phophoenolpyruvate in the presence of activators AMP and ribose 5-phosphate consistent with kinetic properties of full-length enzyme
additional information
-
allosteric mechanism of rM1-PYK, overview
additional information
P30613
energetic coupling between an oxidizable cysteine and the phosphorylatable N-terminus of human liver pyruvate kinase determines substrate affinity and activity, overview. Oxidation of Cys436 and phosphorylation of the N-terminus at Ser12 may function through a similar mechanism, namely the interruption of an activating interaction between the nonphosphorylated N-terminus with the nonoxidized main body of the protein. Modeling of C436M-L-PYK-citrate-Mn-ATP-Fru-1,6-bisphosphate complex using crystal structure of S12D mutant in a S12D-L-PYK-Fru-1,6-bisphosphate-Mn-Na-citrate complex, overview
additional information
-
expression of M2-PK is under the control of nutrients, insulin, different transcription factors such as SP1, SP3, HIF-1alpha, as well as c-myc, the zonula occludens protein 2 (ZO-2), Ras and microRNA 133a and 133b
additional information
-
movement of the B domain is essential for the catalytic reaction. Rotation of the B domain in the opening of the cleft between domains B and A induced by the binding of activating cations allows substrates to bind, whereas substrate binding shifts the rotation of the B domain in the closure of the cleft. The enzyme exhibits a more dynamic structure after binding of activating metal ions and substrates, whereas binding of Phe decreases the dynamics
additional information
-
catalysis by muscle pyruvate kinase involves domain movements and conformational changes induced by activating cations and its substrates. Fluorescence acrylamide quenching analyses reveal that interactions with Mg2+ and K+ lead to a more exposed active site of the enzyme while interactions with phosphoenolpyruvate and ADP decrease solvent accessibility of the active site, overview
additional information
-
the transition between inactive T-state and active R-state is accompanied by a simple symmetrical 6o rigid body rocking motion of the A- and C-domain cores in each of the four subunits. Eight essential salt bridge locks form across the C-C interface providing tetramer rigidity with a coupled 7fold increase in reaction rate
additional information
-
allosteric site structure and regulation, overview. Comparison of the B domain open and closed conformation shows reorientation of the monomers with a concomitant change in the buried surface among adjacent monomers. The change in the buried surface is associated with significant B domain movements in one of the interacting monomers. A loop in the interface between the A and B domains plays an important role linking the position of the B domain to the buried surface among monomers through two alpha-helices. An unusual ordered conformation is observed in one of the allosteric binding domains, it is related to a specific apicomplexan insertion
additional information
-, Q5CSM7
the partially closed active site structure contains an alpha6' helix that unwinds and assumes an extended conformation, a glycerol molecule is located near the gamma-phosphate site of ATP. A sulfate ion is found at a site that is occupied by a phosphate of the effector molecule
additional information
Staphylococcus aureus RN4220
-
the C-terminally truncated enzyme exhibits high affinity toward both phophoenolpyruvate and ADP and exhibits hyperbolic kinetics toward phophoenolpyruvate in the presence of activators AMP and ribose 5-phosphate consistent with kinetic properties of full-length enzyme
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
P14618
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
P11974
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Amaranthus sp.
-
-
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Q3S1N4
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Q5F2M7
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
P30614
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Pigeon
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Q9LBS6, -
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
C6KTA4
-
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Gluconacetobacter xylinus
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Busycotypus canaliculatum
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Q8GQS6, -
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Q969A2
-
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Antarctic fish
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Q10208
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
P51182, -
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
P51181
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-, Q27686
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
4 phosphoenolpyruvate-binding sites/enzyme molecule
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
no positive cooperativity for ADP
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
ADP preferred substrate, UDP, IDP, GDP and CDP may also be used with lower effectivity
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Musa cavendishii
-
ADP preferred substrate, UDP, IDP, GDP and CDP may also be used with lower effectivity
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
no allosteric activation
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
poor substrates: UDP, GDP
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
best nucleoside diphosphate substrate
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
other nucleoside diphosphates can replace ADP with a different rank order of effectiveness for enzyme form I and II
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
catalyzes the addition of a proton and the loss of a phosphoryl group which is transferred to ADP
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Cardium tuberculatum
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
positive cooperativity for phosphoenolpyruvate
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
involved in regulation of metabolism of an aerobic organism capable of net glucose synthesis
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Cardium tuberculatum
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
allosteric enzyme
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
key enzyme in glycolysis
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
final regulatory point in catabolic Embden-Meyerhoff-Parnas pathway
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
rate-controlling enzyme of glycolytic flux
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
probably involved in supplying additional carbon-skeletons for ammonium assimilation
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
the enzyme catalyzes an important regulatory step in the glycolysis pathway, the main route that provides energy for brain function
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Q8GQS6, -
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
show the reaction diagram
-
the enzyme is expressed during the intraerythrocytic-stage of its developlental cycle that may play important metabolic roles during infection, important role of pyruvate kinase during malarial infection
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
100% activity with ADP
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Bacillus subtilis 168
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Streptococcus mutans JC2
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Saccharomyces cerevisiae JT20454
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Trypanoplasma borreli K-100
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Escherichia coli JM101
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Halobacterium salinarum 9
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Rhodosporidium toruloides CBS 14
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Bacillus licheniformis A-5
-
positive cooperativity for phosphoenolpyruvate, allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Escherichia coli K12
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Escherichia coli K12
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Lactococcus lactis C10
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Mycobacterium smegmatis CDC
-
best nucleoside diphosphate substrate, positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium LT-2
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
show the reaction diagram
-
-
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
show the reaction diagram
-
in normal murine lymphocytes and in tumor cells M2-PK phosphorylates prothymosin alpha on a threonine
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
show the reaction diagram
-
isozyme M2-type acts as a ProTalpha kinase phosphorylating ProTalpha
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
show the reaction diagram
-
ProTalpha kinase activity
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
P14618
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
P30613
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
Q6GG09
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
C6UXB6, P0AD62
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-, Q5CSM7
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
Escherichia coli K-12 W3110
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
Yersinia enterocolitica WA-314
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
Brassica juncea Pusa Bold
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
Staphylococcus aureus RN4220
Q6GG09
-
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
poor substrate
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
poor substrate
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
reaction at 25% the rate of ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
-
reaction with PKp-isozyme at 30%, with PKc-isozyme at 12% the rate of ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
Streptococcus mutans JC2
-
poor substrate, less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
show the reaction diagram
Mycobacterium smegmatis CDC
-
less effective than ADP
-
-
?
dADP + phosphoenolpyruvate
dATP + pyruvate
show the reaction diagram
-
23% activity compared to ADP
-
-
?
dADP + phosphoenolpyruvate
dATP + pyruvate
show the reaction diagram
-
26% activity compared to ADP
-
-
?
dADP + phosphoenolpyruvate
dATP + pyruvate
show the reaction diagram
-
9.9% activity compared to ADP
-
-
?
dCDP + phosphoenolpyruvate
dCTP + pyruvate
show the reaction diagram
-
0.082% activity compared to ADP
-
-
?
dCDP + phosphoenolpyruvate
dCTP + pyruvate
show the reaction diagram
-
0.5% activity compared to ADP
-
-
?
dCDP + phosphoenolpyruvate
dCTP + pyruvate
show the reaction diagram
-
2.9% activity compared to ADP
-
-
?
dGDP + phosphoenolpyruvate
dGTP + pyruvate
show the reaction diagram
-
1.82% activity compared to ADP
-
-
?
dGDP + phosphoenolpyruvate
dGTP + pyruvate
show the reaction diagram
-
10.2% activity compared to ADP
-
-
?
dGDP + phosphoenolpyruvate
dGTP + pyruvate
show the reaction diagram
-
44% activity compared to ADP
-
-
?
dTDP + phosphoenolpyruvate
dTTP + pyruvate
show the reaction diagram
-
0.035% activity compared to ADP
-
-
?
dTDP + phosphoenolpyruvate
dTTP + pyruvate
show the reaction diagram
-
4.6% activity compared to ADP
-
-
?
dTDP + phosphoenolpyruvate
dTTP + pyruvate
show the reaction diagram
-
4.8% activity compared to ADP
-
-
?
epsilon-ADP + phosphoenolpyruvate
?
show the reaction diagram
-
poor substrate
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
-
-
-
-
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
-
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
Cardium tuberculatum
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
reaction at 55% the rate of ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
reaction for PKc-isozyme at 71%, for PKp-isozyme at 39% the rate of ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
preference for GDP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
Streptococcus mutans JC2
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
Lactococcus lactis C10
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
-
-
-
-
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
-
-
-
-
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
-
-
-
-
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
-
-
-
-
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
-
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
-
-
-
-
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
Cardium tuberculatum
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
reaction with PKp-isozyme at 20%, with PKc-isozyme at 89% the rate of ADP
-
-
?
TDP + phosphoenolpyruvate
TTP + pyruvate
show the reaction diagram
-
poor substrate
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
-
reaction at about 70% the rate of ADP, PKc-isozyme
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
-
reaction at about 31% the rate of ADP, PKp-isozyme
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
show the reaction diagram
Streptococcus mutans JC2
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
show the reaction diagram
-
reaction at 53% the rate of ADP
-
-
?
additional information
?
-
-
preferred: purine nucleotides
-
-
-
additional information
?
-
-
broad specificity for nucleoside diphosphates
-
-
-
additional information
?
-
-
allosteric enzyme: homotropic
-
-
-
additional information
?
-
-
allosteric enzyme: homotropic
-
-
-
additional information
?
-
-
allosteric enzyme: homotropic
-
-
-
additional information
?
-
-
pyruvate kinase is a substrate of protein kinase A
-
-
-
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
?
-
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
-
-
-
additional information
?
-
Saccharomyces cerevisiae JT20454
-
pyruvate kinase is a substrate of protein kinase A
-
-
-
additional information
?
-
Halobacterium salinarum 9
-
allosteric enzyme: homotropic
-
-
-
additional information
?
-
Escherichia coli K12
-
specificity overview
-
-
-
additional information
?
-
Mycobacterium smegmatis CDC
-
allosteric enzyme: homotropic
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
C6KTA4
-
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
involved in regulation of metabolism of an aerobic organism capable of net glucose synthesis
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Cardium tuberculatum
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
allosteric enzyme
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
key enzyme in glycolysis
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
final regulatory point in catabolic Embden-Meyerhoff-Parnas pathway
-
-
-
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
rate-controlling enzyme of glycolytic flux
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
probably involved in supplying additional carbon-skeletons for ammonium assimilation
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
the enzyme catalyzes an important regulatory step in the glycolysis pathway, the main route that provides energy for brain function
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Q8GQS6, -
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
show the reaction diagram
-
the enzyme is expressed during the intraerythrocytic-stage of its developlental cycle that may play important metabolic roles during infection
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Escherichia coli JM101
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
Bacillus licheniformis A-5
-
allosteric enzyme
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
show the reaction diagram
-
-
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
show the reaction diagram
-
in normal murine lymphocytes and in tumor cells M2-PK phosphorylates prothymosin alpha on a threonine
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
P14618
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
P30613
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
Q6GG09
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
C6UXB6, P0AD62
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-, Q5CSM7
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
Escherichia coli K-12 W3110
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
Yersinia enterocolitica WA-314
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
Brassica juncea Pusa Bold
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
Staphylococcus aureus RN4220
Q6GG09
-
-
-
?
