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Information on EC 2.7.1.40 - pyruvate kinase and Organism(s) Homo sapiens and UniProt Accession P30613

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EC Tree
IUBMB Comments
UTP, GTP, CTP, ITP and dATP can also act as donors. Also phosphorylates hydroxylamine and fluoride in the presence of CO2.
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Homo sapiens
UNIPROT: P30613
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pyruvate kinase, m2-pk, pyruvate kinase m2, l-pk, pyk, tum2-pk, pyruvate kinase type m2, liver pyruvate kinase, pyruvate kinase m2 isoform, m2-pyruvate kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
liver pyruvate kinase
-
ATP/pyruvate O'-phosphotransferase
-
-
CTHBP
-
-
-
-
cytosolic thyroid hormone binding protein
-
-
-
-
erythroid (R-type) pyruvate kinase
-
-
fluorokinase
-
-
-
-
hL-PYK
-
-
hPKM2
kinase, fluoro- (phosphorylating)
-
-
-
-
kinase, pyruvate (phosphorylating)
-
-
-
-
L-PK
-
-
-
-
M1-PK
-
isozyme
M2 pyruvate kinase
-
-
M2 type phosphoenolpyruvate kinase
-
-
M2-PK
M2-pyruvate kinase
-
-
phosphoenol transphosphorylase
-
-
-
-
phosphoenolpyruvate kinase
PK-M2
-
-
PK-R
-
-
ProTalphaK
-
-
pyruvate kinase
-
pyruvate kinase isoenzyme M2
-
-
pyruvate kinase isoform M2
-
pyruvate kinase isoforms 2
-
pyruvate kinase M1
-
splice isoform of pyruvate kinase
pyruvate kinase M2
pyruvate kinase M2 isoform
-
pyruvate kinase muscle isoform 2
-
pyruvate kinase muscle isozyme
-
-
-
-
pyruvate kinase type M2
-
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:pyruvate 2-O-phosphotransferase
UTP, GTP, CTP, ITP and dATP can also act as donors. Also phosphorylates hydroxylamine and fluoride in the presence of CO2.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-59-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
ATP + AKT1S1
ADP + phospho-AKT1S1
show the reaction diagram
-
the enzyme phosphorylates Ser202 and Ser203 of AKT1S1
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
show the reaction diagram
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
GDP + phosphoenolpyruvate
GTP + pyruvate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
show the reaction diagram
ATP + AKT1S1
ADP + phospho-AKT1S1
show the reaction diagram
-
the enzyme phosphorylates Ser202 and Ser203 of AKT1S1
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
show the reaction diagram
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg
-
required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-alanine
-
(1,4-dimethoxynaphthalen-2-yl)methyl dipropylcarbamodithioate
-
(1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl diethylcarbamodithioate
-
(1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl morpholine-4-carbodithioate
-
(1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl piperidine-1-carbodithioate
-
(1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl [4-(piperazin-1-yl)phenyl]carbamodithioate
-
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) bis(diethylcarbamodithioate)
-
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) bis(dimethylcarbamodithioate)
-
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) bis(diprop-2-en-1-ylcarbamodithioate)
-
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) bis(dipropylcarbamodithioate)
-
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) di(1,3-thiazolidine-3-carbodithioate)
-
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) dimorpholine-4-carbodithioate
-
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) dipyrrolidine-1-carbodithioate
-
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) dithiomorpholine-4-carbodithioate
-
(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
(2E)-1-(4-methoxyphenyl)-3-(2,4,6-trimethoxyphenyl)prop-2-en-1-one
-
-
(2R,3S)-2-(3,4-diphenoxyphenyl)-3,5,7-triphenoxy-3,4-dihydro-2H-1-benzopyran
-
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl (4-methylpiperidin-1-yl)carbamodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl 1,3-thiazolidine-3-carbodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl 3,5-dimethylmorpholine-4-carbodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl 4-(propan-2-yl)piperazine-1-carbodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl 4-acetylpiperazine-1-carbodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl 4-methylpiperazine-1-carbodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl benzylcarbamodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl bis(2-hydroxyethyl)carbamodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl cyclohexyl(methyl)carbamodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl dibutylcarbamodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl diethylcarbamodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl diprop-2-en-1-ylcarbamodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl dipropylcarbamodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl methylcarbamodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl morpholine-4-carbodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl piperidin-1-ylcarbamodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl piperidine-1-carbodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl pyrrolidine-1-carbodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl thiomorpholine-4-carbodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl [(pyridin-2-yl)methyl]carbamodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl [(pyridin-3-yl)methyl]carbamodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl [(pyridin-4-yl)methyl]carbamodithioate
-
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl [2-(diethylamino)ethyl]carbamodithioate
-
2-aminoisobutyric acid
-
allosteric inhibition
3,5-diphenoxy-2-[(2E)-3-(3,4,5-triphenoxyphenyl)prop-2-en-1-yl]phenol
-
-
3-(2-hydroxy-4-methoxyphenyl)-1-(4-methoxyphenyl)propane-1,2-diol
-
-
3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl 4-acetylpiperazine-1-carbodithioate
-
3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl dipropylcarbamodithioate
-
3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl morpholine-4-carbodithioate
-
3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl piperidine-1-carbodithioate
-
3-oxo-3-(1H-pyrrolo[2,3-b]pyridin-3-yl)propyl [(pyridin-3-yl)methyl]carbamodithioate
-
3-oxo-3-phenylpropyl [(pyridin-3-yl)methyl]carbamodithioate
-
3-[4-(2,3-dihydro-1,4-benzodioxine-6-sulfonyl)-1,4-diazepane-1-sulfonyl]aniline
-
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
5,7-diphenoxy-2-(3,4,5-triphenoxyphenyl)-2H-1-benzopyran
-
-
5-(2,3-dihydro-1,4-benzodioxine-6-sulfonyl)-2-(methanesulfonyl)-2,3-dihydro-1H-isoindole
-
5-(2,5-dimethyl-1H-pyrrol-1-yl)-2-hydroxybenzoic acid
-
81% inhibition at 0.03 mM
6-[(3-aminophenyl)methyl]-4-methyl-2-[methyl(methylidene)-lambda4-sulfanyl]-4,6-dihydro-5H-thieno[2',3':4,5]pyrrolo[2,3-d]pyridazin-5-one
-
7-[(1H-benzimidazol-1-yl)methyl]-2,3-dimethyl-5H-[1,3]thiazolo[3,2-a]pyrimidin-5-one
-
A-Raf protein
proteins known for cellular growth and proliferation such as A-Raf and PML protein are known to downregulate PKM2 activity by interacting with it
-
ADP-Cr2+
-
-
alkannin
-
-
D-alanine
-
allosteric inhibition
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
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
human papillomavirus-16 E7
causes dissociation of PKM2 tetramer into inactive dimer
-
hydroxyl radical
-
inactivation
L-alanine
L-cysteine
L-Phe
23.5% activity left at 1 mM L-Phe in the absence of D-fructose 1,6-bisphosphate
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-proline
-
allosteric inhibition
L-valine
lysophosphatidic acid
-
menadione
-
i.e. vitamin K3, shows a significantly stronger potency to inhibit isozyme PKM2 than to inhibit isozymes PKM1 and PKL
N,N'-(ethane-1,2-diyl)bis[4-(2,3-dichlorobenzoyl)-1-methyl-1H-pyrrole-2-carboxamide]
-
N-(3-carboxy-4-hydroxy)phenyl-2,5-dimethylpyrrole
-
