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ADP + phosphoenolpyruvate
ATP + pyruvate
ATP + AKT1S1
ADP + phospho-AKT1S1
-
the enzyme phosphorylates Ser202 and Ser203 of AKT1S1
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
ATP + pyruvate
ADP + phosphoenolpyruvate
CDP + phosphoenolpyruvate
CTP + pyruvate
dADP + phosphoenolpyruvate
dATP + pyruvate
dCDP + phosphoenolpyruvate
dCTP + pyruvate
dGDP + phosphoenolpyruvate
dGTP + pyruvate
dTDP + phosphoenolpyruvate
dTTP + pyruvate
epsilon-ADP + phosphoenolpyruvate
?
-
poor substrate
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
IDP + phosphoenolpyruvate
ITP + pyruvate
TDP + phosphoenolpyruvate
TTP + pyruvate
UDP + phosphoenolpyruvate
UTP + pyruvate
additional information
?
-
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
Amaranthus sp.
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
Antarctic fish
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
100% activity with ADP
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
4 phosphoenolpyruvate-binding sites/enzyme molecule
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
physiological role
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
poor substrates: UDP, GDP
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
physiological role
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
Busycotypus canaliculatum
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
final regulatory point in catabolic Embden-Meyerhoff-Parnas pathway
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
probably involved in supplying additional carbon-skeletons for ammonium assimilation
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
physiological role
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
-
catalyzes the addition of a proton and the loss of a phosphoryl group which is transferred to ADP
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
no positive cooperativity for ADP
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
641553, 673438, 674082, 674499, 676298, 707450, 707493, 707838, 707871, 707908, 708196, 708214, 708378, 708661, 708734, 708759, 709228, 709286, 709379, 709464, 709909, 710022, 710034, 710048, 710210, 710648 -
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
key enzyme in glycolysis
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
as a function of increasing pH (pH 6.5-8.0), PYK's affinity for phosphoenolpyruvate decreases, while affinity for ATP slightly increases
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
involved in regulation of metabolism of an aerobic organism capable of net glucose synthesis
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
allosteric enzyme
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
physiological role
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
Musa cavendishii
-
ADP preferred substrate, UDP, IDP, GDP and CDP may also be used with lower effectivity
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
100% activity with ADP
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
rate-controlling enzyme of glycolytic flux
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
Pigeon
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
-
the enzyme is expressed during the intraerythrocytic-stage of its developlental cycle that may play important metabolic roles during infection
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
important role of pyruvate kinase during malarial infection
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
other nucleoside diphosphates can replace ADP with a different rank order of effectiveness for enzyme form I and II
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
641555, 641563, 641564, 641572, 661404, 661406, 674052, 675943, 706831, 707914, 708372, 709817, 710084 -
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
the enzyme catalyzes an important regulatory step in the glycolysis pathway, the main route that provides energy for brain function
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
r
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
physiological role
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
r
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
r
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
allosteric enzyme
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
physiological role
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
the enzyme is essential for multicellular development: fruiting body formation is abolished in mutant strain and indole-induced spore formation is delayed
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
ADP preferred substrate, UDP, IDP, GDP and CDP may also be used with lower effectivity
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
the substrate binding order of the Thermofilum pendens enzyme is independent despite lacking an internal positive charge
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
ir
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
best nucleoside diphosphate substrate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
positive cooperativity for phosphoenolpyruvate
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
no allosteric activation
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
100% activity with ADP
-
-
?
ADP + phosphoenolpyruvate
ATP + pyruvate
-
-
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
-
-
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
-
isozyme M2-type acts as a ProTalpha kinase phosphorylating ProTalpha
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
-
in normal murine lymphocytes and in tumor cells M2-PK phosphorylates prothymosin alpha on a threonine
-
-
?
ATP + prothymosin alpha
ADP + phospho-prothymosin alpha
-
ProTalpha kinase activity
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
the enzyme catalyzes the final step of glycolysis
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
the enzyme catalyzes the final step of glycolysis
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
ir
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
r
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
ATP + pyruvate
ADP + phosphoenolpyruvate
-
-
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
reaction at 25% the rate of ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
poor substrate
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
reaction with PKp-isozyme at 30%, with PKc-isozyme at 12% the rate of ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
poor substrate
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
poor substrate
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
CDP + phosphoenolpyruvate
CTP + pyruvate
-
less effective than ADP
-
-
?
dADP + phosphoenolpyruvate
dATP + pyruvate
-
23% activity compared to ADP
-
-
?
dADP + phosphoenolpyruvate
dATP + pyruvate
9.9% activity compared to ADP
-
-
?
dADP + phosphoenolpyruvate
dATP + pyruvate
-
26% activity compared to ADP
-
-
?
dCDP + phosphoenolpyruvate
dCTP + pyruvate
-
0.5% activity compared to ADP
-
-
?
dCDP + phosphoenolpyruvate
dCTP + pyruvate
0.082% activity compared to ADP
-
-
?
dCDP + phosphoenolpyruvate
dCTP + pyruvate
-
2.9% activity compared to ADP
-
-
?
dGDP + phosphoenolpyruvate
dGTP + pyruvate
-
10.2% activity compared to ADP
-
-
?
dGDP + phosphoenolpyruvate
dGTP + pyruvate
1.82% activity compared to ADP
-
-
?
dGDP + phosphoenolpyruvate
dGTP + pyruvate
-
44% activity compared to ADP
-
-
?
dTDP + phosphoenolpyruvate
dTTP + pyruvate
-
4.6% activity compared to ADP
-
-
?
dTDP + phosphoenolpyruvate
dTTP + pyruvate
0.035% activity compared to ADP
-
-
?
dTDP + phosphoenolpyruvate
dTTP + pyruvate
-
4.8% activity compared to ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
reaction at 55% the rate of ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
reaction for PKc-isozyme at 71%, for PKp-isozyme at 39% the rate of ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
preference for GDP
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
-
-
-
?
GDP + phosphoenolpyruvate
GTP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
reaction at 53% the rate of ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
-
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
-
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
reaction with PKp-isozyme at 20%, with PKc-isozyme at 89% the rate of ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
-
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
-
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
-
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
less effective than ADP
-
-
?
IDP + phosphoenolpyruvate
ITP + pyruvate
-
-
-
-
?
TDP + phosphoenolpyruvate
TTP + pyruvate
-
-
95% yield
-
?
TDP + phosphoenolpyruvate
TTP + pyruvate
-
poor substrate
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
reaction at about 70% the rate of ADP, PKc-isozyme
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
reaction at about 31% the rate of ADP, PKp-isozyme
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
UDP + phosphoenolpyruvate
UTP + pyruvate
-
less effective than ADP
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
enzyme is confirmed by total proteome analysis of glycerol-grown cells
-
-
?
additional information
?
-
Antarctic fish
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
broad specificity for nucleoside diphosphates
-
-
?
additional information
?
-
-
allosteric enzyme: homotropic
-
-
?
additional information
?
-
-
allosteric enzyme: homotropic
-
-
?
additional information
?
-
-
allosteric enzyme: homotropic
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
pyruvate kinase M2 is a phosphotyrosine-binding protein
-
-
?
additional information
?
-
-
pyruvate kinase M2 is a phosphotyrosine-binding protein
-
-
?
additional information
?
-
-
the SUMO-E3 ligase protein PIAS3 (inhibitor of activated STAT3) physically interacts with M2-PK and its isoenzyme M1-PK
-
-
?
additional information
?
-
mitogenic factor LPA, SUMO-E3 ligase, tumor endothelial marker-8, hepatitis C virus-NS5B RNA polymerase and HERC-1 via its HECT domain bind to isozyme PKM2
-
-
?
additional information
?
-
-
mitogenic factor LPA, SUMO-E3 ligase, tumor endothelial marker-8, hepatitis C virus-NS5B RNA polymerase and HERC-1 via its HECT domain bind to isozyme PKM2
-
-
?
additional information
?
-
-
nuclear M2-PK participates in the phosphorylation of the epsilon-amino group of histone 1 by direct phosphate transfer from PEP without requiring ATP. M2-PK directly inters with different oncoproteins and components of the protein kinase cascade, such as HPV-16 E7, the tyrosine kinases pp60v-src, BCR-ABL, ETV6-NTRK3, FGFR-1, FLT3 and JAK-2, the serine/threonine kinase A-Raf, cytoplasmic promyelocytic leukemia tumor suppressor protein as well as phosphotyrosine peptides
-
-
?
additional information
?
-
direct physical binding through protein-protein interaction between PHD3 and PKM2 is observed. Homology three-dimensional model of PHD3/PKM2 complex
-
-
-
additional information
?
-
PKM2 during in vitro reconstitution potentially interacts with histone H3 of the 5'-FAM labelled nucleosome octamer core and forms a stable complex. PKM2 phosphorylates histone H3 at T11
-
-
-
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
allosteric enzyme: homotropic
-
-
?
additional information
?
-
-
allosteric enzyme: homotropic
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
the recombinant enzyme shows the following range in its substrate specificity: ADP>dADP>dGDP>dCDP>TDP
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
pyruvate kinase is a substrate of protein kinase A
-
-
?
additional information
?
-
-
pyruvate kinase is a substrate of protein kinase A
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
preferred: purine nucleotides
-
-
?
additional information
?
-
-
specificity overview
-
-
?
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Cd2+
-
multiphasical activation, at pH below physiological value, inhibits at physiological pH
Cs+
activates, at saturating concentrations of PEP3-, ADP-Mg complex and free Mg2+, the Km for Cs+ is 13.5 mM
Cu2+
-
divalent cation required, at 1 mM Cu2+ activation results in 86% of the activity with Mg2+
Fe2+
-
the enzyme is dependent on Mn2+ ion for its activity. Fe2+ and Mg2+ show 70 and 20% of the Mn2+ activity, respectively. No activity is detected without metal or with Zn2+, Cu2+, Co2+, and Ni2+
Li+
can substitute for K+ by 38%
Mg
-
required for activity
Ni2+
-
divalent cation required, at 1 mM Ni2+ activation results in 2% of the activity with Mg2+
Rb+
activates, at saturating concentrations of PEP3-, ADP-Mg complex and free Mg2+, the Km for Rb+ is 5.9 mM
sulfate
each monomer in the asymmetric unit of CpPyK binds two sulfate ions at equivalent positions, one in the C-domain and the other at the interface of the A and C domains, binding structure, overview. The sulfate ion in the C-domain occupies a position corresponding to the 6-phosphate of the effector molecule in different PyKs
Tl+
-
wild-type enzyme and the three mutant enzymes T298S, T298C and T298A show no measurable activity in the presence of K+ or Tl+. Tl+ can activate wild-type enzyme to 85% the activity in the presence of K+. With T298S, T298, and T298A, Tl+ is 1.2-1.8fold better activator than is K+ based on the measured turnover number values
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+
-
activation at low Mg2+ and low Ca2+-concentration
Ca2+
-
divalent cation required, at 1 mM Ca2+ activation results in 3% of the activity with Mg2+
Co2+
-
divalent cation required, at 1 mM Co2+ activation results in 170% of the activity with Mg2+
Co2+
-
multiphasical activation, at pH below physiological value, inhibits at physiological pH
Co2+
-
divalent cation required, at 1 mM Co2+ activation results in 80% of the activity with Mn2+
Co2+
-
divalent cation required, at 1 mM Co2+ activation results in 120% of the activity with Mg2+
divalent cation
-
requirement
divalent cation
-
requirement
divalent cation
-
requires both a divalent and a monovalent cation
divalent cation
-
requirement
divalent cation
-
requires both a divalent and a monovalent cation
divalent cation
-
requirement
divalent cation
-
requirement
divalent cation
-
requires both a divalent and a monovalent cation
divalent cation
-
requirement
divalent cation
-
requires both a divalent and a monovalent cation
K+
-
requirement
K+
-
apparent Km-value: 0.48 mM
K+
-
only together with activating divalent cation
K+
-
fulfills requirement for monovalent cation
K+
Busycotypus canaliculatum
-
-
K+
Pyk2 is co-dependent on Mn2+ and K+
K+
-
1 cation per active site
K+
-
best activator at optimal conditions, in decreasing order of efficiency: K+, Rb+, Cs+, Na+, NH4+, Li+
K+
-
essential activator, in the presence of K+ the affinities for phosphoenolpyruvate, ADP, ADP-Cr2+, and oxalate are 2-6fold higher than in the absence of K+ when ADP cannot bind to the enzyme until phosphoenolpyruvate forms a competent active site
K+
Musa cavendishii
-
requirement
K+
Musa cavendishii
-
Km-value 0.91 mM, hyperbolic saturation kinetics
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+
-
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+
-
necessary for full enzymatic activity
K+
-
fulfills requirement for monovalent cation
K+
-
Km-value: 50 mM in the presence of fructose diphosphate
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+
-
only together with activating divalent cation
K+
-
inhibits above 100 mM
K+
-
activates, torpid PK is significantly more sensitive to KCl with a Ka that is 69% less than the corresponding Ka from the euthermic animal
K+
K117 isozyme requires K+
K+
K117 isozyme requires K+, at saturating concentrations of PEP3-, ADP-Mg complex and free Mg2+, the Km for K+ is 8.5 mM
K+
-
only together with activating divalent cation
Mg2+
-
divalent cation required
Mg2+
-
strict requirement
Mg2+
-
divalent cation required, at 1 mM highest activity with Mg2+
Mg2+
-
apparent Km-value: 0,21 mM
Mg2+
-
fulfills absolute requirement for divalent cation
Mg2+
-
fulfills absolute requirement for divalent cation
Mg2+
Busycotypus canaliculatum
-
-
Mg2+
-
fulfills absolute requirement for divalent cation
Mg2+
-
2 cations per active site
Mg2+
-
no activity in the absence of sugar phosphate activator
Mg2+
-
the enzyme is dependent on Mn2+ ion for its activity. Fe2+ and Mg2+ show 70 and 20% of the Mn2+ activity, respectively. No activity is detected without metal or with Zn2+, Cu2+, Co2+, and Ni2+
Mg2+
Musa cavendishii
-
Km-value 0.27 mM, hyperbolic saturation kinetics
Mg2+
Musa cavendishii
-
fulfills absolute requirement for divalent cation
Mg2+
essential for activity
Mg2+
required for activity
Mg2+
-
kinetics of the enzyme at subsaturating concentrations of activators show that K+ and Mg2+ exhibit high selectivity for their respective cation binding sites, whereas when Na+ substitutes K+, Na+ and Mg2+ bind with high affinity to their incorrect sites. The ratio of the affinities of Mg2+ and K+ for the monovalent cation binding site is close to 200. For Na+ and Mg2+ this ratio is approximately 20
Mg2+
-
addition of Mg2+ protects the enzyme completely from the ferrous ion-mediated inactivation
Mg2+
-
necessary for full enzymatic activity
Mg2+
-
positive homotropic interaction with phosphoenolpyruvate and Mg2+
Mg2+
-
Km-value 0.45 mM for isozyme PKc, 1.6 mM for isozyme PKp
Mg2+
-
fulfills absolute requirement for divalent cation
Mg2+
-
Km-value 2 mM in the presence of fructose diphosphate
Mg2+
-
positive cooperativity
Mg2+
either Mn2+ or Mg2+ are required
Mg2+
-
either Mn2+ or Mg2+ are required
Mg2+
although the maximum activity is 3.8-fold higher with Mg2+ than with Mn2+, the K0.5 for Mn2+ is 250fold lower than the K0.5 for Mg2+, with no significant change in the constants for the substrates. This finding shows that Mn2+ is the preferred divalent cation, consistent with the geochemistry of the Archaean ocean
Mg2+
-
positive cooperativity
Mg2+
-
divalent cation required
Mg2+
-
required, no difference between euthermic and torpid PK responses to MgCl2
Mg2+
required for activity
Mg2+
-
either Mn2+ or Mg2+ are required
Mn2+
-
can partially replace Mg2+
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+
Busycotypus canaliculatum
-
can partially replace Mg2+
Mn2+
Pyk2 is co-dependent on Mn2+ and K+
Mn2+
-
can partially replace Mg2+
Mn2+
-
the activity of the sugar phosphate-activated enzyme is reduced to 50% if Mn2+ is omitted
Mn2+
-
can partially replace Mg2+
Mn2+
-
can partially replace Mg2+
Mn2+
-
required, binds at the active site
Mn2+
-
Km-value: 0.6 mM, flight muscle isozyme
Mn2+
-
divalent cation required
Mn2+
-
fulfills absolute requirement for divalent cation
Mn2+
-
Km-value 0.05 mM for isozyme PKc, 0.5 mM for isozyme PKp
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+
either Mn2+ or Mg2+ are required
Mn2+
-
only together with K+
Mn2+
-
either Mn2+ or Mg2+ are required
Mn2+
although the maximum activity is 3.8-fold higher with Mg2+ than with Mn2+, the K0.5 for Mn2+ is 250fold lower than the K0.5 for Mg2+, with no significant change in the constants for the substrates. This finding shows that Mn2+ is the preferred divalent cation, consistent with the geochemistry of the Archaean ocean
Mn2+
-
positive cooperativity
Mn2+
-
divalent cation required, at 1 mM Mn2+ activation results in 35% of the activity with Mg2+
Mn2+