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
-
pyruvate kinase activity is not observed in the absence of ADP
AMP
-
activation
AMP
-
activation; enzyme form I
AMP
-
activation; not at physiological concentrations
AMP
-
allosteric effector
AMP
-
allosteric effector
AMP
-
allosteric effector
ATP
-
activation; below 4 mM, inhibits above 5 mM
ATP
-
activation; isozyme PK II
ATP
C6UXB6, P0AD62
;
CMP
-
activation
CMP
-
activation; allosteric
GDP
-
activation
GDP
-
activation; allosteric
GMP
-
activation
GMP
-
activation; allosteric
UDP
-
activation
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activation
Ca2+
-
activation at low Mg2+ and low Ca2+-concentration
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+
Cd2+
-
multiphasical activation, at pH below physiological value, inhibits at physiological pH
Co2+
-
multiphasical activation, at pH below physiological value, inhibits at physiological pH
Co2+
-
activation
Co2+
-
can replace Mg2+; requirement
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+
-
divalent cation required, at 1 mM Co2+ activation results in 120% of the activity with Mg2+
Cu2+
-
divalent cation required, at 1 mM Cu2+ activation results in 86% of the activity with Mg2+
Divalent cation
-
requirement; requires both a divalent and a monovalent cation
Divalent cation
-
requirement
Divalent cation
-
requirement
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+
-
activation; strong
K+
-
activation
K+
Cardium tuberculatum
-
requirement
K+
-
activation
K+
-
activation
K+
-
activation
K+
-
Km-value: 50 mM in the presence of fructose diphosphate; requirement
K+
-
as good as NH4+; requirement
K+
-
1 cation per active site; requirement
K+
Busycotypus canaliculatum
-
-
K+
-
fulfills requirement for monovalent cation
K+
-
inhibits above 100 mM; requirement
K+
-
best activator at optimal conditions, in decreasing order of efficiency: K+, Rb+, Cs+, Na+, NH4+, Li+; requirement
K+
-
Km-value 1.6 mM; requirement
K+
-
only together with activating divalent cation; requirement
K+
-
apparent Km-value: 0.48 mM; only together with activating divalent cation
K+
Musa cavendishii
-
Km-value 0.91 mM, hyperbolic saturation kinetics; requirement
K+
Q10208
requirement
K+
-
only together with activating divalent cation
K+
-
fulfills requirement for monovalent cation
K+
-
requirement
K+
Q9LBS6, -
activates
K+
-
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+
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+
-
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+
-
strict requirement
K+
-
binds at the active site
K+
-
K+ is directly involved in the acquisition of the active conformation and movement of the B domain of the enzyme
K+
-
required
Mg
-
required for activity
Mg2+
-
kinetics; requirement
Mg2+
-
fulfills absolute requirement for divalent cation; requirement
Mg2+
-
kinetics; requirement
Mg2+
-
requirement
Mg2+
Pigeon
-
activation
Mg2+
-
activation
Mg2+
-
requirement
Mg2+
-
Km-value: 0.8 mM
Mg2+
-
positive homotropic interaction with phosphoenolpyruvate and Mg2+
Mg2+
-
requirement
Mg2+
-
activation
Mg2+
-
activation; pH-dependent
Mg2+
-
activation; kinetics
Mg2+
-
requirement
Mg2+
-
-
Mg2+
-
Km-value 2 mM in the presence of fructose diphosphate; requirement
Mg2+
-
activation
Mg2+
-
no activity in the absence of sugar phosphate activator
Mg2+
-
2 cations per active site; pH-dependent; requirement
Mg2+
-
-
Mg2+
Busycotypus canaliculatum
-
-
Mg2+
-
fulfills absolute requirement for divalent cation; Km-value 0.45 mM for isozyme PKc, 1.6 mM for isozyme PKp; requirement
Mg2+
-
requirement
Mg2+
-
kinetics; requirement
Mg2+
-
positive cooperativity; requirement
Mg2+
-
requirement
Mg2+
-
positive cooperativity
Mg2+
-
apparent Km-value: 0,21 mM; fulfills absolute requirement for divalent cation
Mg2+
Musa cavendishii
-
fulfills absolute requirement for divalent cation; Km-value 0.27 mM, hyperbolic saturation kinetics
Mg2+
Q10208
requirement
Mg2+
-
either Mn2+ or Mg2+ are required; requirement
Mg2+
-
fulfills absolute requirement for divalent cation
Mg2+
-
requirement
Mg2+
Q9LBS6, -
either Mn2+ or Mg2+ are required
Mg2+
-
requirement
Mg2+
-
either Mn2+ or Mg2+ are required; requirement
Mg2+
-
activation
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+
-
divalent cation required
Mg2+
-
divalent cation required, at 1 mM highest activity with Mg2+
Mg2+
-
divalent cation required
Mg2+
-
required for activity
Mg2+
-
strict requirement
Mg2+
-
essential for activity
Mg2+
-
addition of Mg2+ protects the enzyme completely from the ferrous ion-mediated inactivation
Mg2+
C6UXB6, P0AD62
required; required
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required
Mg2+
-, Q5CSM7
required
Mn2+
-
requirement
Mn2+
-
requirement
Mn2+
-
kinetics; requirement
Mn2+
-
enzyme-bound
Mn2+
-
requirement
Mn2+
-
requirement
Mn2+
Cardium tuberculatum
-
best activator; can partially replace Mg2+
Mn2+
-
Km-value: 0.6 mM, flight muscle isozyme
Mn2+
-
activation; pH-dependent
Mn2+
-
requirement
Mn2+
-
activation; best activator; the activity of the sugar phosphate-activated enzyme is reduced to 50% if Mn2+ is omitted
Mn2+
Busycotypus canaliculatum
-
can partially replace Mg2+
Mn2+
-
fulfills absolute requirement for divalent cation; Km-value 0.05 mM for isozyme PKc, 0.5 mM for isozyme PKp; requirement
Mn2+
-
can partially replace Mg2+; requirement
Mn2+
-
requirement
Mn2+
-
can partially replace Mg2+; requirement
Mn2+
-
can partially replace Mg2+; kinetics; requirement
Mn2+
-
only together with K+; requirement
Mn2+
-
positive cooperativity
Mn2+
-
either Mn2+ or Mg2+ are required
Mn2+
Q9LBS6, -
either Mn2+ or Mg2+ are required
Mn2+
-
either Mn2+ or Mg2+ are required
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+
-
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+
-
divalent cation required
Mn2+
-
divalent cation required, at 1 mM Mn2+ activation results in 35% of the activity with Mg2+
Mn2+
-
required, binds at the active site
Monovalent cation
-
requirement; requires both a divalent and a monovalent cation
Monovalent cation
Cardium tuberculatum
-
requirement
Monovalent cation
-
requirement
Monovalent cation
-
requirement
Monovalent cation
-
requirement; requires both a divalent and a monovalent cation
Monovalent cation
-
requirement; requires both a divalent and a monovalent cation
Monovalent cation
-
requirement
Monovalent cation
-
in decreasing order of efficiency: K+, Rb+, Cs+, Na+, NH4+, Li+
Monovalent cation
-
not
Na+
-
activation, can replace K+
Na+
-
inhibits above 100 mM
Na+
-
can poorly replace K+
Na+
-
in decreasing order of efficiency: K+, Rb+, Cs+, Na+, NH4+, Li+
Na+
Q9LBS6, -
not
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+
Cardium tuberculatum
-
requirement
NH4+
-
as good as K+; requirement
NH4+
Busycotypus canaliculatum
-
can replace K+; requirement
NH4+
-
requirement
NH4+
-
can replace K+; requirement
NH4+
-
can replace K+; inhibits above 100 mM; requirement
NH4+
-
can replace K+; requirement
NH4+
-
in decreasing order of efficiency: K+, Rb+, Cs+, Na+, NH4+, Li+
NH4+
-
activation; can replace K+; kinetics
NH4+
-
can replace K+; only together with activating divalent cation; requirement
Ni2+
-
divalent cation required, at 1 mM Ni2+ activation results in 2% of the activity with Mg2+
sulfate
-, Q5CSM7
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+
-
activation or inhibition, concentration-dependent behaviour
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+
Monovalent cation
-
requirement; requires both a divalent and a monovalent cation
additional information
-
K-type allosteric properties only in the presence of Mg2+, not Mn2+
additional information
Busycotypus canaliculatum
-
interacting effects of various activators and inhibitors
additional information
-
no activation by Cu2+, Ni2+; no activation by Sr2+
additional information
-
no activation by SCN-
additional information
-
no activation by Ba2+; no activation by Cu2+, Ni2+
additional information
-
absolute requirement for a bivalent and a monovalent cation with Mg2+ and K+ fulfilling this; no activation by Li+
additional information
-
absolute requirement for a bivalent and a monovalent cation with Mg2+ and K+ fulfilling this
additional information
Musa cavendishii
-
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
-
absolute requirement for a bivalent and a monovalent cation with Mg2+ and K+ fulfilling this
additional information
-
1 mM Mg2+ does not shows significant activity. No activity is observed with Ca2+ and Zn2+
additional information
-
activity is independent of free Mg2+ concentration in the range 4-20 mM
additional information
-
catalytic activity is independent of K+
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
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
(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'-((1H-indol-2-yl)methylene)-5-bromo-2-hydroxybenzohydrazide
-
-
(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)-2-hydroxybenzohydrazide
-
-
(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)-3-bromobenzohydrazide
-
-
(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'-[(1H-indol-2-yl)methylene]-5-bromo-2-methoxybenzohydrazide
-
-
-
(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
2,3-diphosphoglycerate
-
-
2,3-diphosphoglycerate
Pigeon
-
-
2,3-diphosphoglycerate
-
-
2,4-dihydroxy-N'-[(E)-(2-hydroxy-6,7,8,9-tetrahydrodibenzo[b,d]furan-1-yl)methylidene]benzohydrazide
-
-
2-aminoisobutyric acid
-
allosteric inhibition
-
2-hydroxy-5-iodo-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
-
2-oxoglutarate
Busycotypus canaliculatum
-
not
2-oxoglutarate
-
not
2-oxoglutarate
-
at 5 mM, pH 7.0, 35% inhibition
2-oxoglutarate
-
50% inhibition at 8.3 mM
2-phosphoglycerate
-
only isozyme PKp, not PKc
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-phosphoglycerate
Busycotypus canaliculatum
-
not
3-phosphoglycerate
-
-
3-phosphoglycerate
-
80% activity at pH 6.4, 86% activity at pH 7.4
3-phosphoglycerate
-
8% inhibition at 5 mM
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
-
-
6-phosphogluconate
-
-
A-Raf protein
P14618
proteins known for cellular growth and proliferation such as A-Raf and PML protein are known to downregulate PKM2 activity by interacting with it
-
adenosine
-
0.01 mM
ADP
-
above 1-2 mM
ADP
Busycotypus canaliculatum
-
at high concentrations; fructose 1,6-diphosphate partially restores
ADP
Busycotypus canaliculatum
-
activators restore
ADP
-
at high concentrations; substrate inhibition
AMP
-
in a cooperative manner with ATP
AMP
Busycotypus canaliculatum
-
MgAMP
AMP
-
1 mM, 77% of activity remaining
AMP
-
11% inhibition at 5 mM
Antibody
-
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
-
arginine phosphate
-
flight muscle isozyme: weak; fructose 1,6-diphosphate restores
arginine phosphate
Busycotypus canaliculatum
-
allosteric inhibitor; fructose 1,6-diphosphate restores
ascorbate
-
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
aspartate
-
only isozyme PKp, not PKc
ATP
-
liver, not muscle enzyme
ATP
-
above 6 mM
ATP
-
enzyme form I; strong
ATP
Pigeon
-
-
ATP
-
fructose 1,6-diphosphate does not reverse
ATP
-
in the presence of Mg2+, not Mn2+, reversible by AMP
ATP
-
L- and R-type isozyme; phosphorylated enzyme is more sensitive than unphosphorylated enzyme
ATP
-
in a cooperative manner with AMP
ATP
Busycotypus canaliculatum
-
MgATP2-
ATP
-
glucose 6-phosphate reverses
ATP
-
ADP alleviates; kinetics
ATP
-
50% inhibition at 4 mM; strong
ATP
-
at 1 mM, pH 7.0, 50% inhibition
ATP
-
allosteric inhibitor
ATP
-
1 mM, 77% of activity remaining; 1 mM, 87% of activity remaining
ATP
-
IC50: 8.8 mM at pH 6.4, IC50: 13.7 mM at pH 7.4
ATP
-
as pH increases (pH range 6.5-8.0), ATP elicits more inhibition
ATP
Q6GG09
inhibition of full-length enzyme at concentration above 2.5 mM