a PKM2 inhibitor
N-(3-chloro-4-methylphenyl)-7-fluoro-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
N-(4-(3-(pyridin-3-ylmethyl)-2-thioxo-2,3-dihydrothiazol-4-yl)phenyl)quinoline-8-sulfonamide
-
N-(4-(4-hydroxy-3-((2-methoxypyridin-3-yl)methyl)-2-thioxothiazolidin-4-yl)phenyl)-2,3-dihydrobenzo[b][1,4]dioxine-6-sulfonamide
-
N-(4-(4-hydroxy-3-((4-methylpyridin-3-yl)methyl)-2-thioxothiazolidin-4-yl)phenyl)-2,3-dihydrobenzo[b][1,4]dioxine-6-sulfonamide
-
N-(4-(4-hydroxy-3-((6-(3-(methylsulfonyl)phenyl)pyridin-3-yl)methyl)-2-thioxo-thiazolidin-4-yl)phenyl)-2,3-dihydrobenzo[b][1,4]dioxine-6-sulfonamide
-
N-(4-(4-hydroxy-3-(2-(pyridin-3-yl)ethyl)-2-thioxothiazolidin-4-yl)phenyl)-2,3-dihydrobenzo[b][1,4]dioxine-6-sulfonamide
-
N-(4-(4-hydroxy-3-(imidazo[1,2-a]pyridin-6-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-2,3-dihydrobenzo[b][1,4]dioxine-6-sulfonamide
-
N-(4-(4-hydroxy-3-(pyrazin-2-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-2,3-dihydrobenzo[b][1,4]dioxine-6-sulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-1-phenylmethanesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-1H-pyrrolo[2,3-b]pyridine-3-sulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-2,3-dihydrobenzo[b][1,4]dioxine-6-sulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-2,4,6-trimethylbenzenesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-2-fluorobenzenesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-2-morpholinobenzenesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-2-nitrobenzenesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-2-oxo-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-2-oxo-2Hchromene-6-sulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-3'-nitro-[1,1'-biphenyl]-2-sulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-3-fluorobenzenesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-3-methoxybenzenesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-3-methylbenzenesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-3-oxo-3,4-dihydro-2H-benzo[b][1,4]oxazine-6-sulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-4-cyanobenzenesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-4-fluorobenzenesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-4-methoxybenzenesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-4-methylbenzenesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-4-nitrobenzenesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-5-chloro-2-methoxybenzenesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-N-methylquinoline-8-sulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-[1,1'-biphenyl]-2-sulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)methanesulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)naphthalene-1-sulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)naphthalene-2-sulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)quinolone-8-sulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)thiophene-2-sulfonamide
-
N-(4-(4-hydroxy-3-(pyridin-4-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-2,3-dihydrobenzo[b][1,4]dioxine-6-sulfonamide
-
N-(4-(4-hydroxy-3-(quinolin-3-ylmethyl)-2-thioxothiazolidin-4-yl)phenyl)-2,3-dihydrobenzo[b][1,4]dioxine-6-sulfonamide
-
N-(4-[4-hydroxy-3-[(pyridin-3-yl)methyl]-2-sulfanylidene-1,3-thiazolidin-4-yl]phenyl)-2-methylbenzene-1-sulfonamide
-
N-(4-[4-hydroxy-3-[(pyridin-3-yl)methyl]-2-sulfanylidene-1,3-thiazolidin-4-yl]phenyl)benzenesulfonamide
-
N-(cyclobutylmethyl)-N-[(2-fluoro-4-hydroxyphenyl)methyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
N-[4-[4-(2-methoxyphenyl)piperazine-1-carbonyl]phenyl]quinoline-8-sulfonamide
-
oxalate
-
-
phosphoenolpyruvate
-
at 5°C, concentrations greater than 10 mM are inhibiting
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 (20–30% inhibition of PKM2 activity in a dose-dependent manner)
-
PML protein
proteins known for cellular growth and proliferation such as A-Raf and PML protein are known to downregulate PKM2 activity by interacting with it
-
Pp60v-src
causes dissociation of PKM2 tetramer into inactive dimer
-
shikonin
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
Zn2+
inhibits the M-(muscle)-type isozyme of pyruvate kinase. Zn2+ inhibits pyruvate kinase uncompetitively with respect to the substrate phosphoenolpyruvate (PEP), and competitively with respect to ADP. Zn2+ as a ZnADP complex acts as competitive and uncompetitive inhibitors of the enzyme with respect to the substrate ADP and PEP, respectively. Zn2+ forms a ZnADP complex, which may bind to the ADP-binding site of the free enzyme with the Ki value of 1.4 microM causing competitive inhibition, or to the ADP-site of the enzyme-PEP complex with 2.6 microM resulting in uncompetitive inhibition
[(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
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
fructose-1,6-bisphosphate
hLPYK is allosterically activated by fructose-1,6-bisphosphate (Fru-1,6-BP). The allosteric site, as defined by previous structural studies, is located in domain C between the phosphate-binding loop (residues 444-449) and the allosteric loop (residues 527-533). The 6'-phosphate of Fru-1,6-BP contributes to binding by interacting with the phosphate-binding loop (residues 444-449 between beta1 of sheet D and alpha22)
(1S,2S)-3-(2-hydroxy-4-methoxyphenyl)-1-(4-methoxyphenyl)propane-1,2-diol
-
AC50 value of 0.15 mM
(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
-
-
(2R,3S)-2-phenyl-3,4-dihydro-2H-chromen-3-ol
-
AC50 value of 0.221 mM
(2R,3S)-5,7-diphenoxy-2-(3,4,5-triphenoxyphenyl)-3,4-dihydro-2H-1-benzopyran-3-ol
-
AC50 value of 0.028 mM
(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
-
-
(3S)-7-phenoxy-2-(4-phenoxyphenyl)-3,4-dihydro-2H-1-benzopyran-3-ol
-
AC50 value of 0.115 mM
(3S,4S)-2-(3,4-diphenoxyphenyl)-5,7-diphenoxy-3,4-dihydro-2H-1-benzopyran-3,4-diol
-
AC50 value of 0.048 mM
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-(2-hydroxy-4-phenoxyphenyl)-1-(4-phenoxyphenyl)propane-1,2-diol
-
AC50 value of 0.2 mM
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-[(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
-
-
5-methoxy-2-[(2E)-3-(4-methoxyphenyl)prop-2-en-1-yl]phenol
-
AC50 value of 0.027 mM
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-{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
-
-
D-fructose 1,6-bisphosphate
D-fructose 1,6-diphosphate
D-fructose-1,6-bisphosphate
-
isozyme PKM2 requires D-fructose-1,6-bisphosphate to form the active tetramer, but isozyme PKM1 does not
fructose 1,6-bisphosphate
L-asparagine
-
L-serine
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
phosphorylated hexoses
-
activation
-
succinyl-5-aminoimidazole-4-carboxamide-1-ribose 5'-phosphate
SAICAR, an endogenous metabolite that correlates with an increased level of cell proliferation, it activates pyruvate kinase isoform M2 (PKM2) in its dimeric form, connection between SAICAR binding and the oligomeric state of PKM2, SAICAR stimulates the PKM2 dimer without inducing formation of a PKM2 tetramer. SAICAR binds to PKM2 mutant G415R better than it binds to wild-type PKM2
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.112 - 0.804
phosphoenolpyruvate
0.24 - 14.1
ADP
0.0003 - 2.1
phosphoenolpyruvate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.57 - 1182
phosphoenolpyruvate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.475
phosphoenolpyruvate
mutant PKM2G415R, pH 7.6, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005 - 0.0028
ADP-Cr2+
0.067 - 1.78
L-Phe
0.0048 - 0.077
oxalate
0.0014 - 0.0026
Zn2+
additional information
additional information
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01566
(1,4-dimethoxynaphthalen-2-yl)methyl dipropylcarbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00258
(1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl diethylcarbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00423