the K+-independent enzyme, Mn2+ may mimic the allosteric effect of ribose 5-phosphate
Mn2+
-
either Mn2+ or Mg2+ are required
monovalent cation
-
requirement
monovalent cation
-
requirement
monovalent cation
-
requirement
monovalent cation
-
requires both a divalent and a monovalent cation
monovalent cation
-
requirement
monovalent cation
-
requires both a divalent and a monovalent cation
monovalent cation
-
in decreasing order of efficiency: K+, Rb+, Cs+, Na+, NH4+, Li+
monovalent cation
-
requirement
monovalent cation
-
requirement
monovalent cation
-
requires both a divalent and a monovalent cation
monovalent cation
-
requirement
monovalent cation
-
requires both a divalent and a monovalent cation
monovalent cation
-
requirement
Na+
can substitute for K+ by 51%
Na+
-
can poorly replace K+
Na+
-
in decreasing order of efficiency: K+, Rb+, Cs+, Na+, NH4+, Li+
Na+
-
in aqueous media, muscle pyruvate kinase is highly selective for K+ over Na+. Dimethylsulfoxide favors the partition of K+ and Na+ into the monovalent and divalent cation binding sites of the enzyme. The kinetics of the enzyme at subsaturating concentrations of activators show that K+ and Mg2+ exhibit high selectivity for their respective cation binding sites, whereas when Na+ substitutes K+, Na+ and Mg2+ bind with high affinity to their incorrect sites. The ratio of the affnities of Mg2+ and K+ for the monovalent cation binding site is close to 200. For Na+ and Mg2+ this ratio is approximately 20. The data suggest that K+ induces conformational hanges that prevent the binding of Mg2+ to the monovalent cation binding site
Na+
-
inhibits above 100 mM
Na+
-
activation, can replace K+
NH4+
-
requirement
NH4+
Busycotypus canaliculatum
-
requirement
NH4+
Busycotypus canaliculatum
-
can replace K+
NH4+
can substitute for K+ by 73%
NH4+
-
in decreasing order of efficiency: K+, Rb+, Cs+, Na+, NH4+, Li+
NH4+
-
only together with activating divalent cation
NH4+
-
inhibits above 100 mM
NH4+
activates, at saturating concentrations of PEP3-, ADP-Mg complex and free Mg2+, the Km for NH4+ is 2.7 mM
Zn2+
-
divalent cation required, at 1 mM Zn2+ activation results in 11% of the activity with Mg2+
Zn2+
-
activation or inhibition, concentration-dependent behaviour
Zn2+
-
divalent cation required, at 1 mM Zn2+ activation results in 6.5% of the activity with Mg2+
Zn2+
-
divalent cation required, at 1 mM Zn2 activation results in 2.5% of the activity with Mg2+
additional information
-
K-type allosteric properties only in the presence of Mg2+, not Mn2+
additional information
-
overview
additional information
-
absolute requirement for a bivalent and a monovalent cation with Mg2+ and K+ fulfilling this
additional information
-
overview
additional information
-
absolute requirement for a bivalent and a monovalent cation with Mg2+ and K+ fulfilling this
additional information
Busycotypus canaliculatum
-
interacting effects of various activators and inhibitors
additional information
isozyme Pyk2 exhibits an absolute dependence on Mn2+ together with a monovalent cation. The maximum activity of Pyk2 is detected in the presence of 5 mM Mn2+ and 100 mM K+. When NH4 +, Na+, or Li+ is substituted for K+, the relative activities of Pyk2 are maintained at 73, 51, and 38%, respectively
additional information
isozyme Pyk2 exhibits an absolute dependence on Mn2+ together with a monovalent cation. The maximum activity of Pyk2 is detected in the presence of 5 mM Mn2+ and 100 mM K+. When NH4 +, Na+, or Li+ is substituted for K+, the relative activities of Pyk2 are maintained at 73, 51, and 38%, respectively
additional information
-
isozyme Pyk2 exhibits an absolute dependence on Mn2+ together with a monovalent cation. The maximum activity of Pyk2 is detected in the presence of 5 mM Mn2+ and 100 mM K+. When NH4 +, Na+, or Li+ is substituted for K+, the relative activities of Pyk2 are maintained at 73, 51, and 38%, respectively
additional information
Pyk1 exhibits high catalytic activity using Mn2+ or Co2+ as a cation, Pyk1 only uses Mn2+ or Co2+ as cations
additional information
Pyk1 exhibits high catalytic activity using Mn2+ or Co2+ as a cation, Pyk1 only uses Mn2+ or Co2+ as cations
additional information
-
Pyk1 exhibits high catalytic activity using Mn2+ or Co2+ as a cation, Pyk1 only uses Mn2+ or Co2+ as cations
additional information
-
overview
additional information
-
no activation by Sr2+
additional information
-
no activation by Cu2+, Ni2+
additional information
-
activity is independent of free Mg2+ concentration in the range 4-20 mM
additional information
-
no activation by SCN-
additional information
-
overview
additional information
Musa cavendishii
-
absolute requirement for a bivalent and a monovalent cation with Mg2+ and K+ fulfilling this
additional information
-
no activation by Ba2+
additional information
-
no activation by Cu2+, Ni2+
additional information
-
enzyme spectra in the absence and presence of activating cations, overview
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
-
1 mM Mg2+ does not shows significant activity. No activity is observed with Ca2+ and Zn2+
additional information
-
overview
additional information
-
absolute requirement for a bivalent and a monovalent cation with Mg2+ and K+ fulfilling this
additional information
-
activity is independent of free Mg2+ concentration in the range 4-20 mM
additional information
-
overview
additional information
-
absolute requirement for a bivalent and a monovalent cation with Mg2+ and K+ fulfilling this
additional information
-
no activation by Li+
additional information
the enzyme from Thermofilum pendens is K+-independent. Eukarya pyruvate kinases have glutamate at position 117 (numbered according to the rabbit muscle enzyme), whereas in Bacteria have either glutamate or lysine and in Archaea have other residues. Glutamate at this position makes pyruvate kinases K+-dependent, whereas lysine confers K+-independence because the positively charged residue substitutes for the monovalent cation charge. The enzyme from Thermofilum pendens has Val70 at the corresponding position
additional information
-
the enzyme from Thermofilum pendens is K+-independent. Eukarya pyruvate kinases have glutamate at position 117 (numbered according to the rabbit muscle enzyme), whereas in Bacteria have either glutamate or lysine and in Archaea have other residues. Glutamate at this position makes pyruvate kinases K+-dependent, whereas lysine confers K+-independence because the positively charged residue substitutes for the monovalent cation charge. The enzyme from Thermofilum pendens has Val70 at the corresponding position
additional information
-
1 mM Mg2+ does not shows significant activity. No activity is observed with Ca2+ and Zn2+
additional information
-
catalytic activity is independent of K+
additional information
the pyruvate kinase isozyme sequences with Glu117 have been found to be K+-dependent, whereas those with Lys117 are K+-independent
additional information
the pyruvate kinase isozyme sequences with Glu117 have been found to be K+-dependent, whereas those with Lys117 are K+-independent
additional information
the pyruvate kinase isozyme sequences with Glu117 have been found to be K+-dependent, whereas those with Lys117 are K+-independent. In comparison with other K+-dependent PKs, VcIPK exhibits higher kcat and 2-5fold lower Km for the monovalent cations. No activation by Na+ and Li+. VCIPK is a good example of type Ib activation by monovalent cations. In such a mechanism, M+ coordination is absolutely required for catalysis, where both kcat and kcat/Km increase hyperbolically with [K+]
additional information
the pyruvate kinase isozyme sequences with Glu117 have been found to be K+-dependent, whereas those with Lys117 are K+-independent. In comparison with other K+-dependent PKs, VcIPK exhibits higher kcat and 2-5fold lower Km for the monovalent cations. No activation by Na+ and Li+. VCIPK is a good example of type Ib activation by monovalent cations. In such a mechanism, M+ coordination is absolutely required for catalysis, where both kcat and kcat/Km increase hyperbolically with [K+]
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(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
-
(1S,3S)-1,3-di(1H-indol-3-yl)-1,2,3,4-tetrahydrocyclopenta[b]indole
-
-
(1S,3S)-2-bromo-1,3-di(1H-indol-3-yl)-1,2,3,4-tetrahydrocyclopenta[b]indole
-
-
(1S,3S)-2-chloro-1,3-di(1H-indol-3-yl)-1,2,3,4-tetrahydrocyclopenta[b]indole
-
-
(1S,4S)-1,4-di(1H-indol-3-yl)-2,3,4,9-tetrahydro-1H-carbazole
-
-
(1S,4S)-6-chloro-1,4-bis(5-chloro-1H-indol-3-yl)-2,3,4,9-tetrahydro-1H-carbazole
-
-
(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
-
-
(2E)-1,3-bis(6-bromo-1H-indol-2-yl)prop-2-en-1-one
-
6% inhibition at 0.001 mM
(2E)-1-(3-bromo-2-hydroxyphenyl)-3-(6-bromo-1H-indol-2-yl)prop-2-en-1-one
-
41% inhibition at 0.001 mM
(2E)-1-(4-bromo-2-hydroxyphenyl)-3-(1H-indol-2-yl)prop-2-en-1-one
-
-
(2E)-1-(4-bromo-2-hydroxyphenyl)-3-(6-bromo-1H-indol-2-yl)prop-2-en-1-one
-
-
(2E)-1-(4-methoxyphenyl)-3-(2,4,6-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-1-(5-bromo-1H-indol-2-yl)-3-(6-bromo-1H-indol-2-yl)prop-2-en-1-one
-
21% inhibition at 0.001 mM
(2E)-1-(5-bromo-2-hydroxyphenyl)-3-(1H-indol-2-yl)prop-2-en-1-one
-
10% inhibition at 0.001 mM
(2E)-1-(5-bromo-2-hydroxyphenyl)-3-(6-bromo-1H-indol-2-yl)prop-2-en-1-one
-
15% inhibition at 0.001 mM
(2E)-1-(6-bromo-1H-indol-2-yl)-3-(1H-indol-2-yl)prop-2-en-1-one
-
-
(2E)-1-(6-bromo-1H-indol-2-yl)-3-(5-bromo-2-methoxyphenyl)prop-2-en-1-one
-
-
(2E)-2-[(5-bromo-2-methoxyphenyl)methylidene]-2,3,4,9-tetrahydro-1H-carbazol-1-one
-
22% inhibition at 0.001 mM
(2E)-3-(3-bromo-2-hydroxyphenyl)-1-(6-bromo-1H-indol-2-yl)prop-2-en-1-one
-
-
(2E)-3-(4-bromo-2-hydroxyphenyl)-1-(6-bromo-1H-indol-2-yl)prop-2-en-1-one
-
-
(2E)-3-(5-bromo-1H-indol-3-yl)-1-(1H-indol-2-yl)prop-2-en-1-one
-
-
(2E)-3-(5-bromo-2-hydroxyphenyl)-1-(1H-indol-2-yl)prop-2-en-1-one
-
-
(2E)-3-(5-bromo-2-hydroxyphenyl)-1-(6-bromo-1H-indol-2-yl)prop-2-en-1-one
-
-
(2E)-3-(6-bromo-1H-indol-2-yl)-1-(1H-indol-2-yl)prop-2-en-1-one
-
38% inhibition at 0.001 mM
(2E)-3-(6-bromo-1H-indol-2-yl)-1-(2-hydroxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(6-bromo-1H-indol-3-yl)-1-(1H-indol-2-yl)prop-2-en-1-one
-
45% inhibition at 0.001 mM
(2E)-3-(6-bromo-1H-indol-3-yl)-1-(1H-indol-3-yl)prop-2-en-1-one
-
28% inhibition at 0.001 mM
(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
-
(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
(6R,10S)-2-chloro-6,10-bis(5-chloro-1H-indol-3-yl)-5,6,7,8,9,10-hexahydrocyclohepta[b]indole
-
-
(6R,10S)-3-chloro-6,10-bis(6-chloro-1H-indol-3-yl)-5,6,7,8,9,10-hexahydrocyclohepta[b]indole
-
-
(6R,10S)-6,10-di(1H-indol-3-yl)-5,6,7,8,9,10-hexahydrocyclohepta[b]indole
-
-
(6R,11S)-6,11-di(1H-indol-3-yl)-6,7,8,9,10,11-hexahydro-5H-cycloocta[b]indole
-
-
(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
1-(6-bromo-1-benzothiophen-2-yl)-2-(4-bromophenyl)ethan-1-one
-
43% inhibition at 0.001 mM
1-(6-bromo-1H-indol-2-yl)-2-(4-bromophenyl)ethan-1-one
-
-
2,4-dihydroxy-N'-[(E)-(2-hydroxy-6,7,8,9-tetrahydrodibenzo[b,d]furan-1-yl)methylidene]benzohydrazide
-
-
2-(3-bromo-2-hydroxyphenyl)-1-(6-bromo-1H-indol-2-yl)ethan-1-one
-
-
2-(4-bromophenyl)-1-(1H-indol-2-yl)ethan-1-one
-
41% inhibition at 0.001 mM
2-(5-bromo-1H-benzimidazol-2-yl)-1-(5-bromo-1H-indol-2-yl)ethan-1-one
-
-
2-(5-bromo-1H-benzimidazol-2-yl)-1-(5-bromo-2-hydroxyphenyl)ethan-1-one
-
-
2-(5-bromo-1H-benzimidazol-2-yl)-1-(6-bromo-1H-indol-2-yl)ethan-1-one
-
-
2-(5-bromo-2-hydroxyphenyl)-1-(1H-indol-2-yl)ethan-1-one
-
28% inhibition at 0.001 mM
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(1-methyl-1H-indol-2-yl)ethan-1-one
-
41% inhibition at 0.001 mM
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(1H-indol-2-yl)ethan-1-one
-
-
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(3-bromo-2-hydroxyphenyl)ethan-1-one
-
-
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(3-bromo-2-methoxyphenyl)ethan-1-one
-
22% inhibition at 0.001 mM
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(3-chloro-2-hydroxyphenyl)ethan-1-one
-
43% inhibition at 0.001 mM
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(4-bromo-2-hydroxyphenyl)ethan-1-one
-
-
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(5-bromo-1H-indol-2-yl)ethan-1-one
-
-
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(5-bromo-2-methoxyphenyl)ethan-1-one
-
-
2-aminoisobutyric acid
-
allosteric inhibition
2-bromo-6-[[(6-bromo-1,3-benzothiazol-2-yl)amino]methyl]phenol
-
17% inhibition at 0.001 mM
2-hydroxy-5-iodo-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
-
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
2-[5-(5-bromo-2-methoxyphenyl)-1,3,4-oxadiazol-2-yl]-1H-indole
-
19% inhibition at 0.001 mM
2-[6-(5-bromo-2-methoxyphenyl)pyridin-2-yl]-1H-indole
-
6% inhibition at 0.001 mM
3,5-diphenoxy-2-[(2E)-3-(3,4,5-triphenoxyphenyl)prop-2-en-1-yl]phenol
-
-
3-(2,5-dimethylphenoxy)-1,2-benzothiazole 1,1-dioxide
-
a saccharin derivative, potent inhibitor, but a labile compound
3-(2-hydroxy-4-methoxyphenyl)-1-(4-methoxyphenyl)propane-1,2-diol
-
-
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-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-[(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
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
4-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
-
611% inhibition at 500 nM
4-bromo-2-[(E)-[(6-bromo-1,3-benzothiazol-2-yl)imino]methyl]phenol
-
41% inhibition at 0.001 mM
4-bromo-2-[2-(6-bromo-1H-indol-2-yl)pyridin-4-yl]phenol
-
41% inhibition at 0.001 mM
4-bromo-2-[5-(1H-indol-2-yl)-1,3,4-oxadiazol-2-yl]phenol
-
8% inhibition at 0.001 mM
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
-
-
5,7-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
5-bromo-2-(4-bromophenyl)-1H-indole
-
21% inhibition at 0.001 mM
5-bromo-2-(6-bromo-1,3-benzothiazol-2-yl)-1H-isoindole-1,3(2H)-dione
-
34% inhibition at 0.001 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-3-(4-bromophenyl)-1H-indole
-
20% inhibition at 0.001 mM
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
-
-
5-bromo-N-(5-bromo-1,3-benzothiazol-2-yl)-1H-indole-2-carboxamide
-
-
5-bromo-N-(6-bromo-1,3-benzothiazol-2-yl)-2-hydroxy-N-methylbenzamide
-
5% inhibition at 0.001 mM
5-bromo-N-(6-bromo-1,3-benzothiazol-2-yl)-2-hydroxybenzamide
-
-
6-bromo-3-(4-bromophenyl)-1H-indole
-
-
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
-
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
-
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
Ba2+
-
in decreasing order of inhibitory efficiency: Ni2+, Zn2+, Cu2+, Ca2+, Ba2+
cis-3-4-dihydrohamacanthin B
-
-
cumene hydroperoxide
-
1% residual activity after treatment with 17 mM cumene hydroperoxide at 50°C and pH 7 for 2 h
cysteine
-
fructose 1,6-diphosphate protects
D-alanine
-
allosteric inhibition
D-fructose 1,6-bisphosphate
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
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
guanidine hydrochloride
-
GnHCl
Highly phosphorylated inositol derivatives
Pigeon
-
-
-
human papillomavirus-16 E7
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
K+
-
above 100 mM, activates below
L-aspartate
31% inhibition at 0.2 mM, cPK1; 6% inhibition at 0.2 mM, cPK3
L-proline
-
allosteric inhibition
L-tryptophan
-
1 mM, significant inhibition
menadione
-
i.e. vitamin K3, shows a significantly stronger potency to inhibit isozyme PKM2 than to inhibit isozymes PKM1 and PKL
N'-[(1E)-1-(1,3-benzothiazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
-
-
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-(1H-benzimidazol-2-yl)propylidene]-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,N'-(ethane-1,2-diyl)bis[4-(2,3-dichlorobenzoyl)-1-methyl-1H-pyrrole-2-carboxamide]
-
N-(1,3-benzothiazol-2-yl)-2-hydroxy-5-sulfanylbenzamide
-
13% inhibition at 0.001 mM
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-methylphenyl)-2-[(4-sulfamoylphenyl)amino]pyridine-3-carboxamide
-
-
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-(5-bromo-1,3-benzothiazol-2-yl)-1H-indole-2-carboxamide
-
-
N-(5-bromo-1,3-benzothiazol-2-yl)-2-hydroxy-5-sulfanylbenzamide
-
48% inhibition at 0.001 mM
N-(6-bromo-1,3-benzothiazol-2-yl)-2-hydroxybenzamide
-
65% inhibition at 0.001 mM
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
-
NaF
-
non-specific phosphoenolpyruvate kinase inhibitor
NH4+
-
above 100 mM, activates below
NH4Cl
-
40 mM, 50-60% decrease in activity of recombinant enzyme
Pb2+
-
lead inhibits pyruvate kinase activity in a dose-dependent manner by interaction with its thiol groups
peracetic acid
-
1% residual activity after treatment with 4 mM peracetic acid at 25°C and pH 7 for 15 min
phenylpyruvate
-
competitive with ADP and phosphoenolpyruvate, Ala prevents inhibition
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
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
-
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
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 50°C and pH 7 for 3 h
threonine
-
fructose 1,6-diphosphate protects
valine
-
fructose 1,6-diphosphate protects
[(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
2,3-diphosphoglycerate
-
-
2,3-diphosphoglycerate
-
-
2,3-diphosphoglycerate
Pigeon
-
-
2-oxoglutarate
-
50% inhibition at 8.3 mM
2-oxoglutarate
Busycotypus canaliculatum
-
not
2-oxoglutarate
-
potent inhibitor
2-oxoglutarate
-
at 5 mM, pH 7.0, 35% inhibition
3-phosphoglycerate
-
8% inhibition at 5 mM
3-phosphoglycerate
Busycotypus canaliculatum
-
not
3-phosphoglycerate
-
80% activity at pH 6.4, 86% activity at pH 7.4
ADP
Busycotypus canaliculatum
-
at high concentrations; fructose 1,6-diphosphate partially restores
ADP
Busycotypus canaliculatum
-
activators restore
ADP
-
at high concentrations; substrate inhibition
ADP-Cr2+
-
-
ADP-Cr2+
a dead-end inhibitor; a dead-end inhibitor
AMP
-
1 mM, 77% of activity remaining
AMP
90% inhibition at 0.1 mM, cPK2
AMP
-
11% inhibition at 5 mM
AMP
Busycotypus canaliculatum
-
MgAMP
AMP
-
in a cooperative manner with ATP
arginine phosphate
Busycotypus canaliculatum
-
allosteric inhibitor; fructose 1,6-diphosphate restores
arginine phosphate
-
flight muscle isozyme: weak; fructose 1,6-diphosphate restores
ATP
-
1 mM, 77% of activity remaining; 1 mM, 87% of activity remaining
ATP
16% inhibition at 2 mM, cPK4; 24% inhibition at 2 mM, cPK2; 5% inhibition at 2 mM, cPK5; 73% inhibition at 2 mM, cPK3; 93% inhibition at 2 mM, cPK1
ATP
-
in the presence of Mg2+, not Mn2+, reversible by AMP
ATP
-
48% inhibition at 5 mM, significant allosteric effector of the partially purified enzyme
ATP
Busycotypus canaliculatum
-
MgATP2-
ATP
allosteric regulation
ATP
-
liver, not muscle enzyme
ATP
-
enzyme form I; strong
ATP
-
as pH increases (pH range 6.5-8.0), ATP elicits more inhibition
ATP
-
in a cooperative manner with AMP
ATP
-
50% inhibition at 4 mM; strong
ATP
-
glucose 6-phosphate reverses
ATP
-
fructose 1,6-diphosphate does not reverse
ATP
-
L- and R-type isozyme; phosphorylated enzyme is more sensitive than unphosphorylated enzyme
ATP
-
ADP alleviates; kinetics
ATP
-
IC50: 8.8 mM at pH 6.4, IC50: 13.7 mM at pH 7.4
ATP
product inhibition. Inhibition cannot be reversed by presence of phophoenolpyruvate or ADP
ATP
inhibition of full-length enzyme at concentration above 2.5 mM
ATP
-
at 1 mM, pH 7.0, 50% inhibition
ATP
-
allosteric inhibitor
ATP
-