ATP
-
48% inhibition at 5 mM, significant allosteric effector of the partially purified enzyme
Ba2+
-
in decreasing order of inhibitory efficiency: Ni2+, Zn2+, Cu2+, Ca2+, Ba2+
Ca2+
-
strong at saturating phosphoenolpyruvate concentrations
Ca2+
-
in decreasing order of inhibitory efficiency: Ni2+, Zn2+, Cu2+, Ca2+, Ba2+
Carbamoyl phosphate
-
-
catecholamine
-
-
Cd2+
-
at physiological pH, activating below
citrate
Cardium tuberculatum
-
-
citrate
-
fat body isozyme; weak, flight muscle isozyme
citrate
Busycotypus canaliculatum
-
not
citrate
-
isozyme PKI, kinetics; not isozyme PKII
citrate
-
at 5 mM, pH 7.0, 40% inhibition
citrate
-
50% inhibition at 18.4 mM
citrate
-
noncompetitive with respect to ADP
citrate
-
IC50: 9.2 mM at pH 6.4, IC50: 14.2 mM at pH 7.4
citrate
-
60% inhibition at 5 mM, significant allosteric effector of the partially purified enzyme
Co2+
-
at physiological pH, activating below
Cu2+
-
in decreasing order of inhibitory efficiency: Ni2+, Zn2+, Cu2+, Ca2+, Ba2+
cumene hydroperoxide
-
1% residual activity after treatment with 17 mM cumene hydroperoxide at 50C and pH 7 for 2 h
cysteine
-
fructose 1,6-diphosphate protects
cystine
-
inhibits by two different mechanisms, one through the competition with ADP and phosphoenolpyruvate, and the other non-competitively, probable through oxidation of the thiol groups of the enzyme. GSH and cysteamine fully prevent and reverse the inhibition caused by cystine
cystine
-
2.5 mM, significant inhibition
D-alanine
-
allosteric inhibition
D-fructose 1,6-bisphosphate
-
IC50: 8.4 mM at pH 6.4, IC50: 8.0 mM at pH 7.4
D-fructose 1,6-bisphosphate
Q6GG09
inhibition of full-length enzyme at 10 mM
D-fructose 1,6-bisphosphate
-
phosphorylation of serine and threonine residues is, besides being essential for isozyme M2 catalytic activity, induces a trimeric association of the ProTalpha kinase. This association can be shifted to a tetrameric form by fructose 1,6-bisphosphate, which results in a decrease in ProTalphaK activity
D-Fructose 1-phosphate
-
allosteric inhibitor with a 40% reduction in the Vmax
D-glucose 1-phosphate
-
allosteric inhibitor with a 40% reduction in the Vmax
D-ribose 5-phosphate
-
only isozyme PKp, not PKc
D-ribulose 1,5-bisphosphate
-
isozyme PKp, not PKc
diphosphate
-
IC50: 9.8 mM at pH 6.4, IC50: 17.2 mM at pH 7.4
EGMVLPTVWQPANWMCRLSN
-
peptide aptamer placed within thioredoxin A. Aptamer specifically binds to M2 pyruvate kinase and shifts the isoenzyme into its low affinity dimeric conformation
EGQLRHWGWAWSLASQNFSI
-
peptide aptamer placed within thioredoxin A. Aptamer specifically binds to M2 pyruvate kinase and shifts the isoenzyme into its low affinity dimeric conformation
FeSO4
-
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
fructose 1,6-diphosphate
-
-
fructose 1,6-diphosphate
-
-
fructose 1,6-diphosphate
-
-
fructose 1,6-diphosphate
-
at 5 mM, pH 7.0, 60% inhibition
glucose 6-phosphate
-
at high concentrations
glucose 6-phosphate
Busycotypus canaliculatum
-
not
glucose 6-phosphate
-
only isozyme PKp, not PKc
glutamate
-
IC50: 2.5 mM at pH 6.4, IC50: 1.2 mM at pH 7.4
glyoxylate
-
5 mM, 79% of activity remaining; 5 mM, 83% of activity remaining
GTP
-
0.1 mM GTP reduces the Vmax by 10%
Hexanoate
-
0.5 mM
Highly phosphorylated inositol derivatives
Pigeon
-
-
-
human papillomavirus-16 E7
P14618
causes dissociation of PKM2 tetramer into inactive dimer
-
hydrogen peroxide
-
inhibitory at 0.25%, at pH 7
hydroxyl radical
-
inactivation
iso-citrate
-
10 mM, 70% of activity remaining; 10 mM, 75% of activity remaining
Isocitrate
Busycotypus canaliculatum
-
not
Isocitrate
-
only isozyme PKp, not PKc
Isocitrate
-
76% activity at pH 6.4, 91% activity at pH 7.4
Isocitrate
-
30% inhibition at 5 mM
K+
-
above 100 mM, activates below
KCl
-
40 mM, 50-60% decrease in activity of recombinant enzyme
L-alanine
-
weak; weak, in the presence of Mn2+
L-alanine
-
fructose bisphosphate protects; strong
L-alanine
Cardium tuberculatum
-
phosphoenolpyruvate- and Mg2+-dependent
L-alanine
-
weak; weak, flight muscle isozyme
L-alanine
-
fructose 1,6-diphosphate restores; kinetics
L-alanine
-
-
L-alanine
-
L- and M2-type, not M1-type isozyme
L-alanine
-
fructose 1,6-diphosphate restores
L-alanine
Busycotypus canaliculatum
-
allosteric inhibitor; fructose 1,6-diphosphate restores
L-alanine
-
allosteric inhibition. The pyruvate kinase isozyme from human liver has decreased affinity for phosphoenolpyruvate when allosterically inhibited by alanine. Minimal effect on coupling caused by the methyl group substitution to Ala (2-aminoisobutyric acid vs. Ala)
L-cysteine
-
allosteric inhibition
L-glutamate
-
dihydroxyacetone phosphate reverses
L-glutamate
-
-
L-glutamate
-
not isozyme PKI; strong, isozyme PKII, kinetics
L-glutamate
-
50% inhibition at 4 mM
L-glutamate
Musa cavendishii
-
-
L-glutamate
-
-
L-glutamate
-
5 mM, 30% of activity remaining, IC50: 2.1 mM, IC50: 6.2 mM; 5 mM, 59% of activity remaining, IC50: 6.2 mM
L-lactate
Cardium tuberculatum
-
-
L-lactate
Busycotypus canaliculatum
-
-
L-Phe
-
23.5% activity left at 1 mM L-Phe in the absence of D-fructose 1,6-bisphosphate
L-phenylalanine
-
fructose 1,6-diphosphate protects
L-phenylalanine
-
fructose 1,6-diphosphate protects; not in the presence of Mn2+; strong
L-phenylalanine
-
-
L-phenylalanine
-
isozymes PK I and II differ in sensitivity to the inhibitor
L-phenylalanine
-
strong
L-phenylalanine
-
weak
L-phenylalanine
-
L- and M2-type, not M1-type isozyme
L-phenylalanine
-
fructose 1,6-diphosphate protects
L-phenylalanine
-
strong
L-phenylalanine
Busycotypus canaliculatum
-
alanine and fructose 1,6-diphosphate protect, kinetics; allosteric inhibitor; pH-dependent
L-phenylalanine
-
allosterical inhibitor
L-phenylalanine
-
3 mM, significant inhibition
L-phenylalanine
-
allosteric inhibition. Replacement of the alpha-hydrogen of L-Phe with a methyl group (S)-2-amino-2-methyl-3-phenyl-propionic acid eliminates an allosteric response
L-phenylalanine
-
the carboxyl group of phosphoenolpyruvate is responsible for energetic coupling with Phe binding in the allosteric sites
L-phenylalanine
-
acts as an allosteric inhibitor of muscle isozyme and induces the enzyme to exist in multiple conformations by locking it in an expanded or asymmetric conformation, which is contrary effect to that of phosphoenolpyruvate binding
L-proline
-
allosteric inhibition
L-tryptophan
-
1 mM, significant inhibition
L-valine
-
allosteric inhibition
lysophosphatidic acid
P14618
-
malate
Busycotypus canaliculatum
-
not
malate
-
only isozyme PKp, not PKc
malate
-
78% activity at pH 6.4, 90% activity at pH 7.4
menadione
-
i.e. vitamin K3, shows a significantly stronger potency to inhibit isozyme PKM2 than to inhibit isozymes PKM1 and PKL
MgATP2-
-
feed-back inhibition; fructose 1,6-diphosphate restores
MgATP2-
Busycotypus canaliculatum
-
allosteric inhibitor; fructose 1,6-diphosphate restores
MgATP2-
Busycotypus canaliculatum
-
activators restore activity
MgATP2-
Musa cavendishii
-
-
MgATP2-
-
potent inhibitor
N'-[(1E)-1-(1,3-benzothiazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
-
-
N'-[(1E)-1-(1,3-benzoxazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
-
26% inhibition at 500 nM
N'-[(1E)-1-(1-benzothiophen-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
-
-
N'-[(1E)-1-(1H-benzimidazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
-
-
N'-[(1E)-1-(2,4-dihydroxyphenyl)ethylidene]-3-(5,6-dimethyl-1,3-dihydro-2H-isoindol-2-yl)benzohydrazide
-
-
N'-[(1E)-1-(5-bromo-1-methyl-1H-indol-2-yl)ethylidene]-3-hydroxynaphthalene-2-carbohydrazide
-
-
N'-[(1E)-1-(5-bromo-1-methyl-1H-indol-2-yl)propylidene]-3-hydroxynaphthalene-2-carbohydrazide
-
-
N'-[(1E)-1-(5-bromo-1H-indol-2-yl)ethylidene]-3-hydroxynaphthalene-2-carbohydrazide
-
-
N'-[(1E)-1-(5-bromo-1H-indol-2-yl)propylidene]-3-hydroxynaphthalene-2-carbohydrazide
-
-
N'-[(3E)-5-fluoro-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-3-hydroxybenzohydrazide
-
-
N'-[(3Z)-1-ethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-3-hydroxynaphthalene-2-carbohydrazide
-
-
N-(3-carboxy-4-hydroxy)phenyl-2,5-dimethylpyrrole
-
a PKM2 inhibitor
-
N-(4-methylphenyl)-2-[(4-sulfamoylphenyl)amino]pyridine-3-carboxamide
-
-
N-ethylmaleimide
-
isozyme PK1 is more sensitive than PK2
Na+
-
above 100 mM, activates below
NaF
-
non-specific phosphoenolpyruvate kinase inhibitor
NH4+
-
above 100 mM, activates below
NH4Cl
-
40 mM, 50-60% decrease in activity of recombinant enzyme
Ni2+
-
in decreasing order of inhibitory efficiency: Ni2+, Zn2+, Cu2+, Ca2+, Ba2+
oxalate
-
kinetics
oxalate
-
50% inhibition at 4 mM
oxalate
-
PK I, 80% inhibition at 0.3 mM, PK II, 50% inhibition at 0.3 mM
oxalate
-
50% inhibition at 0.23 mM
oxalate
-
0.2 mM, 50% of activity remaining; 0.2 mM, 71% of activity remaining, IC50: 0.41 mM
oxaloacetate
-
-
oxaloacetate
Busycotypus canaliculatum
-
not
oxaloacetate
-
2 mM, 82% of activity remaining; 2 mM, 88% of activity remaining
Pb2+
-
lead inhibits pyruvate kinase activity in a dose-dependent manner by interaction with its thiol groups
peptide aptamer 9
-
-
-
peracetic acid
-
1% residual activity after treatment with 4 mM peracetic acid at 25C and pH 7 for 15 min
Phe
-
competitive with ADP and phosphoenolpyruvate, Ala prevents inhibition
phenylalanine
-
allosteric inhibitor, regions of pyruvate kinase important for allosteric regulation by phenylalanine, H/D exchange mass spectrometry, overview
phenylalanine
-
allosteric inhibitor
phenylpyruvate
-
competitive with ADP and phosphoenolpyruvate, Ala prevents inhibition
phosphate
-
strong
phosphate
Busycotypus canaliculatum
-
not
phosphate
Busycotypus canaliculatum
-
activators restore
phosphate
-
at high concentrations; strong
phosphate
Q9LBS6, -
severe, restored by addition of fructose 1,6-diphosphate
phosphate
-
at 5 mM, pH 7.0, 40% inhibition
phosphoenolpyruvate
-
1-5 mM
phosphoenolpyruvate
-
at 5C, concentrations greater than 10 mM are inhibiting
Phosphoglycolate
-
only isozyme PKp, not PKc
phosphotyrosine peptide
-
binding of phosphotyrosine peptides to PKM2 results in release of the allosteric activator fructose-1,6-bisphosphate, leading to inhibition of PKM2 enzymatic activity (2030% inhibition of PKM2 activity in a dose-dependent manner)
-
PML protein
P14618
proteins known for cellular growth and proliferation such as A-Raf and PML protein are known to downregulate PKM2 activity by interacting with it
-
Pp60v-src
P14618
causes dissociation of PKM2 tetramer into inactive dimer
-
Procion blue MX-R
-
triazine dye, kinetics, ADP or ADP plus Mg2+ protect, not Mg2+ alone
proline
Busycotypus canaliculatum
-
allosteric inhibitor, fructose 1,6-diphosphate restores
pyridoxal 5'-phosphate
-
1 mM
pyruvate
-
product inhibition
quercetin
-
50% inhibition at 0.1 mM
rutin
-
50% inhibition at 0.07 mM
shikonin
-
a PKM2 inhibitor
silibinin
-
inhibitory to pyruvate kinase, resulting in dose-dependently reduced glycolysis from carbohydrates and a fall in ATP-toADP ratio, together with an increase in lactate-to-pyruvate ratio in perifused hepatocyte
suppressor of cytokine signaling 3
-
in dendritic cells the interaction of M2-PK with suppressor of cytokine signaling 3, SOCS3, induces a decrease of M2-PK activity and ATP production as well as an impairment of dendritic cell-based immunotherapy against tumors
-
t-butyl hydroperoxide
-
in hemolysate exposed to t-butyl hydroperoxide, pyruvate kinase activity decreases along with depletion of glutathione. The addition of glutathione, but not glucose, before exposure completely prevents the inactivation of pyruvate kinase, partial reactivation of inactivated pyruvate kinase is observed by post-addition of both glutathione and glutaredoxin
tert-butyl hydroperoxide
-