(1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl morpholine-4-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00174
(1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl piperidine-1-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.0014
(1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl [4-(piperazin-1-yl)phenyl]carbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00278
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) bis(diethylcarbamodithioate)
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.01
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) bis(dimethylcarbamodithioate)
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.01
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) bis(diprop-2-en-1-ylcarbamodithioate)
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.00308
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) bis(dipropylcarbamodithioate)
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.00096
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) di(1,3-thiazolidine-3-carbodithioate)
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.00264
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) dimorpholine-4-carbodithioate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.00233
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) dipyrrolidine-1-carbodithioate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.00105
(1,4-dioxo-1,4-dihydronaphthalene-2,3-diyl)bis(methylene) dithiomorpholine-4-carbodithioate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.163
(2E)-1-(4-methoxyphenyl)-3-(2,4,6-trimethoxyphenyl)prop-2-en-1-one
Homo sapiens
-
at pH 8.0 and 22°C
0.058
(2R,3S)-2-(3,4-diphenoxyphenyl)-3,5,7-triphenoxy-3,4-dihydro-2H-1-benzopyran
Homo sapiens
-
at pH 8.0 and 22°C
0.02
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl (4-methylpiperidin-1-yl)carbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00528
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl 1,3-thiazolidine-3-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.0117
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl 3,5-dimethylmorpholine-4-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.02
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl 4-(propan-2-yl)piperazine-1-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.02
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl 4-acetylpiperazine-1-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.01424
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl 4-methylpiperazine-1-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00221
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl benzylcarbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.02
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl bis(2-hydroxyethyl)carbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00508
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl cyclohexyl(methyl)carbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00457
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl dibutylcarbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00878
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl diethylcarbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.01411
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl diprop-2-en-1-ylcarbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00679
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl dipropylcarbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.02
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl methylcarbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.01524
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl morpholine-4-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.02
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl piperidin-1-ylcarbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00295
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl piperidine-1-carbodithioate
0.01973
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl pyrrolidine-1-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00589
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl thiomorpholine-4-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.02
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl [(pyridin-2-yl)methyl]carbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.02
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl [(pyridin-3-yl)methyl]carbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.02
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl [(pyridin-4-yl)methyl]carbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.02
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl [2-(diethylamino)ethyl]carbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.145
3,5-diphenoxy-2-[(2E)-3-(3,4,5-triphenoxyphenyl)prop-2-en-1-yl]phenol
Homo sapiens
-
at pH 8.0 and 22°C
0.295
3-(2-hydroxy-4-methoxyphenyl)-1-(4-methoxyphenyl)propane-1,2-diol
Homo sapiens
-
at pH 8.0 and 22°C
0.02
3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl 4-acetylpiperazine-1-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00998
3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl dipropylcarbamodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.0085
3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl morpholine-4-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.00493
3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl piperidine-1-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.028 - 0.191
4-amino-2-methylnaphthalen-1-ol
0.045
5,7-diphenoxy-2-(3,4,5-triphenoxyphenyl)-2H-1-benzopyran
Homo sapiens
-
at pH 8.0 and 22°C
0.01
5-(2,5-dimethyl-1H-pyrrol-1-yl)-2-hydroxybenzoic acid
Homo sapiens
-
in 50 mM Tris, pH 7.5, at 22°C
0.15 - 3.407
menadione
0.0593 - 0.0775
N-(3-carboxy-4-hydroxy)phenyl-2,5-dimethylpyrrole
0.00882
shikonin
0.02
[(5Z)-5-(4-[[(2-iodophenyl)carbonyl]oxy]benzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
-
in 50 mM Tris, pH 7.5, at 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
-
in the absence of K+
250
-
in the presence of K+
330
-
pH 8.0, 30°C, erythrocyte enzyme
420
-
liver enzyme, pH 8.0, 30°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
mutants H391Y and K422R
7.3
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
assay at
25
-
assay at
30
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.85 - 6.69
-
multiple active forms
8
-
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
expression of M2-type pyruvate kinase isoenzyme
Manually annotated by BRENDA team
-
M2-type isoenzyme
Manually annotated by BRENDA team
-
activity in tumor tissue is higher than in normal tissue
Manually annotated by BRENDA team
vultured skin fibroblast
Manually annotated by BRENDA team
-
expression of M2-type pyruvate kinase isoenzyme
Manually annotated by BRENDA team
-
expression of M2-type pyruvate kinase isoenzyme
Manually annotated by BRENDA team
-
isoform pyruvate kinase M2
Manually annotated by BRENDA team
-
a lymphoblastoid cell line
Manually annotated by BRENDA team
-
benign non-ductal tissue in chronic pancreatitis and normal pancreas show variable expression of M2-PK
Manually annotated by BRENDA team
-
expression of M2-type pyruvate kinase isoenzyme
Manually annotated by BRENDA team
-
expression of M2-type pyruvate kinase isoenzyme
Manually annotated by BRENDA team
-
distal, expression of M2-type pyruvate kinase isoenzyme
Manually annotated by BRENDA team
-
expression of M2-type pyruvate kinase isoenzyme
Manually annotated by BRENDA team
-
squamous cell carcinoma of tongue
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
nuclear translocation of M2-PK by the somatostatin analogue TT232, H2O2 or UV light
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