torpid PK is significantly less susceptible to ATP inhibition at 5 and 35°C, with about 5fold and 2fold higher I50 ATP, respectively, as compared to the euthermic values
Ca2+
-
-
Ca2+
-
in decreasing order of inhibitory efficiency: Ni2+, Zn2+, Cu2+, Ca2+, Ba2+
Ca2+
-
strong at saturating phosphoenolpyruvate concentrations
Cd2+
-
at physiological pH, activating below
Cd2+
-
at physiological pH, activating below
citrate
-
-
citrate
74% inhibition at 4 mM, cPK2; 83% inhibition at 4 mM, cPK1; 93% inhibition at 4 mM, cPK3; 97% inhibition at 4 mM, cPK4; 98% inhibition at 4 mM, cPK5
citrate
-
60% inhibition at 5 mM, significant allosteric effector of the partially purified enzyme
citrate
-
50% inhibition at 18.4 mM
citrate
Busycotypus canaliculatum
-
not
citrate
-
fat body isozyme; weak, flight muscle isozyme
citrate
-
noncompetitive with respect to ADP
citrate
citrate at 2 mM inhibits GST-tagged PfPYK activity by over 90%, citrate slightly decreases the affinity for the PEP substrate, with no obvious change in the apparent kcat
citrate
-
IC50: 9.2 mM at pH 6.4, IC50: 14.2 mM at pH 7.4
citrate
-
potent inhibitor
citrate
-
isozyme PKI, kinetics; not isozyme PKII
citrate
-
at 5 mM, pH 7.0, 40% inhibition
citrate
citrate binds TcoPYK's active site, induces an R-state transition, and is a weak inhibitor of enzyme activity, 30% inhibition at 25 mM
Co2+
-
at physiological pH, activating below
Co2+
-
at physiological pH, activating below
Cu2+
-
-
Cu2+
-
in decreasing order of inhibitory efficiency: Ni2+, Zn2+, Cu2+, Ca2+, Ba2+
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-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 1,6-bisphosphate
-
IC50: 8.4 mM at pH 6.4, IC50: 8.0 mM at pH 7.4
D-fructose 1,6-bisphosphate
inhibition of full-length enzyme at 10 mM
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
GTP
-
-
GTP
-
0.1 mM GTP reduces the Vmax by 10%
isocitrate
-
30% inhibition at 5 mM
isocitrate
Busycotypus canaliculatum
-
not
isocitrate
-
only isozyme PKp, not PKc
isocitrate
-
76% activity at pH 6.4, 91% activity at pH 7.4
KCl
-
40 mM, 50-60% decrease in activity of recombinant enzyme
L-Ala
-
-
L-alanine
-
phosphoenolpyruvate- and Mg2+-dependent
L-alanine
Busycotypus canaliculatum
-
allosteric inhibitor; fructose 1,6-diphosphate restores
L-alanine
-
weak; weak, in the presence of Mn2+
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-alanine
-
fructose 1,6-diphosphate restores; kinetics
L-alanine
-
fructose bisphosphate protects; strong
L-alanine
-
weak; weak, flight muscle isozyme
L-alanine
-
L- and M2-type, not M1-type isozyme
L-alanine
-
fructose 1,6-diphosphate restores
L-cysteine
-
allosteric inhibition
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-glutamate
15% inhibition at 0.2 mM, cPK1
L-glutamate
-
50% inhibition at 4 mM
L-glutamate
-
dihydroxyacetone phosphate reverses
L-glutamate
Musa cavendishii
-
-
L-glutamate
-
not isozyme PKI; strong, isozyme PKII, kinetics
L-lactate
-
-
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
-
-
L-phenylalanine
-
fructose 1,6-diphosphate protects
L-phenylalanine
Busycotypus canaliculatum
-
alanine and fructose 1,6-diphosphate protect, kinetics; allosteric inhibitor; pH-dependent
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
allosterical inhibitor
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-phenylalanine
-
fructose 1,6-diphosphate protects; not in the presence of Mn2+; strong
L-phenylalanine
-
isozymes PK I and II differ in sensitivity to the inhibitor
L-phenylalanine
-
L- and M2-type, not M1-type isozyme
L-phenylalanine
-
fructose 1,6-diphosphate protects
L-phenylalanine
-
3 mM, significant inhibition
L-valine
-
allosteric inhibition
malate
Busycotypus canaliculatum
-
not
malate
-
only isozyme PKp, not PKc
malate
-
78% activity at pH 6.4, 90% activity at pH 7.4
MgATP2-
Busycotypus canaliculatum
-
allosteric inhibitor; fructose 1,6-diphosphate restores
MgATP2-
Busycotypus canaliculatum
-
activators restore activity
MgATP2-
-
feed-back inhibition; fructose 1,6-diphosphate restores
MgATP2-
Musa cavendishii
-
-
MgATP2-
-
potent inhibitor
N-ethylmaleimide
-
-
N-ethylmaleimide
-
isozyme PK1 is more sensitive than PK2
Na+
-
-
Na+
-
above 100 mM, activates below
Ni2+
-
-
Ni2+
-
in decreasing order of inhibitory efficiency: Ni2+, Zn2+, Cu2+, Ca2+, Ba2+
oxalate
-
0.2 mM, 50% of activity remaining; 0.2 mM, 71% of activity remaining, IC50: 0.41 mM
oxalate
-
50% inhibition at 4 mM
oxalate
-
50% inhibition at 0.23 mM
oxalate
-
PK I, 80% inhibition at 0.3 mM, PK II, 50% inhibition at 0.3 mM
oxalate
the binding of glucose 6-phosphate and oxalate, which potentially lock the enzyme in its active state, increase the thermal stability of the enzyme
oxalate
dead-end inhibitor
oxalate
a dead-end inhibitor; a dead-end inhibitor
oxaloacetate
-
2 mM, 82% of activity remaining; 2 mM, 88% of activity remaining
oxaloacetate
Busycotypus canaliculatum
-
not
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
phosphate
-
-
phosphate
Busycotypus canaliculatum
-
not
phosphate
Busycotypus canaliculatum
-
activators restore
phosphate
severe, restored by addition of fructose 1,6-diphosphate
phosphate
-
at high concentrations; strong
phosphate
-
at 5 mM, pH 7.0, 40% inhibition
phosphoenolpyruvate
-
1-5 mM
phosphoenolpyruvate
-
at 5°C, concentrations greater than 10 mM are inhibiting
Phosphoglycolate
-
-
Phosphoglycolate
-
only isozyme PKp, not PKc
shikonin
-
a PKM2 inhibitor
sulfate
-
-
tryptophan
-
-
tyrosine
-
-
tyrosine
-
fructose 1,6-diphosphate partially protects
Urea
-
Zn2+
-
inhibition or activation, concentration-dependent behaviour
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
Zn2+
-
in decreasing order of inhibitory efficiency: Ni2+, Zn2+, Cu2+, Ca2+, Ba2+
additional information
-
not inhibited by 6-phosphogluconate, dithiothreitol or sodium tetrathionate; not inhibited by AMP, dithiothreitol or sodium tetrathionate
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK4, poor effects by L-aspartate at 0.2 mM and AMP at 0.1 mM; no effect by L-serine and L-glutamate at 0.2 mM on cPK5, poor effects by L-aspartate at 0.2 mM and AMP at 0.1 mM, and by fructose-1,6-bisphosphate at 1.0 mM; poor effect by L-serine at 0.2 mM on cPK3; poor effect by serine at 0.2 mM on cPK1; poor effects by L-glutamate and L-aspartate at 0.2 mM on cPK2
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK4, poor effects by L-aspartate at 0.2 mM and AMP at 0.1 mM; no effect by L-serine and L-glutamate at 0.2 mM on cPK5, poor effects by L-aspartate at 0.2 mM and AMP at 0.1 mM, and by fructose-1,6-bisphosphate at 1.0 mM; poor effect by L-serine at 0.2 mM on cPK3; poor effect by serine at 0.2 mM on cPK1; poor effects by L-glutamate and L-aspartate at 0.2 mM on cPK2
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK4, poor effects by L-aspartate at 0.2 mM and AMP at 0.1 mM; no effect by L-serine and L-glutamate at 0.2 mM on cPK5, poor effects by L-aspartate at 0.2 mM and AMP at 0.1 mM, and by fructose-1,6-bisphosphate at 1.0 mM; poor effect by L-serine at 0.2 mM on cPK3; poor effect by serine at 0.2 mM on cPK1; poor effects by L-glutamate and L-aspartate at 0.2 mM on cPK2
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK4, poor effects by L-aspartate at 0.2 mM and AMP at 0.1 mM; no effect by L-serine and L-glutamate at 0.2 mM on cPK5, poor effects by L-aspartate at 0.2 mM and AMP at 0.1 mM, and by fructose-1,6-bisphosphate at 1.0 mM; poor effect by L-serine at 0.2 mM on cPK3; poor effect by serine at 0.2 mM on cPK1; poor effects by L-glutamate and L-aspartate at 0.2 mM on cPK2
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK4, poor effects by L-aspartate at 0.2 mM and AMP at 0.1 mM; no effect by L-serine and L-glutamate at 0.2 mM on cPK5, poor effects by L-aspartate at 0.2 mM and AMP at 0.1 mM, and by fructose-1,6-bisphosphate at 1.0 mM; poor effect by L-serine at 0.2 mM on cPK3; poor effect by serine at 0.2 mM on cPK1; poor effects by L-glutamate and L-aspartate at 0.2 mM on cPK2
-
additional information
-
no effect by L-serine and L-glutamate at 0.2 mM on cPK4, poor effects by L-aspartate at 0.2 mM and AMP at 0.1 mM; no effect by L-serine and L-glutamate at 0.2 mM on cPK5, poor effects by L-aspartate at 0.2 mM and AMP at 0.1 mM, and by fructose-1,6-bisphosphate at 1.0 mM; poor effect by L-serine at 0.2 mM on cPK3; poor effect by serine at 0.2 mM on cPK1; poor effects by L-glutamate and L-aspartate at 0.2 mM on cPK2
-
additional information
-
poor inhibition of glucose 1-phosphate and fumaric acid at 5 mM
-
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
glucose-6-phosphate (G6P) has no significant effect on the S0.5 and kcat of Pyk2
-
additional information
glucose-6-phosphate (G6P) has no significant effect on the S0.5 and kcat of Pyk2
-
additional information
-
glucose-6-phosphate (G6P) has no significant effect on the S0.5 and kcat of Pyk2
-
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
-
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
-
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
-
IgE receptor FcepsilonRI rapid phosphorylation of tyrosine residues in M2-PK leads to its inhibition and initiation of mast cell degranulation
-
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
-
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
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
-
additional information
-
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
-
additional information
synthesis and biologic evaluation of naphthoquinone derivatives as selective small molecule inhibitors of PKM2, cytotoxicity of the compounds versus HeLa, H-1299, and HCT-116 cancer cells, overview. Presence of fructose 1,6-bisphosphate increases the IC50 values of some inhibitors
-
additional information
discovery and structure-activity relationship of 4-hydroxy-thiazolidine-2-thione derivatives as tumor cell specific pyruvate kinase M2 activators, AC50 values and cell growth inhibition of cancer cells, molecular modeling and docking study, overview
-
additional information
-
discovery and structure-activity relationship of 4-hydroxy-thiazolidine-2-thione derivatives as tumor cell specific pyruvate kinase M2 activators, AC50 values and cell growth inhibition of cancer cells, molecular modeling and docking study, overview
-
additional information
synthesis and antitumor activity of 2,3-didithiocarbamate substituted naphthoquinones as inhibitors of pyruvate kinase M2 isoform. In vitro cytotoxicity of target compounds in cancer cell lines, IC50 values, overview
-
additional information
-
no inhibition by several amino acids
-
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
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
-
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
-
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
no effects by fructose 1,6-bisphosphate or fructose 2,6-bisphosphate on the enzyme activity
-
additional information
-
no effects by fructose 1,6-bisphosphate or fructose 2,6-bisphosphate on the enzyme activity
-
additional information
-
phosphorylation by cAMP-dependent protein kinase, L- and R-type isozyme
-
additional information
-
no phosphorylation
-
additional information
-
alanine and serine cause no affection of activity but prevent the inhibition caused by phenylalanine, tryptophan or cystine
-
additional information
-
cysteamine or glutathione per se do not modify enzymatic activity, but prevent the toxic effects of lead
-
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
-
not inhibited by 5 mM ADP
-
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
-
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
-
synthesis and evaluation of several series of compounds as inhibitors of methicillin-resistant Staphylococcus aureus (MRSA) pyruvate kinase. Structure-activity analysis, overview. (2E)-3-(5-bromo-1H-indol-3-yl)-1-(1H-indol-3-yl)prop-2-en-1-one and (2E)-1-(3-bromo-2-hydroxyphenyl)-3-(1H-indol-2-yl)prop-2-en-1-one are not inhibitory
-
additional information
-
bisindolyl-cycloalkane indoles result from the reaction of aliphatic dialdehydes and indole. As bisindolyl-natural alkaloid compounds are inhibitors of the methicillin-resistant Staphylococcus aureus (MRSA)-pyruvate kinase (PK), analysis of the compounds as MRSA PK inhibitors, structure-activity relationships of structurally varied compounds, overview. MIC value (mg/ml) of the compounds versus Staphylococcus aureus strains ATCC 25923 and MRSA ATCC 43300. No inhibition by (1S,4S)-7-chloro-1,4-bis(6-chloro-1H-indol-3-yl)-2,3,4,9-tetrahydro-1H-carbazole
-
additional information
-
no substrate inhibition at pH-optimum
-
additional information
-
not inhibited by L-alanine
-
additional information
-
increasing buffer concentrations inhibit, least inhibitory: imidazole-HCl
-
additional information
no significant effect by D-fructose 6-phosphate and D-ribulose 1,5-bisphosphate
-
additional information
-
no significant effect by D-fructose 6-phosphate and D-ribulose 1,5-bisphosphate
-
additional information
no inhibiton by L-alanine
-
additional information
no inhibiton by L-alanine
-
additional information
-
no inhibiton by L-alanine
-
additional information
-
citrate does not have any effect on PK activity at concentrations up to 10 mM. F16P2 also shows little propensity to effect PK activity under the conditions of this experiment up to a concentration of 10 mM
-
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(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
-
-
ATP
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
D-fructose 1,6-diphosphate
D-fructose 2,6-bisphosphate
D-fructose 2,6-diphosphate
D-fructose 6-phosphate
-
requirement with Mg2+, activation with Mn2+
D-fructose-1,6-bisphosphate
D-glucose 1,6-diphosphate
-
slight activation
D-ribose 1-diphosphate 5-phosphate
-
activation, kinetics, much more effective than fructose 1,6-diphosphate or glucose 1,6-diphosphate
D-Ribulose 1,5-diphosphate
D-tagatose 1,6-diphosphate
-
requirement with Mg2+, activation with Mn2+
D-tagatose 6-phosphate
-
requirement with Mg2+, activation with Mn2+
dihydroxyacetone phosphate
erythrose 4-phosphate
-
requirement with Mg2+, activation with Mn2+
fructose 1,6-bisphosphate
fructose 2,6-bisphosphate
fructose-1,6-bisphosphate
glutamic acid
-
activation
glyceraldehyde 3-phosphate
GSH
-
activation, can replace dithiothreittol
isoleucine
-
slight activation, kinetics
isopropyl-beta-D-thiogalactopyranoside
-
50% increased activity at 1 mM
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
Monovalent anions
-
activation, in decreasing order of efficiency: Cl-, Br-, NO3-
-
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
-
-
ribulose 5-phosphate
-
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
-
Triton X-100
-
50% increase of activity of the bound enzyme only
3-phosphoglycerate
-
slight activation
3-phosphoglycerate
allosteric activator. Regulation of the enzyme by a carboxylate molecule rather than a sugar phosphate may reflect a step in the evolution of glycolysis that predates the dominance of sugars in metabolism
6-phosphogluconate
-
192% of activity at 0.05 mM
6-phosphogluconate
-
at 1 mM, 200% of activity
alanine
-
activation
AMP
9% activation at 0.1 mM, cPK3
AMP
wild-type, A0.5 value 0.013 mM
AMP
-
allosteric activator
asparagine
Busycotypus canaliculatum
-
activation
asparagine
-
synergistic activation with fructose 1,6-diphosphate of isozyme PK-aerobic, not PK-anoxic
aspartate
-
allosteric activator
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
activates
D-fructose 1,6-bisphosphate
20.5% increase of activity at 2.5 mM
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
-
induces an association of two inactive dimers to the active tetrameric form
D-fructose 1,6-bisphosphate
triggers allosteric signal transduction, increases activity, binding tetramerizes the enzyme, whereas its release causes dissociation to inactive dimer
D-fructose 1,6-bisphosphate
-
-
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
-
-
D-fructose 1,6-bisphosphate
-
strong activation
D-fructose 1,6-bisphosphate
increases the affinity and reduces the cooperativity of substrate binding, increases Vmax by 20%
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
pH-dependent
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
-
-
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
kinetics
D-fructose 1,6-diphosphate
Busycotypus canaliculatum
-
activation
D-fructose 1,6-diphosphate
Busycotypus canaliculatum
-
stimulates aerobic isozyme more strongly than anoxic isozyme
D-fructose 1,6-diphosphate
Busycotypus canaliculatum
-
synergism with Asp, PK-aerobic, not PK-anoxic
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
major allosteric activator
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
requirement with Mg2+
D-fructose 1,6-diphosphate
-
with Mn2+
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
only PK II, shifting sigmoidal kinetics to hyperbolic curves, decrease in Km
D-fructose 1,6-diphosphate
-
activation
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
-
strong activation, fat body enzyme
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
heterotropic allosteric activator
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
-
activation
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 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
kinetics
D-fructose 1,6-diphosphate
-
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
more evident in the presence of glycerol
D-fructose 1,6-diphosphate
-
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
not
D-fructose 1,6-diphosphate
not
D-fructose 1,6-diphosphate
-
activation
D-fructose 1,6-diphosphate
-
slight
D-fructose 1,6-diphosphate
-
kinetics
D-fructose 1,6-diphosphate
-
allosteric activation together with phosphoenolpyruvate
D-fructose 1,6-diphosphate
-
not
D-fructose 2,6-bisphosphate
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
Busycotypus canaliculatum
-
activation
D-fructose 2,6-diphosphate
-
allosteric effector
D-fructose 2,6-diphosphate
-
allosteric effector
D-fructose 2,6-diphosphate
-
not
D-fructose 2,6-diphosphate
-
activation
D-fructose 2,6-diphosphate
-
allosteric effector
D-fructose 2,6-diphosphate
-
activation
D-fructose 2,6-diphosphate
-
best activator
D-fructose diphosphate
-
activation
D-fructose diphosphate
-
activation
D-fructose diphosphate
-
activation
D-fructose diphosphate
-
enzyme form I
D-fructose diphosphate
-
activation
D-fructose diphosphate
-
cardiac and liver isozyme, together with phosphoenolpyruvate
D-fructose diphosphate
-
activation
D-fructose diphosphate
Pigeon
-
activation
D-fructose diphosphate
-
activation
D-fructose diphosphate
-
activation
D-fructose diphosphate
-
allosteric effector
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
-
D-fructose-1,6-bisphosphate
-
allosteric effector, binds to PykF but not to PykA
D-glucose 1-phosphate
-
not
D-glucose 1-phosphate
-
slight activation, not isozyme PKp
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
isozyme PK II
D-glucose 6-phosphate
-
activation
D-glucose 6-phosphate
-
requirement with Mg2+, activation with Mn2+
D-glucose 6-phosphate
-
activation
D-glucose 6-phosphate
-
not: isozyme PKp
D-glucose 6-phosphate
-
activation
D-glucose 6-phosphate
-
requirement
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-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
not
D-ribose 5-phosphate
-
D-ribose 5-phosphate
-
activation
D-ribose 5-phosphate
-
isozyme PK II
D-ribose 5-phosphate