1% residual activity after treatment with 290 mM tert-butyl hydroperoxide at 50C and pH 7 for 3 h
threonine
-
fructose 1,6-diphosphate protects
tryptophan
-
weak
tyrosine
-
fructose 1,6-diphosphate partially protects
valine
-
fructose 1,6-diphosphate protects
Zn2+
-
inhibition or activation, concentration-dependent behaviour
Zn2+
-
in decreasing order of inhibitory efficiency: Ni2+, Zn2+, Cu2+, Ca2+, Ba2+
[(5Z)-5-(4-[[(2-iodophenyl)carbonyl]oxy]benzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
84% inhibition at 0.03 mM
-
monensin
-
0.0005 mM
additional information
-
no inhibition by several amino acids
-
additional information
-
no substrate inhibition at pH-optimum
-
additional information
-
increasing buffer concentrations inhibit, least inhibitory: imidazole-HCl
-
additional information
-
phosphorylation by cAMP-dependent protein kinase, L- and R-type isozyme
-
additional information
-
no phosphorylation
-
additional information
Busycotypus canaliculatum
-
no inhibition by acetyl-CoA, NADP+, succinate, glycerol 1-phosphate, fructose 6-phosphate, D-octopine, meso-alanopine, NH4Cl, Arg, Gly, taurine, creatine phosphate
-
additional information
Busycotypus canaliculatum
-
interacting effects of various activators and inhibitors
-
additional information
-
not inhibited by propionic acid, N-methyl-L-alanine, N-formyl-L-alanine, N-acetyl-L-alanine, 3 phenylpropionic acid, N-methyl-L-phenylalanine, N-formyl-L-phenylalanine, N-acetyl-L-phenylalanine, and N,N-dimethylphenylalanine
-
additional information
-
alanine and serine cause no affection of activity but prevent the inhibition caused by phenylalanine, tryptophan or cystine
-
additional information
-
not inhibited by 6-phosphogluconate, dithiothreitol or sodium tetrathionate; not inhibited by AMP, dithiothreitol or sodium tetrathionate
-
additional information
-
not inhibited by 5 mM ADP
-
additional information
-
not inhibited by L-alanine
-
additional information
-
hydrogen peroxide does not inactivate
-
additional information
-
screen of a galactose-inducible combinatorial peptide aptamer library consisting of specific 20-mer peptides placed within 12-kDa protein thioredoxin A identifies 14 aptamers which specifically bind to M2 pyruvate kinase and shift the isoenzyme into its low affinity dimeric conformation. The aptamer-induced dimerization and inactivation of M2 pyruvate kinase leads to a significant decrease in the pyruvate kinase mass-action ratio as well as ATP:ADP ratio in the target cells. The expression of M2-pyruvate kinase-binding peptide aptamers moderately reduces the growth of immortalized NIH3T3 cell populations by decelerating cell proliferation, but without affecting apoptotic cell death. The M2-PK-binding peptide aptamers also reduce the proliferation rate of human U-2 OS osteosarcoma cells
-
additional information
-
cysteamine or glutathione per se do not modify enzymatic activity, but prevent the toxic effects of lead
-
additional information
-
phosphorylation at Ser12 interrupts an activating interaction of N-terminal residues (including those at positions 7-10) with the main body of the protein, as a means of inhibiting substrate affinity
-
additional information
-
activation of the high-affinity IgE receptor FcepsilonRI in RBL-2H3 cells causes the rapid phosphorylation of tyrosine residues in M2PK, associated with a decrease in M2PK enzymatic activity
-
additional information
-
L-Arg added to the incubation medium does not alter pyruvate kinase activity in hippocampus, cerebral cortex, and striatum
-
additional information
-
development of highly potent inhibitors which demonstrate complete selectivity for the bacterial enzyme compared to all human orthologues, molecular docking, overview
-
additional information
-
the nitrogen analogue N-(2,5-dimethylphenyl)-1,2-benzothiazol-3-amine 1,1-dioxide of 3-(2,5-dimethylphenoxy)-1,2-benzothiazole 1,1-dioxide is not inhibitory
-
additional information
-
no inhibition by D-phenylalanine and (S)-2-amino-2-methyl-3-phenyl-propionic acid. Analysis of the binding site for allosteric inhibitor amino acids and the allosteric kinetic mechanism, overview. L-Phe elicits the smallest antagonism of phosphoenolpyruvate affinity of all amino acids tested
-
additional information
-
replacing the carboxyl group of the substrate with a methyl alcohol or removing the phosphate altogether greatly reduces substrate affinity. Removal of the carboxyl group is the only modification tested that removes the ability to allosterically reduce the level of Phe binding. Requirement for monovalent and divalent cations for allosteric inhibition
-
additional information
-
alanine is a nonallosteric analogue of phenylalanine, it binds competitively with phenylalanine but elicits a negligible allosteric inhibition, i.e., a negligible reduction in the affinity of the muscle enzyme for the substrate, phosphoenolpyruvate
-
additional information
-
IgE receptor FcepsilonRI rapid phosphorylation of tyrosine residues in M2-PK leads to its inhibition and initiation of mast cell degranulation
-
additional information
-
inhibitor development, synthesis, optimization, and structure-activity relationship analysis, inhibitor potencies in growth inhibition of strains RN4220, ATCC 25923, and ATCC 29213, overview. No inhibition by (E)-5-bromo-2-hydroxy-N'-(1-(5-phenyl-1H-indol-2-yl)ethylidene)benzohydrazide, (Z)-N'-(1-(1H-indol-2-yl)-2,2-dimethylpropylidene)-5-bromo-2-hydroxybenzohydrazide, and 5-bromo-N'-[(1E)-2,2-dimethyl-1-(1-methyl-1H-indol-2-yl)propylidene]-2-hydroxybenzohydrazide
-
additional information
-
D-fructose 1,6-bisphosphate diminishes the inhibitory effects of vitamin K derivatives. No inhibition of isozyme PKM2 by vitamin K1 and vitamin K2
-
additional information
-
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
-
poor inhibition of glucose 1-phosphate and fumaric acid at 5 mM
-
additional information
-
the absence of extracellular serine and glycine has a pronounced inhibitory effect on pyruvate kinase activity, and serine and glycine deprivation decreases PKM2 activity in cells
-
additional information
-
no significant effect by D-fructose 6-phosphate and D-ribulose 1,5-bisphosphate
-
additional information
P14618
poor inhibition by thyroid hormone T3. Tyr phosphorylated peptides interact with isozyme PKM2 at a site near to D-fructose 1,6-bisphosphate-binding pocket and can affect fructose 1,6-bisphosphate binding. Fibroblast growth factor receptor-dependent phosphorylation of iozyme PKM2 at Y105 causes its dimerization by the release of fructose 1,6-bisphosphate leading to Warburg effect
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2R)-1-[(2,6-difluorophenyl)sulfonyl]-4-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-2-methylpiperazine
-
-
(2R)-4-[(2,6-difluorophenyl)sulfonyl]-1-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-2-methylpiperazine
-
-
-
(2S)-1-[(2,6-difluorophenyl)sulfonyl]-4-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-2-methylpiperazine
-
-
(2S)-4-[(2,6-difluorophenyl)sulfonyl]-1-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-2-methylpiperazine
-
-
-
1-acetyl-N-(3,4-dimethylphenyl)-1,2,3,4-tetrahydroquinoline-8-sulfonamide
-
-
1-acetyl-N-(3,4-dimethylphenyl)-2,3-dihydro-1H-indole-5-sulfonamide
-
-
1-[(2,6-difluorophenyl)sulfonyl]-4-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)piperazin-2-one
-
-
-
1-[1-(ethylsulfonyl)-2,3-dihydro-1H-indol-5-yl]-2-[(4-methoxyphenyl)sulfanyl]ethanone
-
-
2,3-dihydro-1,4-benzodioxin-6-yl[2-methyl-1-(methylsulfonyl)-2,3-dihydro-1H-indol-5-yl]methanone
-
-
2,6-difluorophenyl 5-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-2-methyl-2,3-dihydro-1H-indole-1-sulfonate
-
-
2-((2,3-dihydrobenzo[b][1,4]dioxin-6-yl)thio)-1-(2-methyl-1-(methylsulfonyl)indolin-5-yl) ethanone
-
-
2-(2,3-dihydro-1,4-benzodioxin-6-ylsulfanyl)-1-[2-methyl-1-(methylsulfonyl)-2,3-dihydro-1H-indol-5-yl]ethanone
-
-
2-(3,4-dihydro-2H-1,5-benzodioxepin-7-ylsulfanyl)-1-[1-(ethylsulfonyl)-2,3-dihydro-1H-indol-5-yl]ethanone
-
-
2-oxo-N-(pyridin-3-yl)-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
2-oxo-N-(pyridin-4-yl)-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
2-oxo-N-(quinolin-6-yl)-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
2-oxo-N-[3-(trifluoromethyl)phenyl]-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
2-[(3,5-difluorophenyl)sulfanyl]-1-[1-(ethylsulfonyl)-2,3-dihydro-1H-indol-5-yl]ethanone
-
-
3-([4-[(2,6-difluoro-4-methoxyphenyl)sulfonyl]-1,4-diazepan-1-yl]sulfonyl)aniline
-
-
-
3-([4-[(2,6-difluoro-4-methoxyphenyl)sulfonyl]piperazin-1-yl]sulfonyl)aniline
-
highly potent activator of PKM2
-
3-([4-[(2,6-difluorophenyl)sulfonyl]piperazin-1-yl]sulfonyl)aniline
-
highly potent activator of PKM2
3-chloro-N-(3,4-dimethylphenyl)benzenesulfonamide
-
-
3-fluorophenyl (3,4-dimethylphenyl)sulfamate
-
-
3-fluorophenyl 5-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-2,3-dihydro-1H-indene-1-sulfonate
-
-
3-methoxyphenyl 5-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-2-methyl-2,3-dihydro-1H-indole-1-sulfonate
-
-
3-phosphoglycerate
-
slight activation
3-[(3,4-dimethylphenyl)sulfamoyl]benzoic acid
-
-
3-[[4-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-1,4-diazepan-1-yl]sulfonyl]aniline
-
highly potent activator of PKM2
-
3-[[4-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)piperazin-1-yl]sulfonyl]aniline
-
highly potent activator of PKM2
3-{[4-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-1,4-diazepan-1-yl]sulfonyl}aniline
-
i.e. NCGC00185916
4-fluorophenyl (3,4-dimethylphenyl)sulfamate
-
-
4-fluorophenyl 5-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-2-methyl-2,3-dihydro-1H-indole-1-sulfonate
-
-
4-[(2,6-difluorophenyl)sulfonyl]-1-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)piperazin-2-one
-
-
5-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-1-(methylsulfonyl)-1H-indole
-
-
5-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-2-methyl-1-(methylsulfonyl)-2,3-dihydro-1H-indole
-
-
5-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-2-methyl-1-(phenylsulfonyl)-2,3-dihydro-1H-indole
-
-
5-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-3-methyl-1-(methylsulfonyl)-1H-indole
-
-
5-amino-N-(3,4-dimethylphenyl)-1-methyl-1H-indole-7-sulfonamide
-
-
-
6-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-1-(methylsulfonyl)-1,2,3,4-tetrahydroquinoline
-
-
6-(3-methoxybenzyl)-4-methyl-2-(methylsulfinyl)-4,6-dihydro-5H-thieno[2',3':4,5]pyrrolo[2,3-d]pyridazin-5-one
-
i.e. NCGC00186527
6-([4-[(2,6-difluorophenyl)sulfonyl]cyclohexyl]sulfonyl)-2,3-dihydro-1,4-benzodioxine
-
-
6-chloro-N-(3,4-dimethylphenyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-sulfonamide
-
-
6-phosphogluconate
-
at 1 mM, 200% of activity
6-phosphogluconate
-
192% of activity at 0.05 mM
6-{hydroxy[1-(methylsulfonyl)-1,2,3,7a-tetrahydro-5H-inden-5-ylidene]oxido-l6-sulfanyl}-2,3-dihydro-1,4-benzodioxine
-
-
6-{[1-(cyclopropylsulfonyl)-2,3-dihydro-1H-inden-5-yl]sulfonyl}-2,3-dihydro-1,4-benzodioxine
-
-
6-{[1-(ethylsulfonyl)-2,3-dihydro-1H-inden-5-yl]sulfonyl}-2,3-dihydro-1,4-benzodioxine
-
-
6-{[1-(methylsulfonyl)-2,3-dihydro-1H-inden-5-yl]sulfonyl}-2,3-dihydro-1,4-benzodioxine
-
-
6-{[1-(phenylsulfonyl)-2,3-dihydro-1H-inden-5-yl]sulfonyl}-2,3-dihydro-1,4-benzodioxine
-
-
6-{[2-(ethylsulfonyl)-2,3-dihydro-1H-inden-5-yl]sulfonyl}-2,3-dihydro-1,4-benzodioxine
-
-
6-{[2-(methylsulfonyl)-2,3-dihydro-1H-inden-5-yl]sulfonyl}-2,3-dihydro-1,4-benzodioxine
-
-
6-{[2-(phenylsulfonyl)-2,3-dihydro-1H-inden-5-yl]sulfonyl}-2,3-dihydro-1,4-benzodioxine
-
-
6-{[2-(tert-butylsulfonyl)-2,3-dihydro-1H-inden-5-yl]sulfonyl}-2,3-dihydro-1,4-benzodioxine
-
-
7-(chloroamino)-N-(3,4-dimethylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