human liver pyruvate kinase (hLPYK) catalyzes the conversion of phosphoenolpyruvate (PEP) to pyruvate through a phosphoryl transfer from PEP to ADP, generating pyruvate and ATP. In human liver, this penultimate step of glycolysis is allosterically regulated by fructose-1,6-bisphosphate (Fru-1,6-BP), an earlier intermediate of glycolysis
physiological function
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KPYR_HUMAN
574
0
61830
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
240000
gel filtration
62000
4 * 62000, SDS-PAGE
195000 - 205000
-
gel filtration
225500
-
sedimentation equilibrium method
57900
-
calculated from amino acid sequence
58000
60000
80000
-
M2-PK-SUMO-1 conjugate, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 62000, SDS-PAGE
dimer
homotetramer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
the phosphorylated N-terminus does not interact with the main body of the protein or does so with a very low binding energy
phosphoprotein
sumoylation
-
PIAS3 slightly enhances M2-PK sumoylation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme mutant S12D as S12D-L-PYK-Fru-1,6-bisphosphate-Mn-Na-citrate complex, vapor diffusion hanging drop method, PYK S12D at 4 mg/ml in 10 mM MES, pH 6.8, 5 mM MgCl2, 10 mM KCl, and 2 mM DTT, 52 mM Na-ATP, and 1.3 mM Na-Fru-1,6-BP, mixing with well solution in varied ratios of 2:2, 4:2, 2:4, and 4:4, the well solution contains 50 mM sodium citrate, pH 4.9, 26 mM MnCl2, and 3-5% PEG 6000, X-ray diffraction structure determination and analysis at 1.8-1.95 A resolution, molecular replacement and modeling
purified recombinant N-terminally His6-tagged mutant enzymes, hanging drop vapour diffusion method, mixing of 0.0015 ml of 2.0-6.0 mg/ml protein in 50 mM MES, pH 6.8, 100 mM KCl, 10% glycerol, and 2 mM DTT, with 0.0015 ml of reservoir solution containing 200 mM ammonium citrate dibasic, and 20% PEG 3350 for mutant D499N, or 325 mM ammonium citrate dibasic, and 16% PEG 3350 for mutant W527H, or 200 mM ammonium citrate, pH 6.0, and 24% PEG 3350 for mutant DELTA529/S531G, or 200 mM ammonium citrate, pH 5.6, and 16% PEG 3350 for mutant S531E, and equilibration against 1 ml of reservoir solution, at 25°C, X-ray diffraction structrue determination and analysis at 2.15-2.42 A resolution, molecular replacement using the A and C domains of chain A of the S12D variant of hLPYK (PDB ID 4ip7) as a rigid-body model, modeling
purified recombinant PHD3/PKM2 complex, hanging drop vapor diffusion method, mixing of 5 mg/ml protein in 20 mM MES, pH 6.0, 75 mM NaCl, and 1 mM DTT, in a 1:1 ration with reservoir solution, 18°C, two weeks, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement method and modeling
the X-ray structure of human hPKM2 complexed with Mg2+, K+, the inhibitor oxalate, and the allosteric activator D-fructose 1,6-bisphosphate determined to a resolution of 2.82 A. (His)6-tagged hPKM2 complex, hanging drop vapor diffusion
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C436A
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
C436D
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
C436H
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
C436M
site-directed mutagenesis, crystal structure analysis, the mutant of L-PYK is the only residue 436 mutation that strengthens PEP affinity, revealing that the methionine substitution results in the ordering of several N-terminal residues that have not been ordered in previous structures
C436N
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
C436S
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
C436T
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
D499N
site-directed mutagenesis, the structure of the D499N mutant does not provide structural evidence for the previously observed allosteric activation of the D499N variant. The increase in PEP affinity observed for the D499N mutant in the absence of Fru-1,6-BP is due to the disruption of allosteric coupling across the C-C interface, crystal structure determination and analysis
F24A
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
L16A
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
L20A
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
Q18A
site-directed mutagenesis, the mutant shows strengthened phosphoenolpyruvate affinity compared to the wild-type enzyme
R510Q
similar kinetics as wild type, but dramatically decreased stability toward heat, more susceptible to ATP inhibition
S12A
site-directed mutagenesis, the mutant shows strengthened phosphoenolpyruvate affinity compared to the wild-type enzyme
S12D
site-directed mutagenesis, the S12D mutation mimics the effect of phosphorylation on L-PYK function, crystal structure analysis, overview
S531E
site-directed mutagenesis, in the S531E variant glutamate binds in place of the 6'-phosphate of fructose-1,6-bisphosphate in the allosteric site, leading to partial allosteric activation, crystal structure determination and analysis
S531G
construction of mutant DELTA529/S531G, the mutant is not activated by Fru-1,6-BP, crystal structure determination and analysis
T22A
site-directed mutagenesis, the mutant shows strengthened phosphoenolpyruvate affinity compared to the wild-type enzyme
W527H
site-directed mutagenesis, the increase in PEP affinity observed for the W527H mutant in the absence of Fru-1,6-BP is due to the disruption of allosteric coupling across the C-C interface, crystal structure determination and analysis
A137T
-
increased instability, increased sensitivity to the allosteric inhibitor/product
A154T
-
the mutation is associated with pyruvate kinase deficiency
A394S/R479H
-
the mutation is associated with pyruvate kinase deficiency
Arg488X
-
the mutation is associated with pyruvate kinase deficiency
D331G
-
the mutation is associated with pyruvate kinase deficiency
D331G/R479H
-
the mutation is associated with pyruvate kinase deficiency
D331G/R486W
-
the mutation is associated with pyruvate kinase deficiency
D397V/R486W
-
the mutation is associated with pyruvate kinase deficiency
E117K
-
decreased activity
E407G
-
the mutation is associated with pyruvate kinase deficiency
G111R
-
the mutation is associated with pyruvate kinase deficiency
G165V
-
the mutation is associated with pyruvate kinase deficiency
G332S
-
mutation alters catalysis and/or protein stability
G358E
-
the mutation is associated with pyruvate kinase deficiency
G358R/E407K
-
the mutation is associated with pyruvate kinase deficiency
G364D
-
mutation alters catalysis and/or protein stability
G390N
-
mutation alters catalysis and/or protein stability
G415R
site-directed mutagenesis, the mutant binds fructose 1,6-bisphosphate, but is not activated by it, unlike the wild-type PKM2. But the mutant is activated by succinyl-5-aminoimidazole-4-carboxamide-1-ribose 5'-phosphate (SAICAR)
H391Y
H464A
-
site-directed mutagenesis of isozyme PKM2, the mutant shows no binding of and activation by serine
H476L
-
site-directed mutagenesis
I310N
-
the mutation is associated with pyruvate kinase deficiency
I90N
-
the mutation is associated with pyruvate kinase deficiency
K270M
-
inactive
K367M
site-directed mutagenesis, the mutant lacks pyruvate kinase activity
K422R
K433E
the point mutant of PKM2 lacks phosphotyrosine peptide -binding ability
L167M/D331G
-
the mutation is associated with pyruvate kinase deficiency
L272V
-
the mutation is associated with pyruvate kinase deficiency
L374P
-
the mutation is associated with pyruvate kinase deficiency
L73P
-
the mutation is associated with pyruvate kinase deficiency
R163L
-
the mutation is associated with pyruvate kinase deficiency
R40W
-
the mutation is associated with pyruvate kinase deficiency
R479H
R479H/R486W
-
the mutation is associated with pyruvate kinase deficiency
R486W
-
the mutation is associated with pyruvate kinase deficiency
R504L
-
extreme instability
R510Q
-
increased instability, increased sensitivity to the allosteric inhibitor/product
R532W
-
loss of allosteric response to the normal activator
S12D
-
the introduction of S12D mutation mimics the effects of phosphorylation