-
activation
D-ribose 5-phosphate
-
0.1 mM, allosteric activator
D-ribose 5-phosphate
wild-type, A0.5 value 0.0075 mM
D-ribose 5-phosphate
-
activation
D-ribose 5-phosphate
-
requirement with Mg2+, activation with Mn2+
D-ribose 5-phosphate
allosteric activator
D-ribose 5-phosphate
-
activation
D-Ribulose 1,5-diphosphate
-
activation
D-Ribulose 1,5-diphosphate
-
not
D-Ribulose 1,5-diphosphate
-
activation
D-Ribulose 1,5-diphosphate
-
kinetics
D-Ribulose 1,5-diphosphate
-
much more effective than fructose 1,6-diphosphate or glucose 1,6-diphosphate
dihydroxyacetone phosphate
-
activation
dihydroxyacetone phosphate
-
activation
dihydroxyacetone phosphate
-
requirement with Mg2+
dihydroxyacetone phosphate
-
with Mn2+
dihydroxyacetone phosphate
-
activation
dihydroxyacetone phosphate
-
kinetics
dithiothreitol
-
required for optimal activity
dithiothreitol
-
activation
fructose 1,6-bisphosphate
FBP, allosteric regulation, Pyk2 is dependent on FBP activation
fructose 1,6-bisphosphate
-
-
fructose 1,6-bisphosphate
-
fructose 1,6-bisphosphate
-
activates isozyme PKM2 by direct binding
fructose 1,6-bisphosphate
FBP, enzyme PKM2 is allosterically activated by the glycolytic metabolite
fructose 1,6-bisphosphate
FBP, FBP-mediated PKM2 activation requires the tetramerization of PKM2. The dimeric enzyme, e.g. mutant PKM2G415R, is in its tense form and cannot be activated by FBP
fructose 1,6-bisphosphate
FBP, molecular dynamics (MD) simulations of the human PKM2 (hPKM2) monomer in the absence (apo-hPKM2) or presence of FBP (hPKM2-FBP), the molecular dynamics simulations identify conformational changes in PKM2 associated with FBP binding, overview
fructose 1,6-bisphosphate
-
-
fructose 1,6-bisphosphate
-
-
fructose 1,6-bisphosphate
FBP, molecular dynamics simulations identify conformational changes in PKM2 associated with FBP binding
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
-
-
fructose 1,6-bisphosphate
Ka of liver enzyme is 0.029 mM, of anoxic liver enzyme 0.0032 mM
fructose 1,6-bisphosphate
F16BP, lower activation
fructose 1,6-bisphosphate
F16BP, lower activation
fructose 1,6-bisphosphate
slight activation
fructose 1,6-bisphosphate
slight activation, the isozyme with Glu117 is an active K+-dependent enzyme, at the same substrate concentration, its Vmax in the absence of fructose 1,6-bisphosphate is 80% of that with its effector. VcIPK is activated 31fold by fructose 1,6-bisphosphate
fructose 2,6-bisphosphate
F26BP, a much more potent allosteric activator of trypanosomatid PYKs compared to fructose 1,6-bisphosphate, F16BP
fructose 2,6-bisphosphate
F26BP, a much more potent allosteric activator of trypanosomatid PYKs compared to fructose 1,6-bisphosphate, F16BP
fructose 2,6-bisphosphate
-
fructose 6-phosphate
slight activation
fructose 6-phosphate
moderate activation
fructose-1,6-bisphosphate
FBP, 22% activation at 1 mM, cPK1
fructose-1,6-bisphosphate
FBP, 4% activation at 1 mM, cPK2
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)
glucose 6-phosphate
G6P, an activator increasing the apparent maximal velocity of isozyme PYK-I, 1.5fold activation at 5 mM without affecting the affinity and cooperativity towards the PEP substrate. The binding of glucose 6-phosphate and oxalate, which potentially lock the enzyme in its active state, increase the thermal stability of the enzyme. PfPYK might be a V-type allosteric enzyme with respect to G6P. In silico docking of the activator G6P to the canonical effector site, the phosphate group of G6P forms a number of favorable interactions with the PO4-2 motif
glucose 6-phosphate
slight activation
glucose 6-phosphate
VcIIPK is activated 159fold by glucose 6-phosphate
glyceraldehyde 3-phosphate
-
activation
glyceraldehyde 3-phosphate
-
activation
glyceraldehyde 3-phosphate
-
requirement with Mg2+
glyceraldehyde 3-phosphate
-
with Mn2+
glyceraldehyde 3-phosphate
-
not
L-aspartate
-
Ka-value 0.31 mM, reverses inhibition by L-glutamate
L-serine
12% activation at 0.2 mM, cPK2
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
phosphate
-
activation
phosphate
Pigeon
-
activation
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
-
activation
-
phosphorylated hexoses
-
activation
-
phosphorylated hexoses
-
requirement with Mg2+
-
phosphorylated hexoses
-
with Mn2+
-
phosphorylated hexoses
Pigeon
-
activation
-
ribose 5-phosphate
slight activation
ribose 5-phosphate
Rib 5-P, VcIIPK is activated 200fold by ribose 5-phosphate. the pyruvate kinase with Lys117 is a K+-independent enzyme displaying an allosteric activation by ribose 5-phosphate. In the K+-independent enzyme, Mn2+ may mimic the allosteric effect of ribose 5-phosphate
ribose 5-phosphate
the pyruvate kinase with Lys117 is a K+-independent enzyme displaying an allosteric activation by ribose 5-phosphate. In the K+-independent enzyme, Mn2+ may mimic the allosteric effect of ribose 5-phosphate
additional information
-
not activated by 6-phosphogluconate
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK4, poor effect by fructose-1,6-bisphosphate at 1.0 mM
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK4, poor effect by fructose-1,6-bisphosphate at 1.0 mM
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK4, poor effect by fructose-1,6-bisphosphate at 1.0 mM
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK4, poor effect by fructose-1,6-bisphosphate at 1.0 mM
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK4, poor effect by fructose-1,6-bisphosphate at 1.0 mM
-
additional information
-
no effect by L-serine and L-glutamate at 0.2 mM on cPK4, poor effect by fructose-1,6-bisphosphate at 1.0 mM
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK5
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK5
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK5
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK5
-
additional information
no effect by L-serine and L-glutamate at 0.2 mM on cPK5
-
additional information
-
no effect by L-serine and L-glutamate at 0.2 mM on cPK5
-
additional information
poor effect by AMP at 0.1 mM on cPK1
-
additional information
poor effect by AMP at 0.1 mM on cPK1
-
additional information
poor effect by AMP at 0.1 mM on cPK1
-
additional information
poor effect by AMP at 0.1 mM on cPK1
-
additional information
poor effect by AMP at 0.1 mM on cPK1
-
additional information
-
poor effect by AMP at 0.1 mM on cPK1
-
additional information
poor effect by fructose-1,6-bisphosphate at 1 mM and L-glutamate at 0.2 mM on cPK3
-
additional information
poor effect by fructose-1,6-bisphosphate at 1 mM and L-glutamate at 0.2 mM on cPK3
-
additional information
poor effect by fructose-1,6-bisphosphate at 1 mM and L-glutamate at 0.2 mM on cPK3
-
additional information
poor effect by fructose-1,6-bisphosphate at 1 mM and L-glutamate at 0.2 mM on cPK3
-
additional information
poor effect by fructose-1,6-bisphosphate at 1 mM and L-glutamate at 0.2 mM on cPK3
-
additional information
-
poor effect by fructose-1,6-bisphosphate at 1 mM and L-glutamate at 0.2 mM on cPK3
-
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
glucose-6-phosphate (G6P) has no significant effect on the S0.5 and kcat of Pyk2
-
additional information
glucose-6-phosphate (G6P) has no significant effect on the S0.5 and kcat of Pyk2
-
additional information
-
glucose-6-phosphate (G6P) has no significant effect on the S0.5 and kcat of Pyk2
-
additional information
-
not activated by fructose 1,6-bisphosphate
-
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
-
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
different modes of PKM2 activation by FBP and SAICAR, schematic overview
-
additional information
-
different modes of PKM2 activation by FBP and SAICAR, schematic overview
-
additional information
no stimulation: fructose 1,6-bisphosphate
-
additional information
-
no stimulation: fructose 1,6-bisphosphate
-
additional information
-
enzyme is not affected by fructose-1,6-bisphosphate and glucose 6-phosphate
-
additional information
no effects by fructose 1,6-bisphosphate or fructose 2,6-bisphosphate on the enzyme activity
-
additional information
-
no effects by fructose 1,6-bisphosphate or fructose 2,6-bisphosphate on the enzyme activity
-
additional information
no activation by fructose 1,6-bisphosphate
-
additional information
-
no activation by fructose 1,6-bisphosphate
-
additional information
-
no activation by glucose 1,6-diphosphate, 5'-IMP, 2',3'-AMP, 2',3'-GMP, 2',3'-UMP
-
additional information
-
not activated by 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
no significant effect by D-fructose 6-phosphate and D-ribulose 1,5-bisphosphate
-
additional information
-
no significant effect by D-fructose 6-phosphate and D-ribulose 1,5-bisphosphate
-
additional information
L-aspartate has no significant effect on the activity of the liver enzyme at 0-20 mM
-
additional information
L-aspartate has no significant effect on the activity of the liver enzyme at 0-20 mM
-
additional information
-
L-aspartate has no significant effect on the activity of the liver enzyme at 0-20 mM
-
additional information
neither L-aspartate nor fructose 1,6-bisphosphate has an influence on muscle pyruvate kinase in terms of activation
-
additional information
neither L-aspartate nor fructose 1,6-bisphosphate has an influence on muscle pyruvate kinase in terms of activation
-
additional information
-
neither L-aspartate nor fructose 1,6-bisphosphate has an influence on muscle pyruvate kinase in terms of activation
-
additional information
-
citrate does not have any effect on PK activity at concentrations up to 10 mM. fructose 1,6-bisphoaphate also shows little propensity to effect PK activity under the conditions of this experiment up to a concentration of 10 mM
-
additional information
-
no activation by 6-phosphogluconate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.35
ATP
allosteric enzyme, pH 7.0
0.0003 - 4.58
phosphoenolpyruvate
additional information
additional information
-
0.00017
ADP
pH and temperature not specified in the publication
0.00039
ADP
in presence of inhibitor suramin, pH and temperature not specified in the publication
0.03
ADP
cPK2, pH 7.5, 25°C
0.03 - 0.05
ADP
-
PKc-isozyme
0.03 - 0.05
ADP
-
25°C, pH 7.9
0.037
ADP
-
ADP in form of MgADP-
0.055
ADP
-
at pH 7.4, in the presence of 10 mM glutamate
0.069
ADP
70°C, pH not specified in the publication
0.07
ADP
cPK4, pH 7.5, 25°C
0.082 - 0.4
ADP
-
pH 7.1, 37°C
0.082 - 0.4
ADP
-
pH 7.4, 25°C
0.082 - 0.4
ADP
-
L-type isozyme, pH 7.4, 37°C
0.087
ADP
-
ADP in form of MgADP-
0.092
ADP
pH 6.0, 45°C, recombinant enzyme with His6 tag
0.0965
ADP
-
pH 7.0, 25°C
0.101
ADP
-
at pH 6.4, in the presence of 10 mM glutamate
0.113
ADP
80°C, pH not specified in the publication
0.12
ADP
Musa cavendishii
-
hyperbolic saturation kinetics, pH 6.9, 25°C
0.12
ADP
-
cosubstrate UDP, isozyme PKc, 25°C, pH 7.9
0.12
ADP
liver enzyme, pH 7.2, 22°C
0.13
ADP
anoxic liver enzyme, pH 7.2, 22°C
0.137
ADP
65°C, pH not specified in the publication
0.14
ADP
pH 6.0, 45°C, recombinant enzyme without His6 tag
0.14
ADP
cPK3, pH 7.5, 25°C
0.15
ADP
cPK1, pH 7.5, 25°C
0.16 - 0.17
ADP
-
pH 6.5, 25°C
0.16 - 0.17
ADP
-
isozyme II, 30°C, pH 6.8
0.164
ADP
50°C, pH not specified in the publication
0.2
ADP
muscle enzyme, pH 7.2, 22°C
0.2 - 0.35
ADP
-
enzyme form I
0.2 - 0.35
ADP
-
enzyme form I
0.2 - 0.35
ADP
-
30°C, pH 6.8
0.2 - 0.35
ADP
-
25°C, pH 7.9
0.2 - 0.35
ADP
Busycotypus canaliculatum
-
pH 7.0, 20°C
0.2 - 0.35
ADP
-
PKp-isozyme
0.2 - 0.35
ADP
-
PKp-isozyme
0.2 - 0.35
ADP
-
M-type isozyme, 25°C, pH 7.0
0.214
ADP
wild-type, pH 7.5
0.214
ADP
mutant E451W, pH 7.5
0.24
ADP
allosteric enzyme, pH 7.0
0.24
ADP
pH 8.0, 32°C, activation by 2 mM D-fructose-1,6-bisphosphate
0.25
ADP
mutant PKM2G415R, pH 7.6, 37°C
0.26
ADP
pH 7.0, 25°C, recombinant His-tagged enzyme
0.27
ADP
pH 7.0, 25°C, recombinant non-His-tagged enzyme
0.28
ADP
anoxic muscle enzyme, pH 7.2, 22°C
0.32
ADP
-
purified enzyme, pH 7.0, 5°C
0.34
ADP
cPK5, pH 7.5, 25°C
0.357
ADP
-
native enzyme, at pH 7.4 and 37°C
0.365
ADP
-
recombinant enzyme, at pH 7.4 and 37°C
0.39
ADP
-
in the presence of glucose 6-phosphate, pH 7.5
0.4 - 0.6
ADP
-
pH 7.4, 37°C
0.4 - 0.6
ADP
-
R-type isozyme, pH 7.4, 37°C
0.44
ADP
-
purified enzyme, pH 7.0, 35°C
0.46
ADP
-
solubilized enzyme
0.52 - 0.56
ADP
-
bound enzyme
0.57
ADP
-
purified enzyme, pH 7.0, 25°C/room temperature
0.6
ADP
-
50°C, pH not specified in the publication
0.7
ADP
-
in the presence of Mg2+, pH 7.1, 30°C
0.83
ADP
-
in the presence of ATP, pH 7.4, 37°C
0.98 - 1
ADP
-
M1-type isozyme, pH 7.4, 37°C
1.05
ADP
-
apparent value
1.4 - 1.5
ADP
-
M2-type isozyme, pH 7.4, 37°C
2
ADP
-
mutant enzyme E117K, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C
2.3
ADP
-
wild type enzyme, in the presence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C
7.99
ADP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37°C
14.1
ADP
-
wild type enzyme, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°Cin 50 mM Mes-Tris, pH 6.0, at 25°C
2.53
CDP
-
pH 7.4, 25°C
6.8
CDP
-
isozyme PKII, pH 7.1, 25°C
9
CDP
-
isozyme PKI, pH 7.1, 25°C
0.026
GDP
-
pH 7.5
0.0544
GDP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37°C
0.098 - 0.1
GDP
-
pH 7.5, 25°C
0.098 - 0.1
GDP
-
pH 7.4, 25°C
0.25 - 0.26
GDP
-
IDP, isozyme PKc, 25°C, pH 7.9
0.25 - 0.26
GDP
-
UDP, at pH 7.5
2.2
GDP
-
isozyme PKp, 25°C, pH 7.9
0.049 - 0.1
IDP
-
-
0.049 - 0.1
IDP
-
25°C, pH 7.9
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
-
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
-
isozyme PKc
0.193
IDP
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37°C
4
IDP
-
isozyme PKp, 25°C, pH 7.9
0.0003
phosphoenolpyruvate
Y235F mutant, Vmax = 0.6 micromol/min/mg
0.0018
phosphoenolpyruvate
Y235A mutant, Vmax = 1.1 micromol/min/mg
0.0018
phosphoenolpyruvate
Y235S mutant, Vmax = 1.2 micromol/min/mg
0.0019
phosphoenolpyruvate
wild-type, Vmax = 3.8 micromol/min/mg
0.011
phosphoenolpyruvate
muscle enzyme, pH 7.2, 22°C
0.02 - 0.05
phosphoenolpyruvate
-
bound enzyme
0.02 - 0.03
phosphoenolpyruvate
-
solubilized 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
0.025
phosphoenolpyruvate
-
purified enzyme, pH 7.0, 5°C
0.029
phosphoenolpyruvate
muscle enzyme, pH 6.6, 22°C
0.033
phosphoenolpyruvate
-
pH 7.5, 30°C
0.033
phosphoenolpyruvate
-
15°, pH 7.0, isoform PK I, in summer
0.033
phosphoenolpyruvate
-
purified enzyme, pH 7.0, 35°C
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
-
0.04 - 0.063
phosphoenolpyruvate
-
pH 7.5
0.04 - 0.063
phosphoenolpyruvate
-
25°C, pH 7.9
0.04 - 0.063
phosphoenolpyruvate
Busycotypus canaliculatum
-
in the absence of fructose 1,6-diphosphate
0.04 - 0.063
phosphoenolpyruvate
-
in the presence of fructose 1,6-diphosphate
0.04 - 0.063
phosphoenolpyruvate
Busycotypus canaliculatum
-
in the presence of fructose 1,6-diphosphate
0.04 - 0.063
phosphoenolpyruvate
-
in the presence of fructose 1,6-diphosphate
0.04 - 0.063
phosphoenolpyruvate
Busycotypus canaliculatum
-
pH 7.0, 20°C
0.04 - 0.063
phosphoenolpyruvate
-
2 isozymes with different kinetic mechanisms
0.045
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mn2+-activated
0.046
phosphoenolpyruvate
-
at pH 7.4
0.048
phosphoenolpyruvate
-
purified enzyme, pH 7.0, 25°C/room temperature
0.05
phosphoenolpyruvate
-
-
0.05
phosphoenolpyruvate
-
30°C, pH 8.5
0.05
phosphoenolpyruvate
cPK5, pH 7.5, 25°C
0.051
phosphoenolpyruvate
liver enzyme, pH 6.6, 22°C
0.052
phosphoenolpyruvate
-
24°C, pH 8.0
0.057
phosphoenolpyruvate
anoxic muscle enzyme, pH 6.6, 22°C
0.059
phosphoenolpyruvate
-
activated by fructose D-1,6-bisphosphate
0.06
phosphoenolpyruvate
cPK1, pH 7.5, 25°C
0.06
phosphoenolpyruvate
pH 7.0, 25°C, recombinant non-His-tagged enzyme, in presence of fructose 1,6-bisphosphate
0.061
phosphoenolpyruvate
anoxic muscle enzyme, pH 7.2, 22°C
0.064
phosphoenolpyruvate
-
-
0.066
phosphoenolpyruvate
-
pH 6.2, mutant enzyme T298C, Mn2+- and fructose 1,6-bisphosphate activated
0.069
phosphoenolpyruvate
pH 7.0, 25°C, recombinant His-tagged enzyme, in presence of fructose 1,6-bisphosphate
0.07
phosphoenolpyruvate
-
apparent value
0.073
phosphoenolpyruvate
-
recombinant enzyme, at pH 7.4 and 37°C
0.076
phosphoenolpyruvate
-
native enzyme, at pH 7.4 and 37°C
0.082
phosphoenolpyruvate
-
at pH 6.4
0.089
phosphoenolpyruvate
-
pH 6.5, 30°C
0.09
phosphoenolpyruvate
-
30°C, pH 7.5
0.092
phosphoenolpyruvate
anoxic liver enzyme, pH 6.6, 22°C
0.093
phosphoenolpyruvate
-
at pH 7.4, in the presence of 10 mM glutamate
0.093
phosphoenolpyruvate
70°C, pH not specified in the publication
0.098
phosphoenolpyruvate
Musa cavendishii
-
hyperbolic saturation kinetics, pH 6.9, 25°C
0.099
phosphoenolpyruvate
-
pH 6.2, 30°C
0.1
phosphoenolpyruvate
-
pH 6.8, 30°C
0.1
phosphoenolpyruvate
-
in the presence of D-fructose 1,6-bisphosphate
0.11
phosphoenolpyruvate
allosteric enzyme, pH 7.0
0.112
phosphoenolpyruvate
mutant C436M, pH not specified in the publication, 30°C
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 30°C
0.115
phosphoenolpyruvate
65°C, pH not specified in the publication
0.116
phosphoenolpyruvate
-
PykII, in 100 mM Tris-HCl,pH 8.5, at 37°C
0.12
phosphoenolpyruvate
-
pH 6.8, 24°C
0.12
phosphoenolpyruvate
-
30°C, pH 6.5
0.13
phosphoenolpyruvate
-
wild type enzyme, in the presence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C
0.15
phosphoenolpyruvate
-
at pH 6.4, in the presence of 10 mM glutamate
0.15 - 0.16
phosphoenolpyruvate
-
-
0.15 - 0.16
phosphoenolpyruvate
-
enzyme form I
0.17
phosphoenolpyruvate
pH 8.0, 32°C, activation by 2 mM D-fructose-1,6-bisphosphate
0.17
phosphoenolpyruvate
cPK3, pH 7.5, 25°C
0.17
phosphoenolpyruvate
cPK4, pH 7.5, 25°C
0.1785
phosphoenolpyruvate
-
pH 7.0, 25°C
0.18
phosphoenolpyruvate
-
cosubstrate ADP
0.18
phosphoenolpyruvate
-
cosubstrate ADP
0.18
phosphoenolpyruvate
-
pH 7.4, 37°C
0.18
phosphoenolpyruvate
-
L-type isozyme, 25°C, pH 7.0
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 30°C
0.19
phosphoenolpyruvate
-
-
0.193
phosphoenolpyruvate
-
15°, pH 7.0, isoform PK II, in winter
0.2
phosphoenolpyruvate
-
pH 7.1, 30°C, in the presence of Mg2+, 7fold lower in the presence of Mn2+
0.21
phosphoenolpyruvate
-
26°C
0.22
phosphoenolpyruvate
-
in the presence of glucose 6-phosphate, at pH 7.5
0.22
phosphoenolpyruvate
-
enzyme from larva
0.225
phosphoenolpyruvate
50°C, pH not specified in the publication
0.23
phosphoenolpyruvate
pH 7.5, 37°C
0.24
phosphoenolpyruvate
-
mutant enzyme E117K, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C
0.24
phosphoenolpyruvate
wild-type enzyme, pH not specified in the publication, 30°C
0.242
phosphoenolpyruvate
-
pH 6.2, mutant enzyme T298C, Mn2+-activated
0.26
phosphoenolpyruvate
-
enzyme from adult
0.26
phosphoenolpyruvate
80°C, pH not specified in the publication
0.27
phosphoenolpyruvate
-
in the absence of the high-affinity IgE receptor FcepsilonRI
0.3 - 0.96
phosphoenolpyruvate
-
L-type, pH 7.4, 37°C
0.31
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mg2+ and fructose 1,6-bisphosphate activated
0.31
phosphoenolpyruvate
liver enzyme, pH 7.2, 22°C
0.33
phosphoenolpyruvate
recombinant enzyme, pH 7.2, 25°C, in presence of fructose 1,6-bisphosphate
0.345
phosphoenolpyruvate
mutant C436H, pH not specified in the publication, 30°C
0.35
phosphoenolpyruvate
-
-
0.372
phosphoenolpyruvate
mutant C436A, pH not specified in the publication, 30°C
0.38
phosphoenolpyruvate
recombinant enzyme, pH 7.2, 25°C, in presence of fructose 2,6-bisphosphate
0.39
phosphoenolpyruvate