7-(diethylamino)-N-(3,4-dimethylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
7-(dimethylamino)-N-(3,4-dimethylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
7-(fluoroamino)-N-(3-fluoro-4-methylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
7-bromo-N-(3,4-dimethylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
7-bromo-N-(4-chloro-3-methylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
7-chloro-N-(4-chloro-3-methylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
7-[3-(dimethylamino)pyrrolidin-1-yl]-N-(3,4-dimethylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
A-Raf
-
-
-
alanine
-
activation
AMP
-
at 1 mM or below
AMP
-
allosteric activator
AMP
Q02499
wild-type, A0.5 value 0.013 mM
AMP
Q6GG09
allosteric activator
asparagine
Busycotypus canaliculatum
-
activation
asparagine
-
activation; synergistic activation with fructose 1,6-diphosphate of isozyme PK-aerobic, not PK-anoxic
asparagine
-
activation; kinetics
aspartate
Q9LBS6, -
-
aspartate
-
allosteric activator
ATP
Q6GG09
slight activation of the full-length enzyme, not the C-terminally truncated enzyme
CO2
-
activation, kinetics
cysteine
-
activation, can replace dithiothreitol
D-fructose 1,6-bisphosphate
-
activates
D-fructose 1,6-bisphosphate
-
strong activation
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
the smallest allosteric response to D-fructose 1,6-bisphosphate occurs at pH 6.5 and increases up to pH 8.0
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
heterotropic activator of PK1, the modulation of oligomeric state by the allosteric effector D-fructose 1,6-bisphosphate does not occur at a concentration of 10 nM or above
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
20.5% increase of activity at 2.5 mM
D-fructose 1,6-bisphosphate
-
induces an association of two inactive dimers to the active tetrameric form
D-fructose 1,6-bisphosphate
-
induces an association of two inactive dimers to the active tetrameric form. M2-PK showing ProTalpha kinase activity is a trimeric association and possesses no observable pyruvate kinase activity. This association can be shifted by fructose 1,6-P2 to the tetrameric form which results in a reduction of ProTalpha-kinase activity
D-fructose 1,6-bisphosphate
-
increases the affinity and reduces the cooperativity of substrate binding, increases Vmax by 20%
D-fructose 1,6-bisphosphate
P14618
triggers allosteric signal transduction, increases activity, binding tetramerizes the enzyme, whereas its release causes dissociation to inactive dimer
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
-
activation; slight
D-fructose 1,6-diphosphate
-
activation; kinetics
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
Cardium tuberculatum
-
activation
D-fructose 1,6-diphosphate
-
activation; not; strong activation, fat body enzyme
D-fructose 1,6-diphosphate
-
activation; heterotropic allosteric activator
D-fructose 1,6-diphosphate
-
activation; pH-dependent
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
activation; allosteric activation together with phosphoenolpyruvate
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
activation; major allosteric activator
D-fructose 1,6-diphosphate
-
activation; not
D-fructose 1,6-diphosphate
-
activation; requirement with Mg2+; with Mn2+
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
Busycotypus canaliculatum
-
activation
D-fructose 1,6-diphosphate
Busycotypus canaliculatum
-
activation; stimulates aerobic isozyme more strongly than anoxic isozyme; synergism with Asp, PK-aerobic, not PK-anoxic
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
-
activation; kinetics
D-fructose 1,6-diphosphate
-
activation; more evident in the presence of glycerol
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
activation; kinetics
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
Q10208
-
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
-
only PK II, shifting sigmoidal kinetics to hyperbolic curves, decrease in Km
D-fructose 1,6-diphosphate
-
-
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
Q9LBS6, -
-
D-fructose 1,6-diphosphate
-
isoform Pyk1p: is activated up to 8fold with Km lowered up to 30fold, Pyk2p: activity and Km only marginally affected
D-fructose 2,6-bisphosphate
A7LIU4, -
allosteric stimulation
D-fructose 2,6-bisphosphate
-
wild-type, S0.5 value 0.000082 mM
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-diphosphate
-
activation; best activator
D-fructose 2,6-diphosphate
-
allosteric effector
D-fructose 2,6-diphosphate
Busycotypus canaliculatum
-
activation
D-fructose 2,6-diphosphate
-
not
D-fructose 2,6-diphosphate
-
activation; allosteric effector
D-fructose 2,6-diphosphate
-
allosteric effector
D-fructose 6-phosphate
-
requirement with Mg2+, activation with Mn2+
D-fructose diphosphate
-
activation
D-fructose diphosphate
-
activation
D-fructose diphosphate
-
activation
D-fructose diphosphate
-
activation; enzyme form I
D-fructose diphosphate
Pigeon
-
activation
D-fructose diphosphate
-
activation
D-fructose diphosphate
-
activation
D-fructose diphosphate
-
activation; cardiac and liver isozyme, together with phosphoenolpyruvate
D-fructose diphosphate
-
allosteric effector
D-fructose-1,6-bisphosphate
-
-
D-fructose-1,6-bisphosphate
-
isozyme PKM2 requires D-fructose-1,6-bisphosphate to form the active tetramer, but isozyme PKM1 does not
D-fructose-1,6-bisphosphate
-
allosteric effector, binds to PykF but not to PykA
D-glucose 1,6-diphosphate
-
slight activation
D-glucose 1-phosphate
-
slight activation, not isozyme PKp
D-glucose 1-phosphate
-
not
D-glucose 6-phosphate
-
not
D-glucose 6-phosphate
-
requirement with Mg2+, activation with Mn2+
D-glucose 6-phosphate
-
isozyme PK II
D-glucose 6-phosphate
-
activation; not: isozyme PKp
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
activation
D-glucose 6-phosphate
-
activation
D-glucose 6-phosphate
-
requirement
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
radically activates
D-glucose 6-phosphate
-
classic allosteric activation with a 6fold reduction in the apparent Km and no effect on the Vmax
D-ribose 1-diphosphate 5-phosphate
-
activation, kinetics, much more effective than fructose 1,6-diphosphate or glucose 1,6-diphosphate
D-ribose 5-phosphate
-
requirement with Mg2+, activation with Mn2+
D-ribose 5-phosphate
-
activation; isozyme PK II
D-ribose 5-phosphate
-
activation
D-ribose 5-phosphate
-
activation
D-ribose 5-phosphate
-
activation
D-ribose 5-phosphate
P51181
-
D-ribose 5-phosphate
-
-
D-ribose 5-phosphate
P51182, -
-
D-ribose 5-phosphate
-
-
D-ribose 5-phosphate
-
0.1 mM, allosteric activator
D-ribose 5-phosphate
Q02499
wild-type, A0.5 value 0.0075 mM
D-ribose 5-phosphate
Q6GG09
allosteric activator
D-Ribulose 1,5-diphosphate
-
activation
D-Ribulose 1,5-diphosphate
-
activation; kinetics; much more effective than fructose 1,6-diphosphate or glucose 1,6-diphosphate
D-Ribulose 1,5-diphosphate
-
not
D-tagatose 1,6-diphosphate
-
requirement with Mg2+, activation with Mn2+
D-tagatose 6-phosphate
-
requirement with Mg2+, activation with Mn2+
dihydroxyacetone phosphate
-
activation
dihydroxyacetone phosphate
-
activation; requirement with Mg2+; with Mn2+
dihydroxyacetone phosphate
-
activation; kinetics
dithiothreitol
-
required for optimal activity
dithiothreitol
-
activation
erythrose 4-phosphate
-
requirement with Mg2+, activation with Mn2+
fructose 1,6-bisphosphate
-
mutant enzyme T298C shows no catalytic activity in the absence of the heterotrophic activator
fructose 1,6-bisphosphate
-
-
fructose 1,6-bisphosphate
-
activates isozyme PKM2 by direct binding
glutamic acid
-
activation
glutamine
-
activation
glyceraldehyde 3-phosphate
-
activation
glyceraldehyde 3-phosphate
-
activation; requirement with Mg2+; with Mn2+
glyceraldehyde 3-phosphate
-
not
glycerol 3-phosphate
-
-
glycine
-
activation
GSH
-
activation, can replace dithiothreittol
Indole
Q8GQS6, -
stimulates
Insulin
-
stimulation
-
Isoleucine
-
slight activation, kinetics
isopropyl-beta-D-thiogalactopyranoside
-
50% increased activity at 1 mM
L-aspartate
-
Ka-value 0.31 mM, reverses inhibition by L-glutamate
L-serine
-
allosteric activator of PKM2, activates isozyme PKM2 by direct binding
L-serine
-
an allosteric activator of PKM2, serine-dependent regulation of pyruvate kinase M2 and general control nonderepressible 2 kinase to modulate the flux of glycolytic intermediates in support of cell proliferation
methionine
-
activation
Methyl paraoxon
-
in larvae, low doses of methyl paraoxon and methyl parathion activatd the enzyme but as the dose increases the Km value returned to normal levels
methyl parathion
-
in larvae, low doses of methyl paraoxon and methyl parathion activated the enzyme but as the dose increases the Km value returned to normal levels
Myxothiazol
-
0.0001 mM
N-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-methyl-1-(methylsulfonyl)-2,3-dihydro-1H-indole-5-sulfonamide
-
-
N-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(2,3-dihydro-1H-inden-5-yl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(2-fluorophenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(2-methylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3,4-dichlorophenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3,4-dimethylphenyl)-1-methyl-2-oxo-2,3-dihydro-1H-indole-5-sulfonamide
-
-
N-(3,4-dimethylphenyl)-2,2-dimethyl-3,4-dihydro-2H-chromene-6-sulfonamide
-
-
N-(3,4-dimethylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-7-sulfonamide
-
i.e. NCGC00185939
N-(3,4-dimethylphenyl)-2-oxo-2,3,4,5-tetrahydro-1H-1-benzazepine-7-sulfonamide
-
-
N-(3,4-dimethylphenyl)-2-oxo-2,3-dihydro-1H-benzimidazole-4-sulfonamide
-
-
N-(3,4-dimethylphenyl)-2-oxo-2,3-dihydro-1H-indole-4-sulfonamide
-
-
N-(3,4-dimethylphenyl)-2-oxo-7-(piperidin-1-yl)-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3,4-dimethylphenyl)-2-oxo-7-(propan-2-ylamino)-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3,4-dimethylphenyl)-2-oxo-7-(pyrrolidin-1-yl)-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3,4-dimethylphenyl)-3-methyl-2-oxo-2,3-dihydro-1,3-benzoxazole-5-sulfonamide
-
-
N-(3,4-dimethylphenyl)-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-6-sulfonamide
-
-
N-(3,4-dimethylphenyl)-3-oxo-6-phenyl-3,4-dihydro-2H-1,4-benzoxazine-7-sulfonamide
-
-
N-(3,4-dimethylphenyl)-3-oxo-6-[(E)-2-phenylethenyl]-3,4-dihydro-2H-1,4-benzoxazine-7-sulfonamide
-
-
N-(3,4-dimethylphenyl)-4-(2-oxopyrrolidin-1-yl)benzenesulfonamide
-
-
N-(3,4-dimethylphenyl)-4-fluorobenzenesulfonamide
-
-
N-(3,4-dimethylphenyl)-4-methoxybenzenesulfonamide
-
-
N-(3,4-dimethylphenyl)-4-methyl-3,4-dihydro-2H-1,4-benzoxazine-6-sulfonamide
-
-
N-(3,4-dimethylphenyl)-6-fluoro-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-sulfonamide
-
-
N-(3,4-dimethylphenyl)-6-methyl-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-7-sulfonamide
-
-
N-(3,4-dimethylphenyl)-7-(methylamino)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3,4-dimethylphenyl)-7-[(1-hydroxypropan-2-yl)amino]-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3,4-dimethylphenyl)-7-[(2-hydroxyethyl)amino]-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3,4-dimethylphenyl)-7-[(2-hydroxypropan-2-yl)amino]-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3,4-dimethylphenyl)-7-{[(2R)-1-hydroxypropan-2-yl]amino}-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3,4-dimethylphenyl)-7-{[(2S)-1-hydroxypropan-2-yl]amino}-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3,4-dimethylphenyl)naphthalene-2-sulfonamide
-
-