S12E
-
the introduction of S12E mutation mimics the effects of phosphorylation
S437Y
-
site-directed mutagenesis of isozyme PKM2, the mutant shows no binding of and activation by fructose 1,6-bisphosphate
T384M
-
mutation alters catalysis and/or protein stability
V320L
-
the mutation is associated with pyruvate kinase deficiency
V320M/G406R
-
the mutation is associated with pyruvate kinase deficiency
Y235A
site-directed mutagenesis
Y235F
site-directed mutagenesis
Y235S
site-directed mutagenesis
Y593F
-
the mutant cannot be phosphorylated
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
the wild type enzyme shows 56% loss of activity after 3 h at 37°C, the mutant enzyme K422R shows 80% loss of activity after 3 h at 37°C, the mutant enzyme H391Y shows 1% loss of activity after 3 h at 37°C
4
the wild type enzyme and mutant enzyme K422R shows complete loss of activity after 15 min at 4°C, the mutant enzyme H391Y shows 36% loss of activity after 15 min at 4°C
60
the wild type enzyme and mutant enzyme K422R show complete loss of activity after 10 min at 60°C, while mutant enzyme H391Y displays only 2% loss of activity after 10 min at 60°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, enzyme precipitate in ammonium sulfate solution, several years
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography and gel filtration
ammonium sulfate precipitation, DEAE-cellulose column chromatography and Superdex S-200 gel filtration
-
DEAE column chromatography and carboxymethyl-Sepharose column chromatography
-
native enzyme from cytosol by ammonium sulfate fractionation and prothymosin alpha affinity and ion exchange chromatography, and chromatography on a phosphocellulose resin
-
Ni-agarose bead chromatography
-
Ni-NTA column chromatography and DEAE-Sepharose column chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Rosetta by nickel affinity chromatography, dialysis, and gel filtration
recombinant His-tagged PKM2 from Escherichia coli strain BL21 by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLys by nickel affinity chromatography, the His6-tag is cleaved off by PreScission protease followed by a second step of nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant His6-tagged isozymes from Escherichia coli by nickel affinity chromatgraphy
-
recombinant wild-type and mutant H476L from the FF50 strain of Escherichia coli by ammonium sulfate fractionation and anion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pyk, recombinant expression of wild-type and mutant codon-optimized genes as N-terminally His6-tagged enzymes in Escherichia coli strain BL21 Star (DE3)
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli FF50 cells
-
expressed in hematopoietic stem cells from pklr deficient mice, using a retroviral vector system
-
expressed in mouse erythroleukemia cells
-
expression in COS-7 cells
-
expression in Friend erythroleukemic cell line SLC-3
-
expression of His6-tagged isozymes in Escherichia coli
-
expression of wild-type and mutant H476L in the FF50 strain of Escherichia coli
-
gene PKM2, PKM2 overexpression in Hep-G2 cells, real-time RT-PCR enzyme expression analysis, recombinant overexpression of wild-type PKM2 and PKM2 K367M mutant in PKM2-knockdown HeLa S3 cells
gene PKM2, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLys
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Rosetta
recombinant expression of His-tagged PKM2 in Escherichia coli strain BL21
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in children, pyruvate kinase (PK) activity increases significantly in dental plaque corresponding with the caries progression. Streptococcus mutans (MS) and its biotype I are the strains most frequently found in dental plaque of young children. The correlation between the level of Streptococcus mutans in dental plaque and PK activity is both statistically significant and positive
complete absence of M2-pyruvate kinase expression in benign pancreatic ductal epithelium and pancreaticobiliary and duodenal neoplasia
-
HIF-1alpha induces an increased transcription of the pyruvate kinase M gene.. Induction of M2-PK expression by hypermethylated secreted frizzled related protein and mutated adenomatous polyposis coli protein, APC, overview
-
in tongue squamous cell carcinoma cell lines, PKM2 expression is reduced in response to miR-133a and miR-133b precursors transfection
-
oxaliplatin exposure in both HT-29 and HTOXAR-3 cells leads to PK-M2 mRNA up-regulation
-
patients with colorectal adenocarcinoma have the highest median faecal tumour M2-PK level
-
PK-M2 is down-regulates in HTOXAR-3 cells, there is a negative correlation between oxaliplatin resistance and PK-M2 mRNA levels
-
PKM2 is overexpressed in tongue squamous cell carcinoma cells and is associated with the downregulation of miR-133a and miR-133b
-
pyruvate kinase activities are increased by 52.4% in nerve growth factor treatment compared to the cells cultured by horse serum media
-
two patients with transfusion-dependent anemia reveal red blood cell pyruvate kinase to be 33% and 41% of the mean normal value
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
in hemolysate exposed to t-butyl hydroperoxide, pyruvate kinase activity decreases along with depletion of gluathione. 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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
mutation R510Q causes nonspherocytic hemolytic anemia
diagnostics
drug development
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Staal, G.E.J.; Koster, J.F.; Veeger, C.
Human erythrocyte pyruvate kinase
Methods Enzymol.
42C
182-186
1975
Homo sapiens
-
Manually annotated by BRENDA team
Kahn, A.; Marie, J.
Pyruvate kinases from human erythrocytes and liver
Methods Enzymol.
90
131-140
1982
Homo sapiens
-
Manually annotated by BRENDA team
Wang, C.; Chiarelli, L.R.; Bianchi, P.; Abraham, D.J.; Galizzi, A.; Mattevi, A.; Zanella, A.; Valentini, G.
Human erythrocyte pyruvate kinase: characterization of the recombinant enzyme and a mutant form (R510Q) causing nonspherocytic hemolytic anemia
Blood
98
3113-3120
2001
Homo sapiens (P30613), Homo sapiens
Manually annotated by BRENDA team
Yilmaz, S.; Ozan, S.; Ozercan, I.H.
Comparison of pyruvate kinase variants from breast tumor and normal breast
Arch. Med. Res.
34
315-324
2003
Homo sapiens
Manually annotated by BRENDA team
Dombrauckas, J.D.; Santarsiero, B.D.; Mesecar, A.D.
Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis
Biochemistry
44
9417-9429
2005
Homo sapiens (P14618), Homo sapiens
Manually annotated by BRENDA team
Stetak, A.; Veress, R.; Ovadi, J.; Csermely, P.; Keri, G.; Ullrich, A.
Nuclear translocation of the tumor marker pyruvate kinase M2 induces programmed cell death
Cancer Res.
67
1602-1608
2007
Homo sapiens
Manually annotated by BRENDA team
Kumar, Y.; Tapuria, N.; Kirmani, N.; Davidson, B.R.
Tumour M2-pyruvate kinase: a gastrointestinal cancer marker
Eur. J. Gastroenterol. Hepatol.
19
265-276
2007
Homo sapiens
Manually annotated by BRENDA team
Meza, N.W.; Quintana-Bustamante, O.; Puyet, A.; Rio, P.; Navarro, S.; Diez, A.; Bueren, J.A.; Bautista, J.M.; Segovia, J.C.
In vitro and in vivo expression of human erythrocyte pyruvate kinase in erythroid cells: a gene therapy approach
Hum. Gene Ther.
18
502-514
2007
Homo sapiens
Manually annotated by BRENDA team
Pendergrass, D.C.; Williams, R.; Blair, J.B.; Fenton, A.W.
Mining for allosteric information: natural mutations and positional sequence conservation in pyruvate kinase
IUBMB Life
58
31-38
2006
Homo sapiens
Manually annotated by BRENDA team
Oria-Hernandez, J.; Cabrera, N.; Perez-Montfort, R.; Ramirez-Silva, L.
Pyruvate kinase revisited: the activating effect of K+
J. Biol. Chem.
280
37924-37929
2005
Homo sapiens
Manually annotated by BRENDA team
Narli, N.; Satar, M.; Kayrin, L.; Yapicioglu, H.; Oezlue, F.; Budgayci, R.
The activity and kinetics of pyruvate kinase in hypoxic newborns
Pediatr. Hematol. Oncol.