recombinant enzyme, pH 7.2, 25°C, in presence of fructose 1,6-bisphosphate
0.4 - 0.57
phosphoenolpyruvate
Pigeon
-
-
0.4 - 0.57
phosphoenolpyruvate
-
-
0.4 - 0.57
phosphoenolpyruvate
-
pH 7.4, 37°C
0.4 - 0.57
phosphoenolpyruvate
-
M2-type isozyme, pH 7.4, 37°C
0.41
phosphoenolpyruvate
-
pH 7.4, 30°C
0.45
phosphoenolpyruvate
-
allosteric enzyme, pH 7.5, 24°C
0.49
phosphoenolpyruvate
recombinant enzyme, pH 7.2, 25°C, in presence of fructose 2,6-bisphosphate
0.54
phosphoenolpyruvate
-
allosteric enzyme, pH 7.0, 24°C
0.55
phosphoenolpyruvate
pH 7.0, 25°C, recombinant His-tagged enzyme
0.55
phosphoenolpyruvate
anoxic liver enzyme, pH 7.2, 22°C
0.552
phosphoenolpyruvate
mutant S12D, pH not specified in the publication, 30°C
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 25°C
0.65
phosphoenolpyruvate
recombinant enzyme, pH 7.2, 25°C
0.68
phosphoenolpyruvate
pH 7.0, 25°C, recombinant non-His-tagged enzyme
0.703
phosphoenolpyruvate
mutant C436N, pH not specified in the publication, 30°C
0.76
phosphoenolpyruvate
cPK2, pH 7.5, 25°C
0.768
phosphoenolpyruvate
mutant C436T, pH not specified in the publication, 30°C
0.802
phosphoenolpyruvate
mutant C436S, pH not specified in the publication, 30°C
0.804
phosphoenolpyruvate
mutant C436D, pH not specified in the publication, 30°C
0.88
phosphoenolpyruvate
-
in the presence of alanine
0.9
phosphoenolpyruvate
-
-
1
phosphoenolpyruvate
pH 7.0, 25°C, recombinant His-tagged enzyme, in presence of glucose 6-phosphate
1.05
phosphoenolpyruvate
-
26°C
1.1
phosphoenolpyruvate
-
at 25°C
1.18
phosphoenolpyruvate
-
pH 6.2, wild-type enzyme, Mg2+-activated
1.2
phosphoenolpyruvate
mutant PKM2G415R, pH 7.6, 37°C
1.3
phosphoenolpyruvate
-
pH 7.4
1.4
phosphoenolpyruvate
-
R-type isozyme, pH 7.4, 37°C
1.5
phosphoenolpyruvate
-
in the absence of activator
1.88
phosphoenolpyruvate
recombinant enzyme, pH 7.2, 25°C
2.1
phosphoenolpyruvate
pH 8.0, 32°C
3.3
phosphoenolpyruvate
-
50°C, pH not specified in the publication
4.43
phosphoenolpyruvate
-
pH 6.2, mutant enzyme T298C, Mg2+- and fructose 1,6-bisphosphate activated
4.58
phosphoenolpyruvate
pH 7.0, 35°C
0.025
pyruvate
-
25°C, sample taken in June
0.055
pyruvate
-
25°C, sample taken in January
0.48
pyruvate
allosteric enzyme, pH 7.0
0.41
UDP
-
pH 7.4, 25°C
0.72 - 0.73
UDP
-
pH 7.1, 25°C
2.4
UDP
-
isozyme PKp, 25°C, pH 7.9
additional information
additional information
-
-
-
additional information
additional information
-
-
additional information
additional information
-
-
-
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
-
kinetic parameters
-
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
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
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
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
Busycotypus canaliculatum
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic properties
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
pH-dependence
-
additional information
additional information
-
allosteric enzyme
-
additional information
additional information
-
kinetic properties of phosphorylated and dephosphorylated kinases
-
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 of different MW-forms of Chlorella kinase
-
additional information
additional information
-
hyperbolic saturation kinetics for phosphoenolpyruvate, ADP, Mg2+, K+
-
additional information
additional information
-
assay and kinetics overview
-
additional information
additional information
-
assay and kinetics overview
-
additional information
additional information
-
assay and kinetics overview
-
additional information
additional information
-
assay and kinetics overview
-
additional information
additional information
-
assay and kinetics overview
-
additional information
additional information
-
assay and kinetics overview
-
additional information
additional information
Amaranthus sp.
-
coupled assay for leaf crude extracts
-
additional information
additional information
-
coupled assay for leaf crude extracts
-
additional information
additional information
-
coupled assay for leaf crude extracts
-
additional information
additional information
-
coupled assay for leaf crude extracts
-
additional information
additional information
-
coupled assay for leaf crude extracts
-
additional information
additional information
-
allosteric pattern dissappears at pH 5.9
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
Antarctic fish
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
kinetics overview
-
additional information
additional information
-
influence of fructose 1,6-bisphosphate on kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten 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
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
-
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
-
S0.5 value of phosphoenolpyruvate is 1.06 mM for wild-type, 1.3 mM for mutant E451W
-
additional information
additional information
-
kinetics, in presence of saturated substrate concentration, the enzyme exhibits hyperbolic kinetics for both ADP and PEP
-
additional information
additional information
phosphoenolpyruvate affinity is sensitive to the nature of the side chain at position 436
-
additional information
additional information
-
phosphoenolpyruvate affinity is sensitive to the nature of the side chain at position 436
-
additional information
additional information
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
-
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
the kinetic mechanism is random order with a rapid equilibrium
-
additional information
additional information
-
the kinetic mechanism is random order with a rapid equilibrium
-
additional information
additional information
allosteric mechanism and structural changes, overview
-
additional information
additional information
-
allosteric mechanism and structural changes, overview
-
additional information
additional information
despite their different allosteric behavior, both isozymes display a rapid equilibrium random order kinetic mechanism. Kinetic analysis, detailed overview
-
additional information
additional information
despite their different allosteric behavior, both isozymes display a rapid equilibrium random order kinetic mechanism. Kinetic analysis, detailed overview
-
additional information
additional information
isozyme Pyk2 has a relatively lower affinity for ADP compared to isozyme Pyk1
-
additional information
additional information
isozyme Pyk2 has a relatively lower affinity for ADP compared to isozyme Pyk1
-
additional information
additional information
-
isozyme Pyk2 has a relatively lower affinity for ADP compared to isozyme Pyk1
-
additional information
additional information
Michaelis-Menten kinetics for phosphoenolpyruvate
-
additional information
additional information
-
Michaelis-Menten kinetics for phosphoenolpyruvate
-
additional information
additional information
-
torpid pyruvate kinase (PK) displays a nearly threefold increase in Km PEP as compared to control PK when assayed at 5°C
-
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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
0.0168
(1S,3S)-1,3-di(1H-indol-3-yl)-1,2,3,4-tetrahydrocyclopenta[b]indole
Staphylococcus aureus
-
precombinant enzyme, pH 7.5, 30°C
0.0061
(1S,3S)-2-bromo-1,3-di(1H-indol-3-yl)-1,2,3,4-tetrahydrocyclopenta[b]indole
Staphylococcus aureus
-
precombinant enzyme, pH 7.5, 30°C
0.0068
(1S,3S)-2-chloro-1,3-di(1H-indol-3-yl)-1,2,3,4-tetrahydrocyclopenta[b]indole
Staphylococcus aureus
-
precombinant enzyme, pH 7.5, 30°C
0.0085
(1S,4S)-1,4-di(1H-indol-3-yl)-2,3,4,9-tetrahydro-1H-carbazole
Staphylococcus aureus
-
precombinant enzyme, pH 7.5, 30°C
0.05
(1S,4S)-6-chloro-1,4-bis(5-chloro-1H-indol-3-yl)-2,3,4,9-tetrahydro-1H-carbazole
Staphylococcus aureus
-
precombinant enzyme, pH 7.5, 30°C
0.000185
(2-[(1E)-1-[2-(5-bromo-2-hydroxybenzoyl)hydrazinylidene]ethyl]-1-methyl-1H-indol-6-yl)dibromanium
Staphylococcus aureus
-
pH not specified in the publication, 30°C
0.000553
(2E)-1-(4-bromo-2-hydroxyphenyl)-3-(1H-indol-2-yl)prop-2-en-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000132
(2E)-1-(4-bromo-2-hydroxyphenyl)-3-(6-bromo-1H-indol-2-yl)prop-2-en-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
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
0.000005
(2E)-1-(6-bromo-1H-indol-2-yl)-3-(1H-indol-2-yl)prop-2-en-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000008
(2E)-1-(6-bromo-1H-indol-2-yl)-3-(5-bromo-2-methoxyphenyl)prop-2-en-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000403
(2E)-3-(3-bromo-2-hydroxyphenyl)-1-(6-bromo-1H-indol-2-yl)prop-2-en-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000014
(2E)-3-(4-bromo-2-hydroxyphenyl)-1-(6-bromo-1H-indol-2-yl)prop-2-en-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.00178
(2E)-3-(5-bromo-1H-indol-3-yl)-1-(1H-indol-2-yl)prop-2-en-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000355
(2E)-3-(5-bromo-2-hydroxyphenyl)-1-(1H-indol-2-yl)prop-2-en-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000024
(2E)-3-(5-bromo-2-hydroxyphenyl)-1-(6-bromo-1H-indol-2-yl)prop-2-en-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000343
(2E)-3-(6-bromo-1H-indol-2-yl)-1-(2-hydroxyphenyl)prop-2-en-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
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
0.0026
(6R,10S)-2-chloro-6,10-bis(5-chloro-1H-indol-3-yl)-5,6,7,8,9,10-hexahydrocyclohepta[b]indole
Staphylococcus aureus
-
precombinant enzyme, pH 7.5, 30°C
0.0025
(6R,10S)-3-chloro-6,10-bis(6-chloro-1H-indol-3-yl)-5,6,7,8,9,10-hexahydrocyclohepta[b]indole
Staphylococcus aureus
-
precombinant enzyme, pH 7.5, 30°C
0.0102
(6R,10S)-6,10-di(1H-indol-3-yl)-5,6,7,8,9,10-hexahydrocyclohepta[b]indole
Staphylococcus aureus
-
precombinant enzyme, pH 7.5, 30°C
0.0113
(6R,11S)-6,11-di(1H-indol-3-yl)-6,7,8,9,10,11-hexahydro-5H-cycloocta[b]indole
Staphylococcus aureus
-
precombinant enzyme, pH 7.5, 30°C
0.000015
(E)-5-bromo-2-hydroxy-N'-(1-(4,5,6-trifluoro-1Hindol-2-yl)ethylidene)benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000214
(E)-5-bromo-2-hydroxy-N'-(1-(5-hydroxy-1H-indol-2-yl)ethylidene)benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000178
(E)-5-bromo-2-hydroxy-N'-(1-(5-methoxy-1H-indol-2-yl)ethylidene)benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000024
(E)-5-bromo-N'-(1-(4,5-difluoro-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.00002
(E)-5-bromo-N'-(1-(5,6-difluoro-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000049
(E)-5-bromo-N'-(1-(5-bromo-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000451
(E)-5-bromo-N'-(1-(5-bromo-1H-indol-2-yl)propylidene)-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000052
(E)-5-bromo-N'-(1-(5-chloro-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000049
(E)-5-bromo-N'-(1-(5-fluoro-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000024
(E)-5-bromo-N'-(1-(6-bromo-1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000863
(E)-N'-((1H-indol-2-yl)methylene)-5-bromo-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000151
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-2-hydroxy-5-iodobenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.008615
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000074
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-3,5-dibromo-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.00815
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-3-bromobenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.001312
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-4-bromo-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000064
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-5-bromo-2-(prop-2-ynyloxy)benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000324
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-5-bromo-2-hydroxy-4-methoxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000085
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-5-bromo-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000182
(E)-N'-(1-(1H-indol-2-yl)ethylidene)-5-bromo-2-methoxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000126
(E)-N'-(1-(1H-indol-2-yl)propylidene)-5-bromo-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000049
(E)-N'-[(1H-indol-2-yl)methylene]-5-bromo-2-methoxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000063
(E)-N'-[1-(1H-indol-2-yl)ethylidene]-5-bromo-2-ethoxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000445
(E/Z)-N'-((1H-indol-2-yl)(phenyl)methylene)-5-bromo-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.00001
1-(6-bromo-1H-indol-2-yl)-2-(4-bromophenyl)ethan-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000116
2-(3-bromo-2-hydroxyphenyl)-1-(6-bromo-1H-indol-2-yl)ethan-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000012
2-(4-bromophenyl)-1-(1H-indol-2-yl)ethan-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000003
2-(5-bromo-1H-benzimidazol-2-yl)-1-(5-bromo-1H-indol-2-yl)ethan-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000011
2-(5-bromo-1H-benzimidazol-2-yl)-1-(5-bromo-2-hydroxyphenyl)ethan-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000002
2-(5-bromo-1H-benzimidazol-2-yl)-1-(6-bromo-1H-indol-2-yl)ethan-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000011
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(1H-indol-2-yl)ethan-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000043
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(3-bromo-2-hydroxyphenyl)ethan-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000004
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(3-chloro-2-hydroxyphenyl)ethan-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000214
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(4-bromo-2-hydroxyphenyl)ethan-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000023
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(5-bromo-1H-indol-2-yl)ethan-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000008
2-(6-bromo-1,3-benzothiazol-2-yl)-1-(5-bromo-2-methoxyphenyl)ethan-1-one
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000483
2-hydroxy-5-iodo-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°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
0.01
3-(2,5-dimethylphenoxy)-1,2-benzothiazole 1,1-dioxide
Leishmania mexicana
-
pH 7.2, 25°C
0.295
3-(2-hydroxy-4-methoxyphenyl)-1-(4-methoxyphenyl)propane-1,2-diol
Homo sapiens
-
at pH 8.0 and 22°C
0.000042
3-hydroxy-N'-[(1E)-1-(1H-indol-2-yl)ethylidene]naphthalene-2-carbohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000059
3-hydroxy-N'-[(1E)-1-(4,5,6-trifluoro-1-methyl-1H-indol-2-yl)ethylidene]naphthalene-2-carbohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000052
3-hydroxy-N'-[(1E)-1-(4,5,6-trifluoro-1-methyl-1H-indol-2-yl)propylidene]naphthalene-2-carbohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000031
3-hydroxy-N'-[(1E)-1-(4,5,6-trifluoro-1H-indol-2-yl)propylidene]naphthalene-2-carbohydrazide
Staphylococcus aureus
-
pH 7.5, 30°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
0.005
3-[(2,5-dimethylphenyl)sulfanyl]-1,2-benzothiazole 1,1-dioxide
Leishmania mexicana
-
pH 7.2, 25°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
0.000251
5-bromo-2-(ethoxymethoxy)-N'-((1E)-1-(1H-indol-2-yl)ethylidene)benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000841
5-bromo-2-hydroxy-4-methoxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000227
5-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-benzimidazol-2-yl)ethylidene]benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000381
5-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
0.000461
5-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)propylidene]benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000084
5-bromo-2-hydroxy-N'-[(1E)-1-(1H-indol-2-yl)ethylidene]benzohydrazide
Staphylococcus aureus
-
pH not specified in the publication, 30°C
0.000114
5-bromo-2-hydroxy-N'-[(1E)-1-(1H-indol-2-yl)propylidene]benzohydrazide
Staphylococcus aureus
-
pH not specified in the publication, 30°C
0.000055
5-bromo-2-hydroxy-N'-[(1E)-1-(4,5,6-trifluoro-1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000043
5-bromo-2-hydroxy-N'-[(1E)-1-(5-iodo-1H-indol-2-yl)ethylidene]benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000794
5-bromo-2-hydroxy-N'-[(1E)-1-(5-methoxy-1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.006043
5-bromo-2-hydroxy-N'-[(E)-(1-methyl-1H-indol-2-yl)(phenyl)methylidene]benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.003087
5-bromo-2-hydroxy-N'-[(E)-(1-methyl-1H-indol-2-yl)methylidene]benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000145
5-bromo-N'-[(1E)-1-(4,5-difluoro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000061
5-bromo-N'-[(1E)-1-(5,6-difluoro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000016
5-bromo-N'-[(1E)-1-(5,6-difluoro-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH not specified in the publication, 30°C
0.000146
5-bromo-N'-[(1E)-1-(5-bromo-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000168
5-bromo-N'-[(1E)-1-(5-bromo-1-methyl-1H-indol-2-yl)propylidene]-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000228
5-bromo-N'-[(1E)-1-(5-chloro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000165
5-bromo-N'-[(1E)-1-(5-fluoro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000017
5-bromo-N'-[(1E)-1-(6-bromo-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000228
5-bromo-N'-[(1E)-1-(6-chloro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH not specified in the publication, 30°C
0.000165
5-bromo-N'-[(1E)-1-(6-fluoro-1-methyl-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH not specified in the publication, 30°C
0.000045
5-bromo-N'-[(1E)-1-(6-fluoro-1H-indol-2-yl)ethylidene]-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH not specified in the publication, 30°C
0.000008
5-bromo-N-(5-bromo-1,3-benzothiazol-2-yl)-1H-indole-2-carboxamide
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000003
5-bromo-N-(6-bromo-1,3-benzothiazol-2-yl)-2-hydroxybenzamide
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000102
6-bromo-3-(4-bromophenyl)-1H-indole
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.00006
bromodeoxytopsentin
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000016
cis-3-4-dihydrohamacanthin B
Staphylococcus aureus
-
pH and temperature not specified in the publication
8
D-fructose 1,6-bisphosphate
Ricinus communis
-
IC50: 8.4 mM at pH 6.4, IC50: 8.0 mM at pH 7.4
17.2
diphosphate
Ricinus communis
-
IC50: 9.8 mM at pH 6.4, IC50: 17.2 mM at pH 7.4
1.2
glutamate
Ricinus communis
-
IC50: 2.5 mM at pH 6.4, IC50: 1.2 mM at pH 7.4
130 - 550
guanidine hydrochloride
0.000224
N'-[(1E)-1-(1,3-benzothiazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000286
N'-[(1E)-1-(1-benzothiophen-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000091
N'-[(1E)-1-(1H-benzimidazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
0.000126
N'-[(1E)-1-(1H-benzimidazol-2-yl)propylidene]-5-bromo-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000115
N'-[(1E)-1-(5-bromo-1-methyl-1H-indol-2-yl)ethylidene]-3-hydroxynaphthalene-2-carbohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000079
N'-[(1E)-1-(5-bromo-1-methyl-1H-indol-2-yl)propylidene]-3-hydroxynaphthalene-2-carbohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000026