N-(3-chloro-4-fluorophenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3-chloro-4-methylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3-chloro-4-methylphenyl)-7-(fluoroamino)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3-chlorophenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3-fluoro-4-methylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3-fluoro-4-methylphenyl)-7-{[(2S)-1-hydroxypropan-2-yl]amino}-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3-methoxyphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(3-methylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(4-chloro-3-fluorophenyl)-7-(fluoroamino)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(4-chloro-3-fluorophenyl)-7-{[(2S)-1-hydroxypropan-2-yl]amino}-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(4-chloro-3-methylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(4-chloro-3-methylphenyl)-7-(fluoroamino)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(4-chloro-3-methylphenyl)-7-{[(2S)-1-hydroxypropan-2-yl]amino}-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(4-chlorophenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(4-fluoro-3-methylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(4-methoxyphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(4-methylphenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(biphenyl-3-yl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-(naphthalen-2-yl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
N-[1-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)piperidin-4-yl]-2,6-difluorobenzenesulfonamide
-
-
N-[1-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)pyrrolidin-3-yl]-2,6-difluorobenzenesulfonamide
-
-
-
N-[1-[(2,6-difluorophenyl)sulfonyl]azetidin-3-yl]-2,3-dihydro-1,4-benzodioxine-6-sulfonamide
-
-
N-[1-[(2,6-difluorophenyl)sulfonyl]piperidin-4-yl]-2,3-dihydro-1,4-benzodioxine-6-sulfonamide
-
-
-
N-[1-[(2,6-difluorophenyl)sulfonyl]pyrrolidin-3-yl]-2,3-dihydro-1,4-benzodioxine-6-sulfonamide
-
-
N-[2-methyl-1-(methylsulfonyl)-2,3-dihydro-1H-indol-5-yl]-2,3-dihydro-1,4-benzodioxine-6-sulfonamide
-
-
N-[4-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-3-methylphenyl]-N-ethylmethanesulfonamide
-
-
N-[4-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)phenyl]-N-(propan-2-yl)methanesulfonamide
-
-
N-[4-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)phenyl]-N-ethylmethanesulfonamide
-
-
N-[[1-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)azetidin-3-yl]methyl]-2,6-difluorobenzenesulfonamide
-
-
N-{3-[(3,4-dimethylphenyl)sulfamoyl]phenyl}acetamide
-
-
N-{4-[(2,3-dihydro-1,4-benzodioxin-6-ylsulfanyl)acetyl]phenyl}methanesulfonamide
-
-
N-{4-[(3,4-dimethylphenyl)sulfamoyl]phenyl}acetamide
-
-
phenyl 5-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-2-methyl-2,3-dihydro-1H-indole-1-sulfonate
-
-
phosphate
-
activation
phosphate
Pigeon
-
activation
phosphate
-
activation
phosphoenolpyruvate
Q9LBS6, -
-
phosphoenolpyruvate
-
homotropic activator of PK1, the modulation of oligomeric state by the allosteric effector phosphoenolpyruvate does not occur at a concentration of 10 nM or above
Phosphorylated hexoses
Pigeon
-
activation
-
Phosphorylated hexoses
-
activation
-
Phosphorylated hexoses
-
activation; requirement with Mg2+; with Mn2+
-
ribulose 5-phosphate
-
activation
Triton X-100
-
50% increase of activity of the bound enzyme only
Monovalent anions
-
activation, in decreasing order of efficiency: Cl-, Br-, NO3-
-
additional information
-
no activation by 6-phosphogluconate
-
additional information
-
the initial rate of catalysis is modulated by substrate activation by phosphoenolpyruvate and ADP, activation by AMP and inhibition by ATP, phosphate and carbamoyl phosphate
-
additional information
Busycotypus canaliculatum
-
interacting effects of various activators and inhibitors
-
additional information
-
no activation by glucose 1,6-diphosphate, 5'-IMP, 2',3'-AMP, 2',3'-GMP, 2',3'-UMP
-
additional information
-
enzyme is not affected by fructose-1,6-bisphosphate and glucose 6-phosphate
-
additional information
-
not activated by fructose 1,6-bisphosphate
-
additional information
-
not activated by 6-phosphogluconate
-
additional information
-
not activated by fructose 1,6-bisphosphate
-
additional information
A7LIU4, -
no stimulation: fructose 1,6-bisphosphate
-
additional information
-
no allosteric or regulatory effects are observed in the presence of D-fructose 1,6-diphosphate, D-fructose 2,6-diphosphate, D-glucose 6-phosphate, D-ribose 5-phosphate, AMP, ATP, ITP, AMP, L-His, L-Ser, L-Ala, L-Glu, Gln, L-Thr, L-Met, Gly, L-le, L-Asn, L-Cys, L-Pro, L-Arg, L-Lys, L-Phe, L-Trp, L-Leu, L-Asp, L-Val (1 mM each), L-Tyr (0.5 mM), or 0.1 mM acetyl-CoA
-
additional information
Q6GG09
no activation by fructose 1,6-bisphosphate
-
additional information
-
2-oxo-N-aryl-1,2,3,4-tetrahydroquinoline-6-sulfonamides as activators of the tumor cell specific M2 isoform of pyruvate kinase, synthesis, structure-activity relationships, selectivity, and notable physiochemical properties are, overview
-
additional information
-
1-(sulfonyl)-5-(arylsulfonyl)indoline as activators of the tumor cell specific M2 isoform of pyruvate kinase, synthesis, structure-activity relationship analysis, enzyme active site docking, enzymatic reaction kinetics, selectivity, and pharmaceutical properties, overview. Activating potencies of the compounds compared for isozymes PKM2 and PKM1
-
additional information
-
no significant effect by D-fructose 6-phosphate and D-ribulose 1,5-bisphosphate
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.03
0.05
ADP
-
25C, pH 7.9
0.03
0.05
ADP
-
PKc-isozyme
0.046
-
ADP
-
at pH 7.4
0.055
-
ADP
-
at pH 7.4, in the presence of 10 mM glutamate
0.075
-
ADP
-
pH 6.8, 24C
0.082
0.4
ADP
-
L-type isozyme, pH 7.4, 37C
0.082
0.4
ADP
-
pH 7.1, 37C
0.082
0.4
ADP
-
pH 7.4, 25C
0.09
-
ADP
-
at pH 6.4
0.0965
-
ADP
-
pH 7.0, 25C
0.101
-
ADP
-
at pH 6.4, in the presence of 10 mM glutamate
0.12
-
ADP
-
cosubstrate UDP, isozyme PKc, 25C, pH 7.9
0.12
-
ADP
Musa cavendishii
-
hyperbolic saturation kinetics, pH 6.9, 25C
0.14
-
ADP
-
pH 8.0, 24C
0.16
0.17
ADP
-
pH 6.5, 25C
0.16
0.17
ADP
-
-
0.16
0.17
ADP
-
-
0.16
-
ADP
-
pH 6.2, 30C
0.16
-
ADP
-
30C, pH 8.5
0.17
-
ADP
-
30C, pH 7.5
0.2
0.35
ADP
-
-
0.2
0.35
ADP
-
enzyme form I
0.2
0.35
ADP
-
-
0.2
0.35
ADP
Cardium tuberculatum
-
-
0.2
0.35
ADP
-
M-type isozyme, 25C, pH 7.0
0.2
0.35
ADP
Busycotypus canaliculatum
-
pH 7.0, 20C
0.2
0.35
ADP
-
25C, pH 7.9; PKp-isozyme
0.2
0.35
ADP
-
PKp-isozyme
0.2
0.35
ADP
-
30C, pH 6.8; enzyme form I
0.214
-
ADP
-
mutant E451W, pH 7.5; wild-type, pH 7.5
0.235
-
ADP
-
-
0.24
-
ADP
-
30C, pH 6.5
0.24
-
ADP
Q9LBS6, -
allosteric enzyme, pH 7.0
0.24
-
ADP
-
pH 8.0, 32C, activation by 2 mM D-fructose-1,6-bisphosphate
0.3
-
ADP
-
pH 7.4
0.31
-
ADP
-
pH 7.4, 30C
0.34
-
ADP
-
pH 8.0, 32C
0.39
-
ADP
-
in the presence of glucose 6-phosphate, pH 7.5
0.4
0.6
ADP
Pigeon
-
-
0.4
0.6
ADP
-
R-type isozyme, pH 7.4, 37C
0.4
0.6
ADP
-
pH 7.4, 37C
0.46
-
ADP
-
solubilized enzyme
0.52
0.56
ADP
-
bound enzyme
0.6
-
ADP
-
at 25C
0.6
-
ADP
-
50C, pH not specified in the publication
0.7
-
ADP
-
in the presence of Mg2+, pH 7.1, 30C
0.7
-
ADP
-
50C, pH 7.0
0.83
-
ADP
-
in the presence of ATP, pH 7.4, 37C
0.98
1
ADP
-
M1-type isozyme, pH 7.4, 37C
1.05
-
ADP
-
apparent value
1.4
1.5
ADP
-
M2-type isozyme, pH 7.4, 37C
2
-
ADP
-
mutant enzyme E117K, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
2.3
-
ADP
-
wild type enzyme, in the presence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
7.99
-
ADP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37C
14.1
-
ADP
-
wild type enzyme, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25Cin 50 mM Mes-Tris, pH 6.0, at 25C
0.35
-
ATP
Q9LBS6, -
allosteric enzyme, pH 7.0
2.53
-
CDP
-
pH 7.4, 25C
6.8
-
CDP
-
isozyme PKII, pH 7.1, 25C
9
-
CDP
-
isozyme PKI, pH 7.1, 25C
0.026
-
GDP
-
pH 7.5
0.0544
-
GDP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37C
0.098
0.1
GDP
-
-
0.098
0.1
GDP
-
pH 7.4, 25C
0.098
0.1
GDP
-
pH 7.5, 25C
0.25
0.26
GDP
-
IDP, isozyme PKc, 25C, pH 7.9
0.25
0.26
GDP
-
UDP, at pH 7.5
0.67
-
GDP
-
pH 7.1, 37C
1.1
-
GDP
-
pH 7.1, 25C
2.2
-
GDP
-
isozyme PKp, 25C, pH 7.9
0.049
0.1
IDP
-
cosubstrate phosphoenolpyruvate
0.049
0.1
IDP
Cardium tuberculatum
-
cosubstrate phosphoenolpyruvate
0.049
0.1
IDP
-
cosubstrate phosphoenolpyruvate
0.049
0.1
IDP
-
cosubstrate phosphoenolpyruvate
0.049
0.1
IDP
-
cosubstrate phosphoenolpyruvate
0.049
0.1
IDP
-
cosubstrate phosphoenolpyruvate
0.049
0.1
IDP
-
25C, pH 7.9; cosubstrate phosphoenolpyruvate
0.049
0.1
IDP
-
cosubstrate phosphoenolpyruvate; isozyme PKc
0.193
-
IDP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37C
4
-
IDP
-
isozyme PKp, 25C, pH 7.9
0.037
-
MgADP-
-
pH 7.5, 30C
0.0003
-
phosphoenolpyruvate
-
Y235F mutant, Vmax = 0.6 micromol/min/mg
0.0018
-
phosphoenolpyruvate
-
Y235A mutant, Vmax = 1.1 micromol/min/mg; Y235S mutant, Vmax = 1.2 micromol/min/mg
0.0019
-
phosphoenolpyruvate
-
wild-type, Vmax = 3.8 micromol/min/mg
0.02
0.03
phosphoenolpyruvate
-
solubilized enzyme
0.02
0.05
phosphoenolpyruvate
-
bound enzyme
0.021
-
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mn2+- and fructose 1,6-bisphosphate activated
0.024
-
phosphoenolpyruvate
-
15, pH 7.0, isoform PK I, in winter
0.033
-
phosphoenolpyruvate
-
15, pH 7.0, isoform PK I, in summer
0.033
-
phosphoenolpyruvate
-
pH 7.5, 30C
0.04
0.063
phosphoenolpyruvate
-
-
0.04
0.063
phosphoenolpyruvate
-
-
0.04
0.063
phosphoenolpyruvate
-
-
0.04
0.063
phosphoenolpyruvate
-
in the presence of fructose 1,6-diphosphate
0.04
0.063
phosphoenolpyruvate
-
-
0.04
0.063
phosphoenolpyruvate
-
-
0.04
0.063
phosphoenolpyruvate
-
in the presence of fructose 1,6-diphosphate
0.04
0.063
phosphoenolpyruvate
Busycotypus canaliculatum
-
in the absence of fructose 1,6-diphosphate; in the presence of fructose 1,6-diphosphate; pH 7.0, 20C
0.04
0.063
phosphoenolpyruvate
-
25C, pH 7.9; 2 isozymes with different kinetic mechanisms
0.04
0.063
phosphoenolpyruvate
-
-
0.04
0.063
phosphoenolpyruvate
-
pH 7.5
0.04
0.063
phosphoenolpyruvate
-
-
0.045
-
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mn2+-activated
0.046
-
phosphoenolpyruvate
-
at pH 7.4
0.05
-
phosphoenolpyruvate
-
30C, pH 8.5
0.05
-
phosphoenolpyruvate
-
-
0.052
-
phosphoenolpyruvate
-
24C, pH 8.0
0.059
-
phosphoenolpyruvate
-
activated by fructose D-1,6-bisphosphate
0.064
-
phosphoenolpyruvate
-
-
0.066
-
phosphoenolpyruvate
-
pH 6.2, mutant enzyme T298C, Mn2+- and fructose 1,6-bisphosphate activated
0.07
-
phosphoenolpyruvate
-
apparent value
0.082
-
phosphoenolpyruvate
-
at pH 6.4
0.089
-
phosphoenolpyruvate
-
pH 6.5, 30C
0.09
-
phosphoenolpyruvate
-
30C, pH 7.5
0.093
-
phosphoenolpyruvate
-
at pH 7.4, in the presence of 10 mM glutamate
0.098
-
phosphoenolpyruvate
Musa cavendishii
-
hyperbolic saturation kinetics, pH 6.9, 25C
0.099
-
phosphoenolpyruvate
-
pH 6.2, 30C
0.1
-
phosphoenolpyruvate
-
pH 6.8, 30C
0.1
-
phosphoenolpyruvate
-
in the presence of D-fructose 1,6-bisphosphate
0.11
-
phosphoenolpyruvate
Q9LBS6, -
allosteric enzyme, pH 7.0
0.112
-
phosphoenolpyruvate
P30613
mutant C436M, pH not specified in the publication, 30C
0.113
-
phosphoenolpyruvate
-
mutant enzyme C9S/C268S, in the presence of 0.1 mM ribose 5'-phosphate, in 50 mM imidazole-HCl buffer, pH 7.2, 50 mM KCl, 7 mM MgCl2, 0.12 mM NADH, 0.02 mg/ml lactate dehydrogenase, 2 mM PEP, and 4 mM ADP, at 30C
0.116
-
phosphoenolpyruvate
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37C
0.12
-
phosphoenolpyruvate
-
pH 6.8, 24C
0.12
-
phosphoenolpyruvate
-
30C, pH 6.5
0.13
-
phosphoenolpyruvate
-
wild type enzyme, in the presence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
0.15
0.16
phosphoenolpyruvate
-
-
0.15
0.16
phosphoenolpyruvate
-
enzyme form I
0.15
-
phosphoenolpyruvate
-
at pH 6.4, in the presence of 10 mM glutamate
0.17
-
phosphoenolpyruvate
-
pH 8.0, 32C, activation by 2 mM D-fructose-1,6-bisphosphate
0.1785
-