22
567-573
2005
Homo sapiens
Manually annotated by BRENDA team
Iori, E.; Millioni, R.; Puricelli, L.; Arrigoni, G.; Lenzini, L.; Trevisan, R.; James, P.; Rossi, G.P.; Pinna, L.A.; Tessari, P.
Glycolytic enzyme expression and pyruvate kinase activity in cultured fibroblasts from type 1 diabetic patients with and without nephropathy
Biochim. Biophys. Acta
1782
627-633
2008
Homo sapiens (P14618), Homo sapiens
Manually annotated by BRENDA team
Ogasawara, Y.; Funakoshi, M.; Ishii, K.
Pyruvate kinase is protected by glutathione-dependent redox balance in human red blood cells exposed to reactive oxygen species
Biol. Pharm. Bull.
31
1875-1881
2008
Homo sapiens
Manually annotated by BRENDA team
Haug, U.; Hundt, S.; Brenner, H.
Sensitivity and specificity of faecal tumour M2 pyruvate kinase for detection of colorectal adenomas in a large screening study
Br. J. Cancer
99
133-135
2008
Homo sapiens
Manually annotated by BRENDA team
Aisaki, K.; Aizawa, S.; Fujii, H.; Kanno, J.; Kanno, H.
Glycolytic inhibition by mutation of pyruvate kinase gene increases oxidative stress and causes apoptosis of a pyruvate kinase deficient cell line
Exp. Hematol.
35
1190-1200
2007
Homo sapiens
Manually annotated by BRENDA team
Dharmarajan, L.; Case, C.L.; Dunten, P.; Mukhopadhyay, B.
Tyr235 of human cytosolic phosphoenolpyruvate carboxykinase influences catalysis through an anion-quadrupole interaction with phosphoenolpyruvate carboxylate
FEBS J.
275
5810-5819
2008
Homo sapiens (P14618)
Manually annotated by BRENDA team
Wu, X.; Zhou, Y.; Zhang, K.; Liu, Q.; Guo, D.
Isoform-specific interaction of pyruvate kinase with hepatitis C virus NS5B
FEBS Lett.
582
2155-2160
2008
Homo sapiens (P14618)
Manually annotated by BRENDA team
Shimada, N.; Shinagawa, T.; Ishii, S.
Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein
Genes Cells
13
245-254
2008
Homo sapiens
Manually annotated by BRENDA team
Siwko, S.; Mochly-Rosen, D.
Use of a novel method to find substrates of protein kinase C delta identifies M2 pyruvate kinase
Int. J. Biochem. Cell Biol.
39
978-987
2007
Homo sapiens
Manually annotated by BRENDA team
Spoden, G.A.; Mazurek, S.; Morandell, D.; Bacher, N.; Ausserlechner, M.J.; Jansen-Duerr, P.; Eigenbrodt, E.; Zwerschke, W.
Isotype-specific inhibitors of the glycolytic key regulator pyruvate kinase subtype M2 moderately decelerate tumor cell proliferation
Int. J. Cancer
123
312-321
2008
Homo sapiens
Manually annotated by BRENDA team
Fenton, A.W.; Hutchinson, M.
The pH dependence of the allosteric response of human liver pyruvate kinase to fructose-1,6-bisphosphate, ATP, and alanine
Arch. Biochem. Biophys.
484
16-23
2009
Homo sapiens
Manually annotated by BRENDA team
Vander Heiden, M.G.; Christofk, H.R.; Schuman, E.; Subtelny, A.O.; Sharfi, H.; Harlow, E.E.; Xian, J.; Cantley, L.C.
Identification of small molecule inhibitors of pyruvate kinase M2
Biochem. Pharmacol.
79
1118-1124
2010
Homo sapiens
Manually annotated by BRENDA team
Fenton, A.W.; Tang, Q.
An activating interaction between the unphosphorylated N-terminus of human liver pyruvate kinase and the main body of the protein is interrupted by phosphorylation
Biochemistry
48
3816-3818
2009
Homo sapiens
Manually annotated by BRENDA team
Yavarian, M.; Karimi, M.; Shahriary, M.; Afrasiabi, A.
Prevalence of pyruvate kinase deficiency among the south Iranian population: Quantitative assay and molecular analysis
Blood Cells Mol. Dis.
40
308-311
2008
Homo sapiens
Manually annotated by BRENDA team
Aloysius, M.M.; Zaitoun, A.M.; Bates, T.E.; Albasri, A.; Ilyas, M.; Rowlands, B.J.; Lobo, D.N.
Complete absence of M2-pyruvate kinase expression in benign pancreatic ductal epithelium and pancreaticobiliary and duodenal neoplasia
BMC Cancer
9
327
2009
Homo sapiens
Manually annotated by BRENDA team
Finkenstedt, A.; Bianchi, P.; Theurl, I.; Vogel, W.; Witcher, D.R.; Wroblewski, V.J.; Murphy, A.T.; Zanella, A.; Zoller, H.
Regulation of iron metabolism through GDF15 and hepcidin in pyruvate kinase deficiency
Br. J. Haematol.
144
789-793
2009
Homo sapiens
Manually annotated by BRENDA team
Kedar, P.; Hamada, T.; Warang, P.; Nadkarni, A.; Shimizu, K.; Fujji, H.; Ghosh, K.; Kanno, H.; Colah, R.
Spectrum of novel mutations in the human PKLR gene in pyruvate kinase-deficient Indian patients with heterogeneous clinical phenotypes
Clin. Genet.
75
157-162
2009
Homo sapiens
Manually annotated by BRENDA team
Koss, K.; Maxton, D.; Jankowski, J.
Faecal dimeric M2 pyruvate kinase in colorectal cancer and polyps correlates with tumour staging and surgical intervention
Colorectal Dis.
10
244-248
2008
Homo sapiens
Manually annotated by BRENDA team
Johnson, M.W.; Maestranzi, S.; Duffy, A.M.; Dewar, D.H.; Ciclitira, P.J.; Sherwood, R.A.; Nicholls, J.R.
Faecal M2-pyruvate kinase: a novel, noninvasive marker of ileal pouch inflammation
Eur. J. Gastroenterol. Hepatol.
21
544-550
2009
Homo sapiens
Manually annotated by BRENDA team
van Wijk, R.; Huizinga, E.G.; van Wesel, A.C.; van Oirschot, B.A.; Hadders, M.A.; van Solinge, W.W.
Fifteen novel mutations in PKLR associated with pyruvate kinase (PK) deficiency: structural implications of amino acid substitutions in PK
Hum. Mutat.
30
446-453
2009
Homo sapiens
Manually annotated by BRENDA team
Kim, J.Y.; Kim, D.Y.; Ro, J.Y.
Granule formation in NGF-cultured mast cells is associated with expressions of pyruvate kinase type M2 and annexin I proteins
Int. Arch. Allergy Immunol.
146
287-297
2008
Homo sapiens
Manually annotated by BRENDA team
Wong, T.S.; Liu, X.B.; Chung-Wai Ho, A.; Po-Wing Yuen, A.; Wai-Man Ng, R.; Ignace Wei, W.
Identification of pyruvate kinase type M2 as potential oncoprotein in squamous cell carcinoma of tongue through microRNA profiling
Int. J. Cancer
123
251-257
2008
Homo sapiens
Manually annotated by BRENDA team
Akhtar, K.; Gupta, V.; Koul, A.; Alam, N.; Bhat, R.; Bamezai, R.N.