N'-[(1E)-1-(5-bromo-1H-indol-2-yl)ethylidene]-3-hydroxynaphthalene-2-carbohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000018
N'-[(1E)-1-(5-bromo-1H-indol-2-yl)propylidene]-3-hydroxynaphthalene-2-carbohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.00091
N'-[(3Z)-1-ethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-3-hydroxynaphthalene-2-carbohydrazide
Staphylococcus aureus
-
pH not specified in the publication, 30°C
0.0593 - 0.0775
N-(3-carboxy-4-hydroxy)phenyl-2,5-dimethylpyrrole
0.000051
N-(5-bromo-1,3-benzothiazol-2-yl)-1H-indole-2-carboxamide
Staphylococcus aureus
-
pH and temperature not specified in the publication
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
0.00295
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl piperidine-1-carbodithioate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.00295
(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)methyl piperidine-1-carbodithioate
Homo sapiens
recombinant His-tagged enzyme, pH 7.5, 37°C
0.028
4-amino-2-methylnaphthalen-1-ol
Homo sapiens
-
pH 7.5, 25°C, recombinant His6-tagged isozyme PKM2, in absence of D-fructose 1,6-bisphosphate
0.045
4-amino-2-methylnaphthalen-1-ol
Homo sapiens
-
pH 7.5, 25°C, recombinant His6-tagged isozyme PKM2, in presence of D-fructose 1,6-bisphosphate
0.12
4-amino-2-methylnaphthalen-1-ol
Homo sapiens
-
pH 7.5, 25°C, recombinant His6-tagged isozyme PKL, in absence of D-fructose 1,6-bisphosphate
0.191
4-amino-2-methylnaphthalen-1-ol
Homo sapiens
-
pH 7.5, 25°C, recombinant His6-tagged isozyme PKM1, in absence of D-fructose 1,6-bisphosphate
0.000381
5-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000381
5-bromo-2-hydroxy-N'-[(1E)-1-(1-methyl-1H-indol-2-yl)ethylidene]benzohydrazide
Staphylococcus aureus
-
pH not specified in the publication, 30°C
0.8
ATP
Saccharolobus solfataricus
65°C, pH not specified in the publication
0.8
ATP
Saccharolobus solfataricus
70°C, pH not specified in the publication
0.8
ATP
Saccharolobus solfataricus
80°C, pH not specified in the publication
1.1
ATP
Trachemys scripta elegans
anoxic liver enzyme, pH 7.2, 22°C, in presence of fructose 1,6-bisphosphate
1.3
ATP
Lepus europaeus
-
enzyme from heart, at pH 7.4 and 30°C
1.8
ATP
Lepus europaeus
-
enzyme from skeletal muscle, at pH 7.4 and 30°C
2
ATP
Oryctolagus cuniculus
-
enzyme from heart, at pH 7.4 and 30°C
2
ATP
Trachemys scripta elegans
liver enzyme, pH 7.2, 22°C, in presence of fructose 1,6-bisphosphate
2.5
ATP
Trachemys scripta elegans
liver enzyme, pH 7.2, 22°C
2.7
ATP
Trachemys scripta elegans
anoxic liver enzyme, pH 7.2, 22°C
5
ATP
Brassica juncea
-
pH 7.0, 25°C
5
ATP
Oryctolagus cuniculus
-
enzyme from skeletal muscle, at pH 7.4 and 30°C
7.9
ATP
Trachemys scripta elegans
anoxic muscle enzyme, pH 7.2, 22°C
11.6
ATP
Trachemys scripta elegans
muscle enzyme, pH 7.2, 22°C
13.7
ATP
Ricinus communis
-
IC50: 8.8 mM at pH 6.4, IC50: 13.7 mM at pH 7.4
3.64
citrate
Brassica juncea
-
pH 7.0, 25°C
14.2
citrate
Ricinus communis
-
IC50: 9.2 mM at pH 6.4, IC50: 14.2 mM at pH 7.4
130
guanidine hydrochloride
Urocitellus richardsonii
-
torpid enzyme, pH 7.0, 35°C
350
guanidine hydrochloride
Urocitellus richardsonii
-
torpid enzyme, pH 7.0, 5°C
376
guanidine hydrochloride
Urocitellus richardsonii
-
euthermic enzyme, pH 7.0, 5°C
443
guanidine hydrochloride
Urocitellus richardsonii
-
euthermic enzyme, pH 7.0, 25°C/room temperature
550
guanidine hydrochloride
Urocitellus richardsonii
-
torpid enzyme, pH 7.0, 25°C/room temperature
51
KCl
Trachemys scripta elegans
anoxic muscle enzyme, pH 7.2, 22°C
54
KCl
Trachemys scripta elegans
muscle enzyme, pH 7.2, 22°C
410
KCl
Trachemys scripta elegans
anoxic liver enzyme, pH 7.2, 22°C
433
KCl
Trachemys scripta elegans
liver enzyme, pH 7.2, 22°C
0.01
L-alanine
Trachemys scripta elegans
anoxic liver enzyme, pH 7.2, 22°C
0.1
L-alanine
Trachemys scripta elegans
liver enzyme, pH 7.2, 22°C
6.2
L-glutamate
Arabidopsis thaliana
-
5 mM, 30% of activity remaining, IC50: 2.1 mM, IC50: 6.2 mM
6.2
L-glutamate
Arabidopsis thaliana
-
5 mM, 59% of activity remaining, IC50: 6.2 mM
34.4
Lactate
Trachemys scripta elegans
muscle enzyme, pH 7.2, 22°C
131
Lactate
Trachemys scripta elegans
anoxic liver enzyme, pH 7.2, 22°C
177.6
Lactate
Trachemys scripta elegans
anoxic muscle enzyme, pH 7.2, 22°C
187
Lactate
Trachemys scripta elegans
liver enzyme, pH 7.2, 22°C
0.15
menadione
Homo sapiens
-
pH 7.5, 25°C, recombinant His6-tagged isozyme PKM2, in absence of D-fructose 1,6-bisphosphate
0.381
menadione
Homo sapiens
-
pH 7.5, 25°C, recombinant His6-tagged isozyme PKM2, in presence of D-fructose 1,6-bisphosphate
0.837
menadione
Homo sapiens
-
pH 7.5, 25°C, recombinant His6-tagged isozyme PKL, in absence of D-fructose 1,6-bisphosphate
3.407
menadione
Homo sapiens
-
pH 7.5, 25°C, recombinant His6-tagged isozyme PKM1, in absence of D-fructose 1,6-bisphosphate
0.000091
N'-[(1E)-1-(1H-benzimidazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH 7.5, 30°C
0.000091
N'-[(1E)-1-(1H-benzimidazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000091
N'-[(1E)-1-(1H-benzimidazol-2-yl)ethylidene]-5-bromo-2-hydroxybenzohydrazide
Staphylococcus aureus
-
pH not specified in the publication, 30°C
0.0593
N-(3-carboxy-4-hydroxy)phenyl-2,5-dimethylpyrrole
Homo sapiens
-
pH 7.5, 25°C, recombinant His6-tagged isozyme PKM2, in absence of D-fructose 1,6-bisphosphate
0.0775
N-(3-carboxy-4-hydroxy)phenyl-2,5-dimethylpyrrole
Homo sapiens
-
pH 7.5, 25°C, recombinant His6-tagged isozyme PKM2, in presence of D-fructose 1,6-bisphosphate
0.149
oxalate
Plasmodium falciparum
pH and temperature not specified in the publication
0.41
oxalate
Arabidopsis thaliana
-
0.2 mM, 71% of activity remaining, IC50: 0.41 mM
0.00882
shikonin
Homo sapiens
pH 7.5, 37°C
0.00882
shikonin
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
600
Urea
Urocitellus richardsonii
-
torpid enzyme, pH 7.0, 35°C
900
Urea
Urocitellus richardsonii
-
euthermic enzyme, pH 7.0, 5°C
1190
Urea
Urocitellus richardsonii
-
torpid enzyme, pH 7.0, 25°C/room temperature
1260
Urea
Urocitellus richardsonii
-
euthermic enzyme, pH 7.0, 25°C/room temperature
1406
Urea
Trachemys scripta elegans
anoxic muscle enzyme, pH 7.2, 22°C
1410
Urea
Trachemys scripta elegans
liver enzyme, pH 7.2, 22°C
1728
Urea
Urocitellus richardsonii
-
torpid enzyme, pH 7.0, 5°C
1901
Urea
Trachemys scripta elegans
muscle enzyme, pH 7.2, 22°C
1980
Urea
Trachemys scripta elegans
anoxic liver enzyme, pH 7.2, 22°C
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evolution
significant evolutionary distance existing between the type I and type II isoenzymes in Gram-negative bacteria
evolution
14 putative pyruvate kinase genes are encoded by the Arabidopsis thaliana genome. Determination of five cytosol-localized pyruvate kinases, out of the fourteen putative pyruvate kinase genes encoded by the Arabidopsis thaliana genome, phylogenetic analysis. The five identified cytosolic pyruvate kinase isoforms adjust the carbohydrate flux through the glycolytic pathway in Arabidopsis thaliana, by distinct regulatory qualities, such as individual expression pattern as well as dissimilar responsiveness to allosteric effectors and enzyme subgroup association
evolution
although Corynebacterium glutamicum is assumed to possess only one Pyk (pyk1, NCgl2008), NCgl2809 is annotated as a pyruvate kinase with an unknown role. NCgl2809 is identified as encoding pyruvate kinase (pyk2) in Corynebacterium glutamicum
evolution
enzyme EhPyk is the shortest Pyk known to date as it contains only two of the three characterized domains when compared to the other homologues, phylogenetic analysis, the enzyme belongs to a distinct branch from the known type I/II Pyks
evolution
-
although Corynebacterium glutamicum is assumed to possess only one Pyk (pyk1, NCgl2008), NCgl2809 is annotated as a pyruvate kinase with an unknown role. NCgl2809 is identified as encoding pyruvate kinase (pyk2) in Corynebacterium glutamicum
-
evolution
-
significant evolutionary distance existing between the type I and type II isoenzymes in Gram-negative bacteria
-
evolution
-
although Corynebacterium glutamicum is assumed to possess only one Pyk (pyk1, NCgl2008), NCgl2809 is annotated as a pyruvate kinase with an unknown role. NCgl2809 is identified as encoding pyruvate kinase (pyk2) in Corynebacterium glutamicum
-
evolution
-
although Corynebacterium glutamicum is assumed to possess only one Pyk (pyk1, NCgl2008), NCgl2809 is annotated as a pyruvate kinase with an unknown role. NCgl2809 is identified as encoding pyruvate kinase (pyk2) in Corynebacterium glutamicum
-
evolution
-
although Corynebacterium glutamicum is assumed to possess only one Pyk (pyk1, NCgl2008), NCgl2809 is annotated as a pyruvate kinase with an unknown role. NCgl2809 is identified as encoding pyruvate kinase (pyk2) in Corynebacterium glutamicum
-
evolution
-
although Corynebacterium glutamicum is assumed to possess only one Pyk (pyk1, NCgl2008), NCgl2809 is annotated as a pyruvate kinase with an unknown role. NCgl2809 is identified as encoding pyruvate kinase (pyk2) in Corynebacterium glutamicum
-
evolution
-
although Corynebacterium glutamicum is assumed to possess only one Pyk (pyk1, NCgl2008), NCgl2809 is annotated as a pyruvate kinase with an unknown role. NCgl2809 is identified as encoding pyruvate kinase (pyk2) in Corynebacterium glutamicum
-
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
-
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
-
pyruvate kinase deficiency provides protection against infection and replication of Plasmodium falciparum in human erythrocytes
malfunction
-
pyruvate kinase-deficient Escherichia coli exhibits increased plasmid copy number and cyclic AMP levels
malfunction
-
the pyruvate kinase-deficient co-isogenic mouse strain CBAPk-1slc is protected against Babesia rodhaini infection
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
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
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
-
the absence of extracellular serine and glycine has a pronounced inhibitory effect on pyruvate kinase activity
malfunction
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
-
depletion of isoform PKM2 suppresses the proliferation of Hep-G2 and Huh-7 cells and enhances the activities of the epidermal growth factor/epidermal growth factor receptor and transforming growth factorbetA1/transforming growth factor receptor signaling pathways
malfunction
-
hereditary enzyme deficiency leads to chronic nonspherocytic hemolytic anemia
malfunction
aberrant growth factor signalling and oxidative stress inhibit PKM2, which results in the diversion of glucose carbons into anabolic and redox regulating pathways that are essential for cell growth and survival. Proliferating PKM2-null tumour cells have no detectable PK expression, which likely reflects an adaptation that suppresses expression of PKM1 in these tumours. Consistent with a negative role of high PK activity in tumour growth, both exogenous expression of PKM1 or pharmacological activators that overcome endogenous PKM2-inhibiting mechanisms impede tumour growth by increasing cellular PK activity, effectively rendering endogenous PKM2 into a PKM1-like enzyme
malfunction
aberrant growth factor signalling and oxidative stress inhibit PKM2, which results in the diversion of glucose carbons into anabolic and redox regulating pathways that are essential for cell growth and survival. Proliferating PKM2-null tumour cells have no detectable PK expression, which likely reflects an adaptation that suppresses expression of PKM1 in these tumours. Consistent with a negative role of high PK activity in tumour growth, both exogenous expression of PKM1 or pharmacological activators that overcome endogenous PKM2-inhibiting mechanisms impede tumour growth by increasing cellular PK activity, effectively rendering endogenous PKM2 into a PKM1-like enzyme
malfunction
allosteric site structure analysis of wild-type and mutant enzymes, overview. 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. The structure of the D499N mutant does not provide structural evidence for the previously observed allosteric activation of the D499N variant
malfunction
complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases. Fed-batch fermentation of the pyk2-overexpressing WTDELTApyk1 strain produces 60.27 g/l of lactic acid, which is a 47% increase compared to the parent strain under oxygen deprivation
malfunction
deletion of pyk1 results in marginal Pyk activity that is below the detection limit. Complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases
malfunction
overexpression of wild-type PKM2 increases H3K9 acetylation at the CYP1A1 enhancer, whereas overexpression of the PKM2K367M mutant fails to do so, indicating that efficient histone acetylation at the CYP1A1 enhancer requires the pyruvate kinase activity of PKM2
malfunction
-
skeletal muscle PK from the Richardson's ground squirrel may be regulated posttranslationally between the euthermic and torpid states, and this may inhibit PK functioning during torpor in accordance with the decrease in glycolytic rate during dormancy
malfunction
the inhibition of pyruvate kinase by Zn2+ may be responsible for the cytotoxicity of this metal by decreasing glycolytic flux
malfunction
-
deletion of pyk1 results in marginal Pyk activity that is below the detection limit. Complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases
-
malfunction
-
complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases. Fed-batch fermentation of the pyk2-overexpressing WTDELTApyk1 strain produces 60.27 g/l of lactic acid, which is a 47% increase compared to the parent strain under oxygen deprivation
-
malfunction
-
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
-
deletion of pyk1 results in marginal Pyk activity that is below the detection limit. Complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases
-
malfunction
-
complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases. Fed-batch fermentation of the pyk2-overexpressing WTDELTApyk1 strain produces 60.27 g/l of lactic acid, which is a 47% increase compared to the parent strain under oxygen deprivation
-
malfunction
-
deletion of pyk1 results in marginal Pyk activity that is below the detection limit. Complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases
-
malfunction
-
complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases. Fed-batch fermentation of the pyk2-overexpressing WTDELTApyk1 strain produces 60.27 g/l of lactic acid, which is a 47% increase compared to the parent strain under oxygen deprivation
-
malfunction
-
pyruvate kinase-deficient Escherichia coli exhibits increased plasmid copy number and cyclic AMP levels
-
malfunction
-
deletion of pyk1 results in marginal Pyk activity that is below the detection limit. Complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases
-
malfunction
-
complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases. Fed-batch fermentation of the pyk2-overexpressing WTDELTApyk1 strain produces 60.27 g/l of lactic acid, which is a 47% increase compared to the parent strain under oxygen deprivation
-
malfunction
-
deletion of pyk1 results in marginal Pyk activity that is below the detection limit. Complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases
-
malfunction
-
complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases. Fed-batch fermentation of the pyk2-overexpressing WTDELTApyk1 strain produces 60.27 g/l of lactic acid, which is a 47% increase compared to the parent strain under oxygen deprivation
-
malfunction
-
deletion of pyk1 results in marginal Pyk activity that is below the detection limit. Complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases
-
malfunction
-
complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene restores its growth on D-ribose, which demonstrates that Pyk2 can substitute for Pyk1 in vivo. Under oxygen deprivation, pyk1 or pyk2 deficiency decreases the generation of lactic acid, and the overexpression of either pyk1 or pyk2 increases the production of lactic acid as the activity of Pyk increases. Fed-batch fermentation of the pyk2-overexpressing WTDELTApyk1 strain produces 60.27 g/l of lactic acid, which is a 47% increase compared to the parent strain under oxygen deprivation
-
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
type-II pyruvate kinase is involved in fatty acid type-II biosynthesis
metabolism
-
CDC19 or HTG2 is involved in the phenotype of high-temperature growth
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
-
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
-
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
pyruvate kinase catalyzes the final step in glycolysis converting phosphoenolpyruvate to pyruvate, it is a central metabolic regulator
metabolism
pyruvate kinase catalyzes the last but rate-limiting step of glycolysis
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
-
pyruvate kinase isoenzyme M2 plays an important role in the control of glucose metabolism
metabolism
-
pyruvate kinase M2 activates mTORC1 by phosphorylating its inhibitor AKT1S1
metabolism
-
red blood cell pyruvate kinase is a key regulatory enzyme of red cell metabolism
metabolism
anaerobic fermentative metabolism of glycerol. Proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
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
metabolism
mode of cancer metabolism to potentially modulate the gene expression and sustain incessant proliferation by tweaking the chromatin topography, overview
metabolism
-
pyruvate kinase (PK) is a key member of the glycolytic pathway. Ground squirrel torpor during winter hibernation is characterized by numerous physiological and biochemical changes, including alterations to fuel metabolism. During torpor, many tissues switch from carbohydrate to lipid catabolism, often by regulating key enzymes within glycolytic and lipolytic pathways
metabolism
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pyruvate kinase (PK) is an essential hub protein in the interactome of MRSA. PK plays a central role in the carbohydrate metabolism. It catalyzes the final rate-limiting step in the glycolysis which converts phosphoenolpyruvate (PEP) to pyruvate under ATP formation from ADP in an irreversible process
metabolism
pyruvate kinase M2 (PKM2) and pyruvate dehydrogenase complex (PDC) regulate production of acetyl-CoA, which functions as an acetyl donor in diverse enzymatic reactions, including histone acetylation. PKM2, the E2 subunit of PDC and histone acetyltransferase p300 constitute a complex on chromatin with arylhydrocarbon receptor (AhR), a transcription factor associated with xenobiotic metabolism. All of these factors are recruited to the enhancer of AhR-target genes, in an AhR-dependent manner
metabolism
the ATP synthesis in the pathogen Entamoeba histolytica is solely dependent on the glycolysis pathway where pyruvate kinase (Pyk) catalyzes the final reaction. This reaction is essentially an irreversible step of the pathway. Pyruvate kinase has been characterized as an enzyme, which is critical for the metabolic flux control of the second half of the Embden-Meyerhof-Parnas pathway. The regulation of Pyk is essential not only for this pathway but also for all other major cellular metabolisms coordinated in the cell
metabolism
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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