phosphoenolpyruvate
-
pH 7.0, 25C
0.18
-
phosphoenolpyruvate
-
cosubstrate ADP
0.18
-
phosphoenolpyruvate
-
cosubstrate ADP; L-type isozyme, 25C, pH 7.0
0.18
-
phosphoenolpyruvate
-
pH 7.4, 37C
0.18
-
phosphoenolpyruvate
-
isozyme PKp
0.181
-
phosphoenolpyruvate
-
15, pH 7.0, isoform PK II, in summer
0.186
-
phosphoenolpyruvate
-
wild type enzyme, in the presence of 0.1 mM ribose 5'-phosphate, in 50 mM imidazole-HCl buffer, pH 7.2, 50 mM KCl, 7 mM MgCl2, 0.12 mM NADH, 0.02 mg/ml lactate dehydrogenase, 2 mM PEP, and 4 mM ADP, at 30C
0.19
-
phosphoenolpyruvate
-
-
0.193
-
phosphoenolpyruvate
-
15, pH 7.0, isoform PK II, in winter
0.2
-
phosphoenolpyruvate
-
pH 7.1, 30C, in the presence of Mg2+, 7fold lower in the presence of Mn2+
0.21
-
phosphoenolpyruvate
-
26C
0.22
-
phosphoenolpyruvate
-
in the presence of glucose 6-phosphate, at pH 7.5
0.22
-
phosphoenolpyruvate
-
enzyme from larva
0.24
-
phosphoenolpyruvate
-
mutant enzyme E117K, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
0.24
-
phosphoenolpyruvate
P30613
wild-type enzyme, pH not specified in the publication, 30C
0.242
-
phosphoenolpyruvate
-
pH 6.2, mutant enzyme T298C, Mn2+-activated
0.26
-
phosphoenolpyruvate
-
enzyme from adult
0.27
-
phosphoenolpyruvate
-
in the absence of the high-affinity IgE receptor FcepsilonRI
0.3
0.96
phosphoenolpyruvate
-
L-type, pH 7.4, 37C
0.31
-
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mg2+ and fructose 1,6-bisphosphate activated
0.345
-
phosphoenolpyruvate
P30613
mutant C436H, pH not specified in the publication, 30C
0.35
-
phosphoenolpyruvate
-
-
0.372
-
phosphoenolpyruvate
P30613
mutant C436A, pH not specified in the publication, 30C
0.4
0.57
phosphoenolpyruvate
Pigeon
-
-
0.4
0.57
phosphoenolpyruvate
-
M2-type isozyme, pH 7.4, 37C
0.4
0.57
phosphoenolpyruvate
-
pH 7.4, 37C
0.4
0.57
phosphoenolpyruvate
-
-
0.41
-
phosphoenolpyruvate
-
pH 7.4, 30C
0.45
-
phosphoenolpyruvate
-
allosteric enzyme, pH 7.5, 24C
0.54
-
phosphoenolpyruvate
-
allosteric enzyme, pH 7.0, 24C
0.552
-
phosphoenolpyruvate
P30613
mutant S12D, pH not specified in the publication, 30C
0.59
-
phosphoenolpyruvate
-
in the presence of the high-affinity IgE receptor FcepsilonRI
0.6
-
phosphoenolpyruvate
-
enzyme from pupae
0.61
-
phosphoenolpyruvate
-
wild type enzyme, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
0.703
-
phosphoenolpyruvate
P30613
mutant C436N, pH not specified in the publication, 30C
0.768
-
phosphoenolpyruvate
P30613
mutant C436T, pH not specified in the publication, 30C
0.802
-
phosphoenolpyruvate
P30613
mutant C436S, pH not specified in the publication, 30C
0.804
-
phosphoenolpyruvate
P30613
mutant C436D, pH not specified in the publication, 30C
0.88
-
phosphoenolpyruvate
-
in the presence of alanine
0.9
-
phosphoenolpyruvate
-
-
1.05
-
phosphoenolpyruvate
-
26C
1.1
-
phosphoenolpyruvate
-
at 25C
1.18
-
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mg2+-activated
1.3
-
phosphoenolpyruvate
-
pH 7.4
1.4
-
phosphoenolpyruvate
-
R-type isozyme, pH 7.4, 37C
1.5
-
phosphoenolpyruvate
-
in the absence of activator
2.1
-
phosphoenolpyruvate
-
pH 8.0, 32C
3.3
-
phosphoenolpyruvate
-
50C, pH not specified in the publication
4.43
-
phosphoenolpyruvate
-
pH 6.2, mutant enzyme T298C, Mg2+- and fructose 1,6-bisphosphate activated
0.025
-
pyruvate
-
25C, sample taken in June
0.055
-
pyruvate
-
25C, sample taken in January
0.48
-
pyruvate
Q9LBS6, -
allosteric enzyme, pH 7.0
0.41
-
UDP
-
pH 7.4, 25C
0.72
0.73
UDP
-
pH 7.1, 25C
1.25
-
UDP
-
pH 7.1, 37C
2.4
-
UDP
-
isozyme PKp, 25C, pH 7.9
0.087
-
MgADP-
-
pH 6.5, 30C
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
kinetic properties
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
kinetic properties; kinetic study
-
additional information
-
additional information
-
kinetic properties
-
additional information
-
additional information
-
kinetic properties compared to pyruvate kinase from other insects
-
additional information
-
additional information
-
alteration of kinetic properties by purification
-
additional information
-
additional information
-
kinetic properties; pH-dependence
-
additional information
-
additional information
-
kinetic properties
-
additional information
-
additional information
-
kinetic parameters
-
additional information
-
additional information
-
allosteric pattern dissappears at pH 5.9
-
additional information
-
additional information
-
allosteric enzyme; kinetic properties; kinetic properties of phosphorylated and dephosphorylated kinases
-
additional information
-
additional information
-
kinetic parameters
-
additional information
-
additional information
-
kinetic parameters
-
additional information
-
additional information
Busycotypus canaliculatum
-
kinetic properties
-
additional information
-
additional information
Busycotypus canaliculatum
-
kinetic parameters
-
additional information
-
additional information
-
kinetic parameters
-
additional information
-
additional information
-
kinetic parameters
-
additional information
-
additional information
-
kinetic properties; kinetic properties of different MW-forms of Chlorella kinase
-
additional information
-
additional information
-
kinetics overview
-
additional information
-
additional information
-
kinetic parameters; kinetics overview
-
additional information
-
additional information
-
kinetics overview
-
additional information
-
additional information
-
kinetic parameters; kinetics overview
-
additional information
-
additional information
-
kinetics overview
-
additional information
-
additional information
-
kinetic parameters; kinetics overview
-
additional information
-
additional information
-
kinetics overview
-
additional information
-
additional information
-
kinetic parameters
-
additional information
-
additional information
-
kinetic parameters
-
additional information
-
additional information
-
kinetic parameters
-
additional information
-
additional information
-
kinetic parameters
-
additional information
-
additional information
-
hyperbolic saturation kinetics for phosphoenolpyruvate, ADP, Mg2+, K+
-
additional information
-
additional information
-
assay and kinetics overview
-
additional information
-
additional information
Q10208
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
coupled assay for leaf crude extracts
-
additional information
-
additional information
-
influence of fructose 1,6-bisphosphate on kinetics
-
additional information
-
additional information
-
Km value of the enzyme towards phosphoenolpyruvate is higher in the pupae stage than in the rest developmental stages although the same enzyme type appears to be present throughout the life span of the insect. Starvation results to activation of the enzyme by increasing the Km value in the two feeding stages, namely larvae and adult, while injury has the opposite effect
-
additional information
-
additional information
A7LIU4, -
in the presence of the effector fructose 2,6-bisphosphate the enzyme displays a hyperbolic saturation curve, whereas in the absence of fructose 2,6-bisphosphate the curve is sigmoid. The phosphoenolpyruvate concentration for S0.5 in presence of fructose 2,6-bisphosphate is 0.08 mM, and 1.16 mM in absence, with a concomitant increase in Vmax from 492.1 U/mg in absence to 506.99 U/mg in presence of fructose 2,6-bisphosphate. For ADP, a Km of 0.32 mM has been calculated
-
additional information
-
additional information
-
S0.5 value of phosphoenolpyruvate is 1.06 mM for wild-type, 1.3 mM for mutant E451W
-
additional information
-
additional information
Q6GG09
steady-state kinetics of recombinant wild-type and truncated PKin the absence or presence of 1 mM AMP as a function of phosphoenolpyruvate
-
additional information
-
additional information
P30613
phosphoenolpyruvate affinity is sensitive to the nature of the side chain at position 436
-
additional information
-
additional information
-
kinetics, in presence of saturated substrate concentration, the enzyme exhibits hyperbolic kinetics for both ADP and PEP
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
47.6
-
ADP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37C
110
-
GDP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37C
131
-
IDP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37C
1.97
-
phosphoenolpyruvate
-
mutant enzyme T298A, activated be Tl+ and Mn2+
3.2
-
phosphoenolpyruvate
-
wild type enzyme, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
12.1
-
phosphoenolpyruvate
-
pH 6.2, mutant enzyme T298C, Mn2+-activated
12.2
-
phosphoenolpyruvate
-
mutant enzyme T298C, activated be Tl+ and Mn2+
13.9
-
phosphoenolpyruvate
-
pH 6.2, mutant enzyme T298C, Mn2+- and fructose 1,6-bisphosphate activated
21.5
-
phosphoenolpyruvate
-
mutant enzyme T298S, activated be Tl+ and Mn2+
41.3
-
phosphoenolpyruvate
-
pH 6.2, mutant enzyme T298C, Mg2+- and fructose 1,6-bisphosphate activated
58.4
-
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mn2+-activated
66
-
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mn2+- and fructose 1,6-bisphosphate activated
161
-
phosphoenolpyruvate
-
mutant enzyme E117K, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
226
-
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mg2+ and fructose 1,6-bisphosphate activated
232
-
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mg2+-activated
1182
-
phosphoenolpyruvate
-
wild type enzyme, in the presence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
1736
-
phosphoenolpyruvate
-
mutant enzyme C9S/C268S, in the presence of 0.1 mM ribose 5'-phosphate, in 50 mM imidazole-HCl buffer, pH 7.2, 50 mM KCl, 7 mM MgCl2, 0.12 mM NADH, 0.02 mg/ml lactate dehydrogenase, 2 mM PEP, and 4 mM ADP, at 30C
3204
-
phosphoenolpyruvate
-
wild type enzyme, in the presence of 0.1 mM ribose 5'-phosphate, in 50 mM imidazole-HCl buffer, pH 7.2, 50 mM KCl, 7 mM MgCl2, 0.12 mM NADH, 0.02 mg/ml lactate dehydrogenase, 2 mM PEP, and 4 mM ADP, at 30C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6
-
ADP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37C
6504
2020
-
GDP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37C
10807
681
-
IDP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37C
11572
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0005
-
ADP-Cr2+
-
mutant enzyme E117K, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
0.0013
-
ADP-Cr2+
-
wild type enzyme, in the presence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
0.0028
-
ADP-Cr2+
-
wild type enzyme, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
0.8
-
citrate
-
with respect to ADP
3.7
-
L-glutamate
Musa cavendishii
-
cosubstrate MgADP-, pH 7.5, 25C
4.4
-
L-glutamate
Musa cavendishii
-
cosubstrate phosphoenolpyruvate, pH 7.5, 25C
13.6
-
L-glutamate
Musa cavendishii
-
cosubstrate phosphoenolpyruvate, pH 6.9, 25C
19.2
-
L-glutamate
Musa cavendishii
-
cosubstrate MgADP-, pH 6.9, 25C
0.067
-
L-Phe
-
mutant enzyme K422R, in the absence of D-fructose 1,6-bisphosphate
0.162
-
L-Phe
-
mutant enzyme K422R, in the presence of 2.5 mM D-fructose 1,6-bisphosphate
0.176
-
L-Phe
-
wild type enzyme, in the absence of D-fructose 1,6-bisphosphate
0.261
-
L-Phe
-
wild type enzyme, in the presence of 2.5 mM D-fructose 1,6-bisphosphate
1.431
-
L-Phe
-
mutant enzyme H391Y, in the absence of D-fructose 1,6-bisphosphate
1.78
-
L-Phe
-
mutant enzyme H391Y, in the presence of 2.5 mM D-fructose 1,6-bisphosphate
1.77
-
MgATP2-
-
37C, pH 7.0
3.9
-
MgATP2-
Musa cavendishii
-
cosubstrate MgADP-, pH 6.9, 25C
4
-
MgATP2-
Musa cavendishii
-
cosubstrate MgADP-, pH 7.5, 25C
9.6
-
MgATP2-
Musa cavendishii
-
cosubstrate phosphoenolpyruvate, pH 6.9, 25C
10
-
MgATP2-
Musa cavendishii
-
cosubstrate phosphoenolpyruvate, pH 7.5, 25C
0.0048
-
oxalate
-
mutant enzyme E117K, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