Differential behavior of missense mutations in the intersubunit contact domain of the human pyruvate kinase M2 isozyme
J. Biol. Chem.
284
11971-11981
2009
Homo sapiens (P14618), Homo sapiens
Manually annotated by BRENDA team
Spoden, G.A.; Morandell, D.; Ehehalt, D.; Fiedler, M.; Jansen-Duerr, P.; Hermann, M.; Zwerschke, W.
The SUMO-E3 ligase PIAS3 targets pyruvate kinase M2
J. Cell. Biochem.
107
293-302
2009
Homo sapiens
Manually annotated by BRENDA team
Ervens, J.; Fuchs, H.; Niemann, V.T.; Hoffmeister, B.
Pyruvate kinase isoenzyme M2 is not of diagnostic relevance as a marker for oral cancer
J. Craniomaxillofac. Surg.
36
89-94
2008
Homo sapiens
Manually annotated by BRENDA team
Ayi, K.; Liles, W.C.; Gros, P.; Kain, K.C.
Adenosine triphosphate depletion of erythrocytes simulates the phenotype associated with pyruvate kinase deficiency and confers protection against Plasmodium falciparum in vitro
J. Infect. Dis.
200
1289-1299
2009
Homo sapiens
Manually annotated by BRENDA team
Boxer, M.B.; Jiang, J.K.; Vander Heiden, M.G.; Shen, M.; Skoumbourdis, A.P.; Southall, N.; Veith, H.; Leister, W.; Austin, C.P.; Park, H.W.; Inglese, J.; Cantley, L.C.; Auld, D.S.; Thomas, C.J.
Evaluation of substituted N,N-diarylsulfonamides as activators of the tumor cell specific M2 isoform of pyruvate kinase
J. Med. Chem.
53
1048-1055
2009
Homo sapiens
Manually annotated by BRENDA team
Martinez-Balibrea, E.; Plasencia, C.; Gines, A.; Martinez-Cardus, A.; Musulen, E.; Aguilera, R.; Manzano, J.L.; Neamati, N.; Abad, A.
A proteomic approach links decreased pyruvate kinase M2 expression to oxaliplatin resistance in patients with colorectal cancer and in human cell lines
Mol. Cancer Ther.
8
771-778
2009
Homo sapiens
Manually annotated by BRENDA team
Meza, N.W.; Alonso-Ferrero, M.E.; Navarro, S.; Quintana-Bustamante, O.; Valeri, A.; Garcia-Gomez, M.; Bueren, J.A.; Bautista, J.M.; Segovia, J.C.
Rescue of pyruvate kinase deficiency in mice by gene therapy using the human isoenzyme
Mol. Ther.
17
2000-2009
2009
Homo sapiens
Manually annotated by BRENDA team
Ayi, K.; Min-Oo, G.; Serghides, L.; Crockett, M.; Kirby-Allen, M.; Quirt, I.; Gros, P.; Kain, K.C.
Pyruvate kinase deficiency and malaria
N. Engl. J. Med.
358
1805-1810
2008
Homo sapiens
Manually annotated by BRENDA team
Christofk, H.R.; Vander Heiden, M.G.; Wu, N.; Asara, J.M.; Cantley, L.C.
Pyruvate kinase M2 is a phosphotyrosine-binding protein
Nature
452
181-186
2008
Homo sapiens (P14618), Homo sapiens
Manually annotated by BRENDA team
Christofk, H.R.; Vander Heiden, M.G.; Harris, M.H.; Ramanathan, A.; Gerszten, R.E.; Wei, R.; Fleming, M.D.; Schreiber, S.L.; Cantley, L.C.
The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth
Nature
452
230-233
2008
Homo sapiens
Manually annotated by BRENDA team
Titapiwatanakun, R.; Hoyer, J.D.; Crain, K.; Arndt, C.A.
Relative red blood cell enzyme levels as a clue to the diagnosis of pyruvate kinase deficiency
Pediatr. Blood Cancer
51
819-821
2008
Homo sapiens
Manually annotated by BRENDA team
Ferguson, E.C.; Rathmell, J.C.
New roles for pyruvate kinase M2: working out the Warburg effect
Trends Biochem. Sci.
33
359-362
2008
Homo sapiens
Manually annotated by BRENDA team
Alontaga, A.Y.; Fenton, A.W.
Effector analogues detect varied allosteric roles for conserved protein-effector interactions in pyruvate kinase isozymes
Biochemistry
50
1934-1939
2011
Homo sapiens
Manually annotated by BRENDA team
Holyoak, T.; Zhang, B.; Deng, J.; Tang, Q.; Prasannan, C.B.; Fenton, A.W.
Energetic coupling between an oxidizable cysteine and the phosphorylatable N-terminus of human liver pyruvate kinase
Biochemistry
52
466-476
2013
Homo sapiens (P30613), Homo sapiens
Manually annotated by BRENDA team
Diaz-Jullien, C.; Moreira, D.; Sarandeses, C.S.; Covelo, G.; Barbeito, P.; Freire, M.
The M2-type isoenzyme of pyruvate kinase phosphorylates prothymosin alpha in proliferating lymphocytes
Biochim. Biophys. Acta
1814
355-365
2011
Homo sapiens
Manually annotated by BRENDA team
Mazurek, S.
Pyruvate kinase M2: A key enzyme of the tumor metabolome and its medical relevance
Biomed. Res.
23
133-142
2012
Homo sapiens, Mus musculus
-
Manually annotated by BRENDA team
Walsh, M.J.; Brimacombe, K.R.; Veith, H.; Bougie, J.M.; Daniel, T.; Leister, W.; Cantley, L.C.; Israelsen, W.J.; Vander Heiden, M.G.; Shen, M.; Auld, D.S.; Thomas, C.J.; Boxer, M.B.
2-Oxo-N-aryl-1,2,3,4-tetrahydroquinoline-6-sulfonamides as activators of the tumor cell specific M2 isoform of pyruvate kinase
Bioorg. Med. Chem. Lett.
21
6322-6327
2011
Homo sapiens
Manually annotated by BRENDA team
Yacovan, A.; Ozeri, R.; Kehat, T.; Mirilashvili, S.; Sherman, D.; Aizikovich, A.; Shitrit, A.; Ben-Zeev, E.; Schutz, N.; Bohana-Kashtan, O.; Konson, A.; Behar, V.; Becker, O.M.
1-(sulfonyl)-5-(arylsulfonyl)indoline as activators of the tumor cell specific M2 isoform of pyruvate kinase
Bioorg. Med. Chem. Lett.
22
6460-6468
2012
Homo sapiens
Manually annotated by BRENDA team
Chen, J.; Jiang, Z.; Wang, B.; Wang, Y.; Hu, X.
Vitamin K3 and K5 are inhibitors of tumor pyruvate kinase M2
Cancer Lett.
316
204-210
2012
Homo sapiens
Manually annotated by BRENDA team
Chaneton, B.; Hillmann, P.; Zheng, L.; Martin, A.C.; Maddocks, O.D.; Chokkathukalam, A.; Coyle, J.E.; Jankevics, A.; Holding, F.P.; Vousden, K.H.; Frezza, C.; OReilly, M.; Gottlieb, E.