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metabolism
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pyruvate kinase is a crucial regulatory enzyme involved in glycolysis
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metabolism
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pyruvate kinase (PK) is an essential hub protein in the interactome of MRSA. PK plays a central role in the carbohydrate metabolism. It catalyzes the final rate-limiting step in the glycolysis which converts phosphoenolpyruvate (PEP) to pyruvate under ATP formation from ADP in an irreversible process
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physiological function
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part of citric acid cycle
physiological function
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M2-PK is a metabolic sensor which regulates cell proliferation, cell growth and apoptotic cell death in a glucose supply-dependent manner
physiological function
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Oct-4-mediated transcriptional activity is positively regulated by PKM2
physiological function
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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
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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
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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
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
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suppressor of cytokine signaling 3 interacts with M2-PK to decrease ATP production causing dendritic cell dysfunction
physiological function
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vesicle-associated pyruvate kinase can support vesicular glutamate and other neurotransmitter uptake in the presence of its substrates
physiological function
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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
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catalytic allosteric mechanism, overview
physiological function
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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
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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
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PYK plays a central role in a number of proliferative and infectious diseases
physiological function
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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
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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
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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 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
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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
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required role of the active site in allosteric regulation involving substrate binding, requirement for monovalent and divalent cations, overview
physiological function
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
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
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the enzyme is involved in the modified Embden-Meyerhof pathway
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
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the expression of the M2 isozyme of pyruvate kinase plays an important role in the anabolic metabolism of cancer cells
physiological function
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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
the enzyme catalyzes the final step of glycolysis
physiological function
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the enzyme is involved in glycogen catabolism
physiological function
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isoform PKM2 plasy different roles in modulating the proliferation and metastasis of hepatocellular carcinoma cells
physiological function
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the conversion between the pyruvate kinase and protein kinase activities of PKM2 are an important mechanism mediating the effects of growth signals in promoting cell proliferation
physiological function
allosteric regulation of trypanosomatid PYKs, overview
physiological function
allosteric regulation of trypanosomatid PYKs, overview
physiological function
cytosolic PK is a key player in energy allocation, as it generates ATP in the cytosol, supplies pyruvate to the TCA cycle and thereby drives mitochondrial ATP synthesis. The cytosolic pyruvate kinase (cPK) represents a key glycolytic enzyme by catalyzing phosphate transfer from phosphoenolpyruvate (PEP) to ADP for the synthesis of ATP. Besides its important functions in cellular energy homeostasis, the activity of cytosolic pyruvate kinase underlies tight regulation, for instance by allosteric effectors, that impact stability of its quaternary structure. The five identified cytosolic pyruvate kinase isoforms adjust the carbohydrate flux through the glycolytic pathway in Arabidopsis thaliana, by distinct regulatory qualities, such as individual expression pattern as well as dissimilar responsiveness to allosteric effectors and enzyme subgroup association
physiological function
cytosolic PK is a key player in energy allocation, as it generates ATP in the cytosol, supplies pyruvate to the TCA cycle and thereby drives mitochondrial ATP synthesis. The cytosolic pyruvate kinase (cPK) represents a key glycolytic enzyme by catalyzing phosphate transfer from phosphoenolpyruvate (PEP) to ADP for the synthesis of ATP. Besides its important functions in cellular energy homeostasis, the activity of cytosolic pyruvate kinase underlies tight regulation, for instance by allosteric effectors, that impact stability of its quaternary structure. The five identified cytosolic pyruvate kinase isoforms adjust the carbohydrate flux through the glycolytic pathway in Arabidopsis thaliana, by distinct regulatory qualities, such as individual expression pattern as well as dissimilar responsiveness to allosteric effectors and enzyme subgroup association. Spatial distribution of glycolytic enzymes within the cell constitutes a further point of regulation, since enzymes may localize at sites of demand for glycolytic intermediates
physiological function
human liver pyruvate kinase (hLPYK) converts phosphoenolpyruvate to pyruvate in the final step of glycolysis. hLPYK is allosterically activated by fructose-1,6-bisphosphate (Fru-1,6-BP)
physiological function
human pyruvate kinase isoform M2 (PKM2) is a glycolytic enzyme isoform implicated in cancer. Malignant cancer cells have higher levels of dimeric PKM2, which is regarded as an inactive form of tetrameric pyruvate kinase. The enzymatic activity of the PKM2 dimer likely has a key role in cancer progression. In addition to its classical role in generating ATP from ADP and the phosphate donor PEP, PKM2 also has been found to phosphorylate protein substrates
physiological function
PKM2 is recruited to gene enhancers of the AhR-target genes in an AhR-dependent manner and promotes AhR transactivation. Pyruvate kinase M2 (PKM2) and pyruvate dehydrogenase complex (PDC) regulate production of acetyl-CoA, which functions as an acetyl donor in diverse enzymatic reactions, including histone acetylation. PKM2, the E2 subunit of PDC and histone acetyltransferase p300 constitute a complex on chromatin with arylhydrocarbon receptor (AhR), a transcription factor associated with xenobiotic metabolism. All of these factors, also PKM2, are recruited to the enhancer of AhR-target genes, in an AhR-dependent manner. PKM2 contributes to enhancement of transcription of cytochrome P450 1A1 (CYP1A1), an AhR-target gene, acetylation at lysine 9 of histone H3 at the CYP1A1 enhancer. A local acetyl-CoA production system is proposed in which PKM2 and PDC locally supply acetyl-CoA to p300 from abundant PEP for histone acetylation at the gene enhancer. PKM2 sensitizes AhR-mediated detoxification in actively proliferating cells such as cancer and fetal cells
physiological function
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pyruvate kinase (PK) is an essential hub protein in the interactome of MRSA. PK plays a central role in the carbohydrate metabolism. It catalyzes the final rate-limiting step in the glycolysis which converts phosphoenolpyruvate (PEP) to pyruvate under ATP formation from ADP in an irreversible process
physiological function
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pyruvate kinase (PK) is responsible for catalyzing the final step of glycolysis, which involves the transfer of the phosphoryl group of phosphoenolpyruvate (PEP) to ADP to produce pyruvate and ATP. Pyruvate kinase has been identified as a highly interconnected essential hub protein in methicillin-resistant Staphylococcus aureus (MRSA), with structural features distinct from the human homologues
physiological function
pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection
physiological function
pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection. Pyk2 functions as a pyruvate kinase and contributes to the increased level of Pyk activity under oxygen deprivation. The catalytic activity of Pyk2 is allosterically regulated by fructose 1,6-bisphosphate activation and ATP inhibition
physiological function
pyruvate kinase enzyme catalyzes the last rate-limiting step of glycolysis converting phosphoenolpyruvate to pyruvate with the subsequent production of ATP. Pyruvate kinase M2 (PKM2) is an oncofetal isoform generated as a result of alternative splicing of the PKM mRNA transcript exhibit low basal activity and thus is a key player in regulating the glycolytic flux contributing to cancer progression. It results in the build-up of glycolytic intermediates which are directed towards the biosynthetic processes. PKM2 mediates metabolic reshuffling and is ubiquitously upregulated in several cancer types. The non-metabolic function of PKM2 as key nuclear kinase and modulator of gene expression is instrumental in cancer progression and tumorigenesis. The non-canonical function of PKM2 is an epigenetic modulator. Enzyme PKM2 interacts with the reconstituted mononucleosome complex through histone H3 and possibly obstructs the access to DNA binding factors. The interaction negatively impacts the ATP-dependent remodeling activity of chromodomain helicase DNA binding protein-7 (Chd7). Chd7 remodeling activity is required to ameliorate DNA damage and is crucial to genome stability. PKM2 blocks the Chd7 mediated sliding of nucleosome. It can be conjectured that stalling Chd7 may lead to impaired DNA damage and increased genomic instability. PKM2 negatively regulates nucleosome repositioning in chromatin and may exacerbate cancer by altering the nucleosome architecture, mechanism, overview. The nucleosome digestion activity of the PKM2-nucleosome complex is remarkably impaired as can be inferred from the digestion profile. Pyruvate kinase M2 can potentially disrupt the ChD7-mediated remodeling of nucleosome
physiological function
pyruvate kinase M2 (PKM2) is a rate-limiting enzyme of the glycolytic pathway which is highly expressed in cancer cells. Cancer cells rely heavily on PKM2 for anabolic and energy requirements
physiological function
pyruvate kinase M2 isoform (PKM2) is a crucial protein responsible for aerobic glycolysis of cancer cells. Activation of PKM2 may alter an aberrant metabolism in cancer cells
physiological function
pyruvate kinase muscle isoform 2 (PKM2) is a key glycolytic enzyme involved in ATP generation and critical for cancer metabolism. PKM2 is expressed in many human cancers and is regulated by complex mechanisms that promote tumor growth and proliferation. Amino acids are involved in regulation of pyruvate kinase muscle isoform 2, overview. Various stimuli allosterically regulate PKM2 by cycling it between highly active and less active states. Several small molecules activate PKM2 by binding to its intersubunit interface. Despite binding similarly to PKM2, cysteine and serine differentially regulate the enzyme
physiological function
relationship between pyruvate kinase activity and cariogenic biofilm formation in Streptococcus mutans biotypes in caries patients, analysis of pyruvate kinase activity with respect to caries severity, statistical analysis, overview
physiological function
The prolyl hydroxylase 3 (PHD3, EC 1.14.11.29) protein is less abundant in normal oxygen conditions (normoxia) but increases under deficient oxygen condition (hypoxia). Since cancerous cells often thrive in hypoxic conditions and predominantly express the pyruvate kinase isoforms 2 (PKM2), the PHD3/PKM2 interaction might be particularly important in cancer development. Protein interaction analysis and PHD3/PKM2 complex structure analysis, overview. PHD3 hydroxylates the PKM2 at two specific proline residues. The hydroxylated PKM2 shows enhanced binding with HIF-1alpha, which in turn increases the activity of HIF-1alpha
physiological function
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the skeletal muscle pyruvate kinase from the hibernating ground squirrel shows potential regulation by posttranslational modification during torpor. Torpid pyruvate kinase (PK) displays a nearly threefold increase in Km PEP as compared to control PK when assayed at 5°C. Torpid PK is significantly more phosphorylated than the euthermic control. PK from the torpid condition is also shown to possess nearly twofold acetyl content as compared to control PK
physiological function
various intracellular mechanisms in cancer cells maintain PKM2 in a low-activity monomeric state and forced stabilisation of tetrameric PKM2 increases its enzymatic activity thereby impeding cell proliferation
physiological function
various intracellular mechanisms in cancer cells maintain PKM2 in a low-activity monomeric state and forced stabilisation of tetrameric PKM2 increases its enzymatic activity thereby impeding cell proliferation
physiological function
Vibrio cholerae has two isozymes that contribute to the pyruvate kinase activity: one K+-dependent constitutively active isozyme and another K+-independent isozyme with essential allosteric activation. The pyruvate kinase isozyme sequences with Glu117 have been found to be K+-dependent, whereas those with Lys117 are K+-independent
physiological function
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pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection
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physiological function
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pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection. Pyk2 functions as a pyruvate kinase and contributes to the increased level of Pyk activity under oxygen deprivation. The catalytic activity of Pyk2 is allosterically regulated by fructose 1,6-bisphosphate activation and ATP inhibition
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physiological function
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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
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physiological function
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pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection
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physiological function
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pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection. Pyk2 functions as a pyruvate kinase and contributes to the increased level of Pyk activity under oxygen deprivation. The catalytic activity of Pyk2 is allosterically regulated by fructose 1,6-bisphosphate activation and ATP inhibition
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physiological function
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the enzyme catalyzes the final step of glycolysis
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physiological function
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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
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physiological function
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pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection
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physiological function
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pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection. Pyk2 functions as a pyruvate kinase and contributes to the increased level of Pyk activity under oxygen deprivation. The catalytic activity of Pyk2 is allosterically regulated by fructose 1,6-bisphosphate activation and ATP inhibition
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physiological function
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pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection
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physiological function
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pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection. Pyk2 functions as a pyruvate kinase and contributes to the increased level of Pyk activity under oxygen deprivation. The catalytic activity of Pyk2 is allosterically regulated by fructose 1,6-bisphosphate activation and ATP inhibition
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physiological function
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Vibrio cholerae has two isozymes that contribute to the pyruvate kinase activity: one K+-dependent constitutively active isozyme and another K+-independent isozyme with essential allosteric activation. The pyruvate kinase isozyme sequences with Glu117 have been found to be K+-dependent, whereas those with Lys117 are K+-independent
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physiological function
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pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection
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physiological function
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pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection. Pyk2 functions as a pyruvate kinase and contributes to the increased level of Pyk activity under oxygen deprivation. The catalytic activity of Pyk2 is allosterically regulated by fructose 1,6-bisphosphate activation and ATP inhibition
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physiological function
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pyruvate kinase (PK) is responsible for catalyzing the final step of glycolysis, which involves the transfer of the phosphoryl group of phosphoenolpyruvate (PEP) to ADP to produce pyruvate and ATP. Pyruvate kinase has been identified as a highly interconnected essential hub protein in methicillin-resistant Staphylococcus aureus (MRSA), with structural features distinct from the human homologues
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physiological function
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allosteric regulation of trypanosomatid PYKs, overview
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physiological function