0.029
-
oxalate
-
wild type enzyme, in the presence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
0.077
-
oxalate
-
wild type enzyme, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25C
1.9
-
tryptophan
-
apparent value
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000185
-
(2-[(1E)-1-[2-(5-bromo-2-hydroxybenzoyl)hydrazinylidene]ethyl]-1-methyl-1H-indol-6-yl)dibromanium
-
pH not specified in the publication, 30C
1.5e-05
-
(E)-5-bromo-2-hydroxy-N'-(1-(4,5,6-trifluoro-1Hindol-2-yl)ethylidene)benzohydrazide
-
pH 7.5, 30C
0.000214
-
(E)-5-bromo-2-hydroxy-N'-(1-(5-hydroxy-1H-indol-2-yl)ethylidene)benzohydrazide
-
pH 7.5, 30C
0.000178
-
(E)-5-bromo-2-hydroxy-N'-(1-(5-methoxy-1H-indol-2-yl)ethylidene)benzohydrazide
-
pH 7.5, 30C
2.4e-05
-
(E)-5-bromo-N'-(1-(4,5-difluoro-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
pH 7.5, 30C
2e-05
-
(E)-5-bromo-N'-(1-(5,6-difluoro-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
pH 7.5, 30C
4.9e-05
-
(E)-5-bromo-N'-(1-(5-bromo-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
pH 7.5, 30C
0.000451
-
(E)-5-bromo-N'-(1-(5-bromo-1H-indol-2-yl)propylidene)-2-hydroxybenzohydrazide
-
pH 7.5, 30C
5.2e-05
-
(E)-5-bromo-N'-(1-(5-chloro-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
pH 7.5, 30C
4.9e-05
-
(E)-5-bromo-N'-(1-(5-fluoro-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
pH 7.5, 30C
2.4e-05
-
(E)-5-bromo-N'-(1-(6-bromo-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
pH 7.5, 30C
0.000863
-
(E)-N'-((1H-indol-2-yl)methylene)-5-bromo-2-hydroxybenzohydrazide
-
pH 7.5, 30C
0.000151
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-2-hydroxy-5-iodobenzohydrazide
-
pH 7.5, 30C
0.008615
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
-
pH 7.5, 30C
7.4e-05
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-3,5-dibromo-2-hydroxybenzohydrazide
-
pH 7.5, 30C
0.00815
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-3-bromobenzohydrazide
-
pH 7.5, 30C
0.001312
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-4-bromo-2-hydroxybenzohydrazide
-
pH 7.5, 30C
6.4e-05
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-5-bromo-2-(prop-2-ynyloxy)benzohydrazide
-
pH 7.5, 30C
0.000324
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-5-bromo-2-hydroxy-4-methoxybenzohydrazide
-
pH 7.5, 30C
8.5e-05
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-5-bromo-2-hydroxybenzohydrazide
-
pH 7.5, 30C
0.000182
-
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-5-bromo-2-methoxybenzohydrazide
-
pH 7.5, 30C
0.000126
-
(E)-N'-(1-(1H-indol-2-yl)propylidene)-5-bromo-2-hydroxybenzohydrazide
-
pH 7.5, 30C
4.9e-05
-
(E)-N'-[(1H-indol-2-yl)methylene]-5-bromo-2-methoxybenzohydrazide
-
pH 7.5, 30C
-
6.3e-05
-
(E)-N'-[1-(1H-indol-2-yl)ethylidene]-5-bromo-2-ethoxybenzohydrazide
-
pH 7.5, 30C
0.000445
-
(E/Z)-N'-((1H-indol-2-yl)(phenyl)methylene)-5-bromo-2-hydroxybenzohydrazide
-
pH 7.5, 30C
0.000483
-
2-hydroxy-5-iodo-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
pH 7.5, 30C
0.01
-
3-(2,5-dimethylphenoxy)-1,2-benzothiazole 1,1-dioxide
-
pH 7.2, 25C
4.2e-05
-
3-hydroxy-N'-[(1E)-1-(1H-indol-2-yl)ethylidene]naphthalene-2-carbohydrazide
-
pH 7.5, 30C
5.9e-05
-
3-hydroxy-N'-[(1E)-1-(4,5,6-trifluoro-1-methyl-1H-indol-2-yl)ethylidene]naphthalene-2-carbohydrazide
-
pH 7.5, 30C
5.2e-05
-
3-hydroxy-N'-[(1E)-1-(4,5,6-trifluoro-1-methyl-1H-indol-2-yl)propylidene]naphthalene-2-carbohydrazide
-
pH 7.5, 30C
3.1e-05
-
3-hydroxy-N'-[(1E)-1-(4,5,6-trifluoro-1H-indol-2-yl)propylidene]naphthalene-2-carbohydrazide
-
pH 7.5, 30C
0.005
-
3-[(2,5-dimethylphenyl)sulfanyl]-1,2-benzothiazole 1,1-dioxide
-
pH 7.2, 25C
0.028
-
4-amino-2-methylnaphthalen-1-ol
-
pH 7.5, 25C, recombinant His6-tagged isozyme PKM2, in absence of D-fructose 1,6-bisphosphate
-
0.045
-
4-amino-2-methylnaphthalen-1-ol
-
pH 7.5, 25C, recombinant His6-tagged isozyme PKM2, in presence of D-fructose 1,6-bisphosphate
-
0.12
-
4-amino-2-methylnaphthalen-1-ol
-
pH 7.5, 25C, recombinant His6-tagged isozyme PKL, in absence of D-fructose 1,6-bisphosphate
-
0.191
-
4-amino-2-methylnaphthalen-1-ol
-
pH 7.5, 25C, recombinant His6-tagged isozyme PKM1, in absence of D-fructose 1,6-bisphosphate
-
0.01
-
5-(2,5-dimethyl-1H-pyrrol-1-yl)-2-hydroxybenzoic acid
-
in 50 mM Tris, pH 7.5, at 22C
-
0.000251
-
5-bromo-2-(ethoxymethoxy)-N'-((1E)-1-(1H-indol-2-yl)ethylidene)benzohydrazide
-
pH 7.5, 30C
0.000841
-
5-bromo-2-hydroxy-4-methoxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
pH 7.5, 30C
0.000227
-
5-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-benzimidazol-2-yl)ethylidene]benzohydrazide
-
pH 7.5, 30C
0.000381
-
5-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
pH not specified in the publication, 30C
0.000381
-
5-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
pH 7.5, 30C
0.000461
-
5-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)propylidene]benzohydrazide
-
pH 7.5, 30C
8.4e-05
-
5-bromo-2-hydroxy-N'-[(1E)-1-(1H-indol-2-yl)ethylidene]benzohydrazide
-
pH not specified in the publication, 30C
0.000114
-
5-bromo-2-hydroxy-N'-[(1E)-1-(1H-indol-2-yl)propylidene]benzohydrazide
-
pH not specified in the publication, 30C
5.5e-05
-
5-bromo-2-hydroxy-N'-[(1E)-1-(4,5,6-trifluoro-1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
pH 7.5, 30C
4.3e-05
-
5-bromo-2-hydroxy-N'-[(1E)-1-(5-iodo-1H-indol-2-yl)ethylidene]benzohydrazide
-
pH 7.5, 30C
0.000794
-
5-bromo-2-hydroxy-N'-[(1E)-1-(5-methoxy-1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
pH 7.5, 30C
0.006043
-
5-bromo-2-hydroxy-N'-[(E)-(1-methyl-1H-indol-2-yl)(phenyl)methylidene]benzohydrazide
-
pH 7.5, 30C
0.003087
-
5-bromo-2-hydroxy-N'-[(E)-(1-methyl-1H-indol-2-yl)methylidene]benzohydrazide
-
pH 7.5, 30C
0.000145
-
5-bromo-N'-[(1E)-1-(4,5-difluoro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
pH 7.5, 30C
6.1e-05
-
5-bromo-N'-[(1E)-1-(5,6-difluoro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
pH 7.5, 30C
1.6e-05
-
5-bromo-N'-[(1E)-1-(5,6-difluoro-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
pH not specified in the publication, 30C
0.000146
-
5-bromo-N'-[(1E)-1-(5-bromo-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
pH 7.5, 30C
0.000168
-
5-bromo-N'-[(1E)-1-(5-bromo-1-methyl-1H-indol-2-yl)propylidene]-2-hydroxybenzohydrazide
-
pH 7.5, 30C
0.000228
-
5-bromo-N'-[(1E)-1-(5-chloro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
pH 7.5, 30C
0.000165
-
5-bromo-N'-[(1E)-1-(5-fluoro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
pH 7.5, 30C
1.7e-05
-
5-bromo-N'-[(1E)-1-(6-bromo-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
pH 7.5, 30C
0.000228
-
5-bromo-N'-[(1E)-1-(6-chloro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
pH not specified in the publication, 30C
0.000165
-
5-bromo-N'-[(1E)-1-(6-fluoro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
pH not specified in the publication, 30C
4.5e-05
-
5-bromo-N'-[(1E)-1-(6-fluoro-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
-
pH not specified in the publication, 30C
5
-
ATP
-
pH 7.0, 25C
13.7
-
ATP
-
IC50: 8.8 mM at pH 6.4, IC50: 13.7 mM at pH 7.4
3.64
-
citrate
-
pH 7.0, 25C
14.2
-
citrate
-
IC50: 9.2 mM at pH 6.4, IC50: 14.2 mM at pH 7.4
8
-
D-fructose 1,6-bisphosphate
-
IC50: 8.4 mM at pH 6.4, IC50: 8.0 mM at pH 7.4
17.2
-
diphosphate
-
IC50: 9.8 mM at pH 6.4, IC50: 17.2 mM at pH 7.4
1.2
-
glutamate
-
IC50: 2.5 mM at pH 6.4, IC50: 1.2 mM at pH 7.4
6.2
-
L-glutamate
-
5 mM, 30% of activity remaining, IC50: 2.1 mM, IC50: 6.2 mM; 5 mM, 59% of activity remaining, IC50: 6.2 mM
0.15
-
menadione
-
pH 7.5, 25C, recombinant His6-tagged isozyme PKM2, in absence of D-fructose 1,6-bisphosphate
0.381
-
menadione
-
pH 7.5, 25C, recombinant His6-tagged isozyme PKM2, in presence of D-fructose 1,6-bisphosphate
0.837
-
menadione
-
pH 7.5, 25C, recombinant His6-tagged isozyme PKL, in absence of D-fructose 1,6-bisphosphate
3.407
-
menadione
-
pH 7.5, 25C, recombinant His6-tagged isozyme PKM1, in absence of D-fructose 1,6-bisphosphate
0.000224
-
N'-[(1E)-1-(1,3-benzothiazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
-
pH 7.5, 30C
0.000286
-
N'-[(1E)-1-(1-benzothiophen-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
-
pH 7.5, 30C
9.1e-05
-
N'-[(1E)-1-(1H-benzimidazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
-
pH not specified in the publication, 30C
9.1e-05
-
N'-[(1E)-1-(1H-benzimidazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
-
pH 7.5, 30C
0.000115
-
N'-[(1E)-1-(5-bromo-1-methyl-1H-indol-2-yl)ethylidene]-3-hydroxynaphthalene-2-carbohydrazide
-
pH 7.5, 30C
7.9e-05
-
N'-[(1E)-1-(5-bromo-1-methyl-1H-indol-2-yl)propylidene]-3-hydroxynaphthalene-2-carbohydrazide
-
pH 7.5, 30C
2.6e-05
-
N'-[(1E)-1-(5-bromo-1H-indol-2-yl)ethylidene]-3-hydroxynaphthalene-2-carbohydrazide
-
pH 7.5, 30C
1.8e-05
-
N'-[(1E)-1-(5-bromo-1H-indol-2-yl)propylidene]-3-hydroxynaphthalene-2-carbohydrazide
-
pH 7.5, 30C
0.00091
-
N'-[(3Z)-1-ethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-3-hydroxynaphthalene-2-carbohydrazide
-
pH not specified in the publication, 30C
0.0593
-
N-(3-carboxy-4-hydroxy)phenyl-2,5-dimethylpyrrole
-
pH 7.5, 25C, recombinant His6-tagged isozyme PKM2, in absence of D-fructose 1,6-bisphosphate
-
0.0775
-
N-(3-carboxy-4-hydroxy)phenyl-2,5-dimethylpyrrole
-
pH 7.5, 25C, recombinant His6-tagged isozyme PKM2, in presence of D-fructose 1,6-bisphosphate
-
0.41
-
oxalate
-
0.2 mM, 71% of activity remaining, IC50: 0.41 mM
0.02
-
[(5Z)-5-(4-[[(2-iodophenyl)carbonyl]oxy]benzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
in 50 mM Tris, pH 7.5, at 22C
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.001
-
-
below, wild-type strain DSM133, pH 7.5, 55C
0.02
-
-
in the absence of K+
0.028
-
-
50C, pH not specified in the publication, enzyme from lactate-grown cells
0.039
-
-
clarified extract
0.05
-
Trichosporonoides megachiliensis
-
-
0.12
-
-
sperm homogenate
0.13
-
-
50C, pH not specified in the publication, enzyme from starch-grown cells
0.14
-
-
mutant strain YD01, pH 7.5, 55C
0.52
-
-
mutant strain DS8, pH 7.5, 55C
0.84
-
-
mutant strain YD02, pH 7.5, 55C
51
-
-
pH 6.8, 24C
51
-
-
pH 6.5, 30C
59
-
Musa cavendishii
-
pH 6.9, 25C
68.2
-
A7LIU4, -
mutant H480Q, pH 7.2, 25C
73.1
-
-
after 1874fold purification
85
-
-
purified recombinant PykA, pH 7.5, 30C
98
-
A7LIU4, -
mutant K453L/H480Q, pH 7.2, 25C
108
-
-
purified recombinant PykF, pH 7.5, 30C
116.7
-
-
after 972fold purification
156.9
-
A7LIU4, -
mutant K453L, pH 7.2, 25C
175
-
P51181
30C
178.1
-
A7LIU4, -
wild-type, pH 7.2, 25C
191
-
-
pH 7.4, 22C
201
-
-
pH 7.5, 60C
202
-
P51182, -
30C
203
-
-
pH 6.9, 30C
210
-
-
pH 7.1, 30C
218
-
-
isozyme PKp
233
-
-
25C, pH 7.0, M-type isozyme from neck muscle
250
-
-
in the presence of K+
307
-
-
pH 7.4, 37C, R-type isozyme
330
-
-
pH 8.0, 30C, erythrocyte enzyme
340
-
-
pH 6.2, 30C
368
-
Busycotypus canaliculatum
-
isozyme PK-aerobic, pH 7.0, 20C
380
-
-
M1-type isozyme, pH 7.4, 37C
380
-
-
M-type isozyme
397.5
-
-
K-type isozyme
420
-
-
liver enzyme, pH 8.0, 30C
520
-
-
M2-type isozyme, 25C, pH 7.4
593
-
-
pH 7.4, 37C
690.7
-
-
partially purified cytosolic isozyme, pH 7.0, 25C
770
-
-
M2-type isozyme, 37C, pH 7.4
780
-
-
M1-type isozyme, 37C, pH 7.4
1341
-
-
pH 7.1, 37C
1685
-
-
isozyme PK5, pH 6.5, 30C
additional information
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-
-
additional information
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-
-
additional information
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-
-
additional information
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Pigeon
-
-
additional information
-
-
-
additional information
-
Cardium tuberculatum
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
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-
-