Serine is a natural ligand and allosteric activator of pyruvate kinase M2
Nature
491
458-462
2012
Homo sapiens
Manually annotated by BRENDA team
Ye, J.; Mancuso, A.; Tong, X.; Ward, P.S.; Fan, J.; Rabinowitz, J.D.; Thompson, C.B.
Pyruvate kinase M2 promotes de novo serine synthesis to sustain mTORC1 activity and cell proliferation
Proc. Natl. Acad. Sci. USA
109
6904-6909
2012
Homo sapiens
Manually annotated by BRENDA team
Gupta, V.; Bamezai, R.N.
Human pyruvate kinase M2: a multifunctional protein
Protein Sci.
19
2031-2044
2010
Homo sapiens (P14618), Homo sapiens
Manually annotated by BRENDA team
van Oirschot, B.A.; Francois, J.J.; van Solinge, W.W.; van Wesel, A.C.; Rijksen, G.; van Amstel, H.K.; van Wijk, R.
Novel type of red blood cell pyruvate kinase hyperactivity predicts a remote regulatory locus involved in PKLR gene expression
Am. J. Hematol.
89
380-384
2014
Homo sapiens
Manually annotated by BRENDA team
Adem, S.; Aslan, A.; Ahmed, I.; Krohn, K.; Guler, C.; Comakl?, V.; Demirdag, R.; Kuzu, M.
Inhibitory and Activating Effects of Some Flavonoid Derivatives on Human Pyruvate Kinase Isoenzyme M2
Arch. Pharm.
349
132-136
2016
Homo sapiens
Manually annotated by BRENDA team
Gao, X.; Wang, H.; Yang, J.J.; Chen, J.; Jie, J.; Li, L.; Zhang, Y.; Liu, Z.R.
Reciprocal regulation of protein kinase and pyruvate kinase activities of pyruvate kinase M2 by growth signals
J. Biol. Chem.
288
15971-15979
2013
Homo sapiens
Manually annotated by BRENDA team
He, C.L.; Bian, Y.Y.; Xue, Y.; Liu, Z.X.; Zhou, K.Q.; Yao, C.F.; Lin, Y.; Zou, H.F.; Luo, F.X.; Qu, Y.Y.; Zhao, J.Y.; Ye, M.L.; Zhao, S.M.; Xu, W.
Pyruvate kinase M2 activates mTORC1 by phosphorylating AKT1S1
Sci. Rep.
6
21524
2016
Homo sapiens
Manually annotated by BRENDA team
Chen, Y.L.; Song, J.J.; Chen, X.C.; Xu, W.; Zhi, Q.; Liu, Y.P.; Xu, H.Z.; Pan, J.S.; Ren, J.L.; Guleng, B.
Mechanisms of pyruvate kinase M2 isoform inhibits cell motility in hepatocellular carcinoma cells
World J. Gastroenterol.
21
9093-9102
2015
Homo sapiens
Manually annotated by BRENDA team
McFarlane, J.S.; Ronnebaum, T.A.; Meneely, K.M.; Chilton, A.; Fenton, A.W.; Lamb, A.L.
Changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation-Pi bond
Acta Crystallogr. Sect. F
75
461-469
2019
Homo sapiens (P30613), Homo sapiens
Manually annotated by BRENDA team
Yan, M.; Chakravarthy, S.; Tokuda, J.M.; Pollack, L.; Bowman, G.D.; Lee, Y.S.
Succinyl-5-aminoimidazole-4-carboxamide-1-ribose 5-phosphate (SAICAR) activates pyruvate kinase isoform M2 (PKM2) in its dimeric form
Biochemistry
55
4731-4736
2016
Homo sapiens (P14618), Homo sapiens
Manually annotated by BRENDA team
Murakami, K.; Yoshino, M.
Zinc inhibition of pyruvate kinase of M-type isozyme
Biometals
30
335-340
2017
Homo sapiens (P14618)
Manually annotated by BRENDA team
Ning, X.; Qi, H.; Li, R.; Li, Y.; Jin, Y.; McNutt, M.A.; Liu, J.; Yin, Y.
Discovery of novel naphthoquinone derivatives as inhibitors of the tumor cell specific M2 isoform of pyruvate kinase
Eur. J. Med. Chem.
138
343-352
2017
Homo sapiens (P14618)
Manually annotated by BRENDA team
Li, R.; Ning, X.; Zhou, S.; Lin, Z.; Wu, X.; Chen, H.; Bai, X.; Wang, X.; Ge, Z.; Li, R.; Yin, Y.
Discovery and structure-activity relationship of novel 4-hydroxy-thiazolidine-2-thione derivatives as tumor cell specific pyruvate kinase M2 activators
Eur. J. Med. Chem.
143
48-65
2018
Homo sapiens (P14618), Homo sapiens
Manually annotated by BRENDA team
Gehrig, S.; Macpherson, J.A.; Driscoll, P.C.; Symon, A.; Martin, S.R.; MacRae, J.I.; Kleinjung, J.; Fraternali, F.; Anastasiou, D.
An engineered photoswitchable mammalian pyruvate kinase
FEBS J.
284
2955-2980
2017
Homo sapiens (P14618), Mus musculus (P52480)
Manually annotated by BRENDA team
Krzysciak, W.; Papie?, M.; Jurczak, A.; Koscielniak, D.; Vyhouskaya, P.; Zagorska-Swiezy, K.; Skalniak, A.
Relationship between pyruvate kinase activity and cariogenic biofilm formation in Streptococcus mutans biotypes in caries patients
Front. Microbiol.
8
856
2017
Homo sapiens (P30613), Homo sapiens
Manually annotated by BRENDA team
Nandi, S.; Dey, M.
Biochemical and structural insights into how amino acids regulate pyruvate kinase muscle isoform 2
J. Biol. Chem.
295
5390-5403
2020
Homo sapiens (A0A024R5Z9), Homo sapiens
Manually annotated by BRENDA team
Ning, X.; Qi, H.; Li, R.; Jin, Y.; McNutt, M.A.; Yin, Y.
Synthesis and antitumor activity of novel 2,3-didithiocarbamate substituted naphthoquinones as inhibitors of pyruvate kinase M2 isoform
J. Enzyme Inhib. Med. Chem.
33
126-129
2018
Homo sapiens (P14618)
Manually annotated by BRENDA team
Kumar, S.; Patel, A.K.
Purification and characterization of prolyl hydroxylase 3/pyruvate kinase isoform 2 protein complex
Mol. Biotechnol.
62
111-118
2020
Homo sapiens (P14618)
Manually annotated by BRENDA team
Matsuda, S.; Adachi, J.; Ihara, M.; Tanuma, N.; Shima, H.; Kakizuka, A.; Ikura, M.; Ikura, T.; Matsuda, T.
Nuclear pyruvate kinase M2 complex serves as a transcriptional coactivator of arylhydrocarbon receptor
Nucleic Acids Res.
44
636-647
2016
Homo sapiens (P14618)
Manually annotated by BRENDA team
Verma, K.; Patel, A.
Pyruvate kinase M2 serves as blockade for nucleosome repositioning and abrogates Chd7 remodeling activity
PLoS ONE
14
e0211515
2019
Homo sapiens (P14618)
Manually annotated by BRENDA team