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Vibrio cholerae has two isozymes that contribute to the pyruvate kinase activity: one K+-dependent constitutively active isozyme and another K+-independent isozyme with essential allosteric activation. The pyruvate kinase isozyme sequences with Glu117 have been found to be K+-dependent, whereas those with Lys117 are K+-independent
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physiological function
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pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection
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physiological function
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pyruvate kinase (Pyk) catalyzes the generation of pyruvate and ATP in glycolysis and functions as a key switch in the regulation of carbon flux distribution. Both the substrates and products of Pyk are involved in the tricarboxylic acid cycle, anaplerosis and energy anabolism, which places Pyk at a primary metabolic intersection. Pyk2 functions as a pyruvate kinase and contributes to the increased level of Pyk activity under oxygen deprivation. The catalytic activity of Pyk2 is allosterically regulated by fructose 1,6-bisphosphate activation and ATP inhibition
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physiological function
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pyruvate kinase (PK) is an essential hub protein in the interactome of MRSA. PK plays a central role in the carbohydrate metabolism. It catalyzes the final rate-limiting step in the glycolysis which converts phosphoenolpyruvate (PEP) to pyruvate under ATP formation from ADP in an irreversible process
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additional information
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allosteric mechanism of rM1-PYK, overview
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
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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
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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
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
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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
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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
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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
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
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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
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
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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
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
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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
amino acid-bound crystal structures of PKM2 display distinctive interactions within the binding pocket, causing unique allosteric effects in the enzyme. Structure-function analyses of amino acid-mediated PKM2 regulation, overview, revealing the chemical requirements in the development of mechanism-based small-molecule modulators targeting the amino acid-binding pocket of PKM2 and provide broader insights into the regulatory mechanisms of complex allosteric enzyme
additional information
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amino acid-bound crystal structures of PKM2 display distinctive interactions within the binding pocket, causing unique allosteric effects in the enzyme. Structure-function analyses of amino acid-mediated PKM2 regulation, overview, revealing the chemical requirements in the development of mechanism-based small-molecule modulators targeting the amino acid-binding pocket of PKM2 and provide broader insights into the regulatory mechanisms of complex allosteric enzyme
additional information
analysis of structure-function relationships of pyruvate kinases (PYKs) from trypanosomatids (Trypanosoma and Leishmania), especially of TcoPYK (Uniprot ID G0UYF4) and TbrPYK (Uniprot ID P30615), overview. Substrate binding causes several structural rearrangements across the entire PYK tetramer that involve (i) AC-core rotation of 6-8° (with residues 430-434 as a pivot point), (ii) closing of the lid domain (rotation of 30-40°), (iii) stabilization of the AA' dimer interfaces, and (iv) flipping of the Arg311 side chain as part of remodeling the catalytic pocket for substrate accommodation
additional information
-
analysis of structure-function relationships of pyruvate kinases (PYKs) from trypanosomatids (Trypanosoma and Leishmania), especially of TcoPYK (Uniprot ID G0UYF4) and TbrPYK (Uniprot ID P30615), overview. Substrate binding causes several structural rearrangements across the entire PYK tetramer that involve (i) AC-core rotation of 6-8° (with residues 430-434 as a pivot point), (ii) closing of the lid domain (rotation of 30-40°), (iii) stabilization of the AA' dimer interfaces, and (iv) flipping of the Arg311 side chain as part of remodeling the catalytic pocket for substrate accommodation
additional information
analysis of structure-function relationships of pyruvate kinases (PYKs) from trypanosomatids (Trypanosoma and Leishmania), especially of TcoPYK (Uniprot ID G0UYF4) and TbrPYK (Uniprot ID P30615), overview. Substrate binding causes several structural rearrangements across the entire PYK tetramer that involve (i) AC-core rotation of 6-8° (with residues 430-434 as a pivot point), (ii) closing of the lid domain (rotation of 30-40°), (iii) stabilization of the AA' dimer interfaces, and (iv) flipping of the Arg311 side chain as part of remodeling the catalytic pocket for substrate accommodation
additional information
changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation-Pi bond. Conformational toggle between the open and closed positions of the allosteric loop, structure analysis of wild-type and mutant enzymes, overview. In the absence of fructose-1,6-bisphosphate the open position is stabilized, in part, by a cation-Pi bond between Trp527 and Arg538' (from an adjacent monomer). 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. The structure of the D499N mutant does not provide structural evidence for the previously observed allosteric activation of the D499N variant
additional information
-
changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation-Pi bond. Conformational toggle between the open and closed positions of the allosteric loop, structure analysis of wild-type and mutant enzymes, overview. In the absence of fructose-1,6-bisphosphate the open position is stabilized, in part, by a cation-Pi bond between Trp527 and Arg538' (from an adjacent monomer). 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. The structure of the D499N mutant does not provide structural evidence for the previously observed allosteric activation of the D499N variant
additional information
comparisons of isozyme PYK-I structures in the active R-state and inactive T-state reveal a rock-and-lock allosteric mechanism regulated by rigid-body rotations of each subunit in the tetramer. It is likely that the GST-tag on the recombinant enzyme partially hinders or affects conformational changes occurring in the PfPYK-I tetramer, which are crucial for allosteric regulation. Structure-function analysis, overview
additional information
-
comparisons of isozyme PYK-I structures in the active R-state and inactive T-state reveal a rock-and-lock allosteric mechanism regulated by rigid-body rotations of each subunit in the tetramer. It is likely that the GST-tag on the recombinant enzyme partially hinders or affects conformational changes occurring in the PfPYK-I tetramer, which are crucial for allosteric regulation. Structure-function analysis, overview
additional information
homology modelling of EhPyk, molecular dynamics simulation study
additional information
-
homology modelling of EhPyk, molecular dynamics simulation study
additional information
molecular dynamics (MD) simulations of the human PKM2 (hPKM2) monomer in the absence (apo-hPKM2) or presence of FBP (hPKM2-FBP), analysis of the mechanical response of PKM2 upon binding of FBP, overview
additional information
the isozymes cPK1-5 show positive, synergistic effects when mixed
additional information
the isozymes cPK1-5 show positive, synergistic effects when mixed
additional information
the isozymes cPK1-5 show positive, synergistic effects when mixed
additional information
the isozymes cPK1-5 show positive, synergistic effects when mixed
additional information
the isozymes cPK1-5 show positive, synergistic effects when mixed
additional information
-
the isozymes cPK1-5 show positive, synergistic effects when mixed
additional information
-
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
-
analysis of structure-function relationships of pyruvate kinases (PYKs) from trypanosomatids (Trypanosoma and Leishmania), especially of TcoPYK (Uniprot ID G0UYF4) and TbrPYK (Uniprot ID P30615), overview. Substrate binding causes several structural rearrangements across the entire PYK tetramer that involve (i) AC-core rotation of 6-8° (with residues 430-434 as a pivot point), (ii) closing of the lid domain (rotation of 30-40°), (iii) stabilization of the AA' dimer interfaces, and (iv) flipping of the Arg311 side chain as part of remodeling the catalytic pocket for substrate accommodation
-
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decamer
-
10 * 57000, isozyme PK2, SDS-PAGE
dimer or tetramer
-
PKM2 can switch between a highly active tetrameric and an inactive dimeric form
hexamer
-
3 * 58000 + 3 64000, SDS-PAGE
monomer
-
1 * 210000, isozyme PKp, SDS-PAGE
octamer
-
4 * 60000 + 4 * 57000, gel filtration
trimer
-
M2-PK showing ProTalpha kinase activity is a trimeric association and possesses no observable pyruvate kinase activity
?
x * 61940, deduced from gene sequence
?
x * 58000, recombinant detagged enzyme, SDS-PAGE
?
x * 54000, recombinant enzyme, SDS-PAGE
?
-
x * 54000, recombinant enzyme, SDS-PAGE
-
?
-
x * 54000, recombinant enzyme, SDS-PAGE
-
?
x * 50000, SDS-PAGE, x * 49800, calculated
?
-
x * 50000, SDS-PAGE, x * 49800, calculated
-
?
x * 62570, deduced from gene sequence
dimer
-
-
dimer
-
predominant enzyme form
dimer
-
nearly inactive dimeric form
dimer
dimeric PKM2 is regarded as an inactive form of tetrameric pyruvate kinase, but the enzymatic activity of the PKM2 dimer is determined in presence of metabolite SAICAR
dimer
-
nearly inactive dimeric form
dimer
2 * 55400, SDS-PAGE, predominantly a dimer, but also some tetramer
dimer
-
2 * 57000, SDS-PAGE
homodimer
2 * 36000, recombinant enzyme, SDS-PAGE
homodimer
-
2 * 29495, MALDI-TOF spectrometry
homohexamer
6 * 67572, sequence calculation
homohexamer
-
6 * 67572, sequence calculation
-
homohexamer
-
6 * 67572, sequence calculation
-
homohexamer
-
6 * 67572, sequence calculation
-
homohexamer
-
6 * 67572, sequence calculation
-
homohexamer
-
6 * 67572, sequence calculation
-
homohexamer
-
6 * 67572, sequence calculation
-
homotetramer
-
-
homotetramer
-
4 * 56000, gel filtration
homotetramer
-
x-ray crystallography
homotetramer
enzyme structure in complex with ATP, oxalate, and fructose-2,6-bishosphate, overview
homotetramer
-
crystal structure
homotetramer
-
secondary and tertiary structure of muscle isozyme homotetramer and the four monomers with three tryptophans Trp157, Trp481, and Trp514, and bound Mg2+ and K+ per monomer, each monomer consists of the N-terminal domain, domain A, domain B, and domain C, overview
homotetramer
-
structure of muscle isozyme homotetramer and of the four monomers with Y-interface and Z-interface, each monomer consists of the N-terminal domain, domain A, domain B, and domain C, overview
homotetramer
-
4 * 80000, SDS-PAGE
homotetramer
4 * 55000, PYK-I, SDS-PAGE
homotetramer
-
4 * 56000, gel filtration
homotetramer
4 * 65100, about, full-length enzyme, sequence calculation, 4 * 53100, about, C-terminally truncated enzyme mutant, sequence calculation
homotetramer
-
4 * 50000-60000
homotetramer
-
4 * 50000-60000
-
homotetramer
-
4 * 65100, about, full-length enzyme, sequence calculation, 4 * 53100, about, C-terminally truncated enzyme mutant, sequence calculation
-
homotetramer
4 * 50000, recombinant His-tagged VcIIPK, SDS-PAGE, 4 * 54914, recombinant His-tagged VcIIPK, mass spectrometry, 4 * 52333, VcIIPK, sequence calculation
homotetramer
4 * 50000, recombinant His-tagged VcIPK, SDS-PAGE, 4 * 53138, recombinant His-tagged VcIPK, mass spectrometry, 4 * 50439, VcIPK, sequence calculation
homotetramer
-
4 * 50000, recombinant His-tagged VcIIPK, SDS-PAGE, 4 * 54914, recombinant His-tagged VcIIPK, mass spectrometry, 4 * 52333, VcIIPK, sequence calculation
-
homotetramer
-
4 * 50000, recombinant His-tagged VcIPK, SDS-PAGE, 4 * 53138, recombinant His-tagged VcIPK, mass spectrometry, 4 * 50439, VcIPK, sequence calculation
-
homotetramer
-
4 * 50000, recombinant His-tagged VcIIPK, SDS-PAGE, 4 * 54914, recombinant His-tagged VcIIPK, mass spectrometry, 4 * 52333, VcIIPK, sequence calculation
-
homotetramer
-
4 * 50000, recombinant His-tagged VcIPK, SDS-PAGE, 4 * 53138, recombinant His-tagged VcIPK, mass spectrometry, 4 * 50439, VcIPK, sequence calculation
-
tetramer
-
4 * 70000
tetramer
-
4 * 51000, SDS-PAGE
tetramer
-
4 * 49000, SDS-PAGE
tetramer
-
4 * 49000, SDS-PAGE
-
tetramer
-
4 * 65000, SDS-PAGE
tetramer
-
4 * 52000, L-type isozyme
tetramer
-
4 * 56000, SDS-PAGE
tetramer
-
x * 55000 + 4-x * 57000, SDS-PAGE
tetramer
-
4 * 58000, SDS-PAGE
tetramer
Busycotypus canaliculatum
-
4 * 72600, PK-anoxic, SDS-PAGE
tetramer
Busycotypus canaliculatum
-
4 * 71000, PK-aerobic, SDS-PAGE
tetramer
Busycotypus canaliculatum
-
4 * 64400, PK-aerobic, SDS-PAGE
tetramer
-
4 * 57000, SDS-PAGE
tetramer
-
4 * 58000, SDS-PAGE
tetramer
three-dimensional structure determination and analysis, structure comparisons, overview. Each CpPyK monomer consists of four domains: N (residues 23-32), A (residues 42-112 and 212-389), B (residues 113-211) and C (residues 390-526). The A-domain constitutes the central part of the molecule and forms a parallel (alphaa/beta)8 barrel. The B-domain contains nine beta strands that form an antiparallel beta-barrel. The active site is located at the interface of the A and B domains, and residues from both domains participate in substrate binding. The C-domain is composed of five beta strands surrounded by five alpha-helices. The allosteric site for binding the effector molecule is located in the C-domain. The A domains of the two monomers A and B form the major interface
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
4 * 66000, tetrameric in low ionic strength buffer
tetramer
-
4 * 51000, isozyme PK I, SDS-PAGE
tetramer
-
4 * 56000, isozyme PK II, SDS-PAGE
tetramer
-
4 * 62000-64000, SDS-PAGE
tetramer
crystallization data
tetramer
-
4 * 73000, SDS-PAGE
tetramer
-
4 * 73000, SDS-PAGE
-
tetramer
4 * 62000, SDS-PAGE
tetramer
-
4 * 60000, L-type isozyme, SDS-PAGE
tetramer
-
2 * 60000 + 2 * 57000-58000, most important of the "aged" isozymes, PKR2, SDS-PAGE, derived from erythroblast homotetramer by partial proteolysis and transformation into various active heterotetrameric forms with two partially proteolyzed subunits
tetramer
-
x-ray crystallography
tetramer
-
associated within the glycolytic enzyme complex
tetramer
binding of fructose 1,6-bisphosphate tetramerizes the enzyme, whereas its release causes dissociation to dimer
tetramer
-
highly active tetrameric form
tetramer
-
4 * 59000, SDS-PAGE
tetramer
-
4 * 54400, isozyme PK1, SDS-PAGE
tetramer
-
4 * 58000, SDS-PAGE, isozyme PK5
tetramer
-
4 * 59500, K4-type isozyme, SDS-PAGE
tetramer
-
4 * 58600, M4-type isozyme, SDS-PAGE
tetramer
-
highly active tetrameric form
tetramer
Musa cavendishii
-
4 * 57000, SDS-PAGE
tetramer
-
4* 57540, SDS-PAGE
tetramer
-
4* 57540, SDS-PAGE
-
tetramer
-
4 * 48000, SDS-PAGE
tetramer
-
S-type isozyme, SDS-PAGE
tetramer
-
4 * 62000-66000, SDS-PAGE
tetramer
-
2 * 56000 + 2 * 57000, SDS-PAGE
tetramer
-
x * 56000 + x * 57000, SDS-PAGE
tetramer
-
4 * 50000-52000, SDS-PAGE
tetramer
-
4 * 54000, isozyme I, SDS-PAGE
tetramer
-
4 * 47000, isozyme II, SDS-PAGE
tetramer
2 * 55400, SDS-PAGE, predominantly a dimer, but also some tetramer
tetramer
4 * 51300, SDS-PAGE
tetramer
-
structure-based molecular modeling and crystal structure analysis, overview
tetramer
-
4 * 44000, SDS-PAGE
tetramer
-
4 * 44000, SDS-PAGE
-
tetramer
-
4 * 59000, SDS-PAGE
tetramer
-
4 * 63000, SDS-PAGE
tetramer
-
4 * 62000, liver enzyme, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE, M1 isozyme
tetramer
-
4 * 66000, SDS-PAGE
tetramer
-
4 * 57000, SDS-PAGE
tetramer
-
4 * 49000, SDS-PAGE
tetramer
-
4 * 51000, native enzyme, SDS-PAGE
tetramer
-
4 * 56000, recombinant enzyme, SDS-PAGE
tetramer
4 * 57000, SDS-PAGE
tetramer
each monomer is composed of four domains: A, B, C and N, structure, overview. The central A domain, residues I59-G124 and V224-C393, is composed of an (alpha/beta)8 barrel. The B-domain, P125-P223, is composed of only beta-strands and random coils. The catalytic site is located at the interface of these two domains, where residues in domain A interact with PEP and ADP and residues from the B domain contact ADP and Mg2+. The C domain, residues V394-E531, is composed of alpha and beta structural elements. It contains the effector binding/allosteric site. The N-terminal domain includes the first fifty amino acids of the protein and is a helix-loop-helix motif, however in the TgPK1 only a single helix is observed
tetramer
-
4 * 50500, PykF, SDS-PAGE, circular dichroism spectroscopy, and gel filtration, 4 * 51500, PykA, SDS-PAGE, circular dichroism spectroscopy, and gel filtration
tetramer
-
4 * 50500, PykF, SDS-PAGE, circular dichroism spectroscopy, and gel filtration, 4 * 51500, PykA, SDS-PAGE, circular dichroism spectroscopy, and gel filtration
-
additional information
-
structure overview
additional information
Antarctic fish
-
structure overview
additional information
-
structure overview
additional information
-
structure overview
additional information
-
the isozymes are thought to be homotetramers, but hybrid isozymes result in vivo if a cell synthesizes 2 or more subunits simultaneously and in vitro after denaturation/renaturation of isozymic mixtures
additional information
-
overview
additional information
-
overview
additional information
-
structure overview
additional information
-
structure overview
additional information
a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
additional information
a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
additional information
-
a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
additional information
-
a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
-
additional information
-
a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
-
additional information
-
a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
-
additional information
-
a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
-
additional information
-
a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
-
additional information
-
a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
-
additional information
-
overview
additional information
secondary structure determination by circular dichroism spectrometry. Effect of pH on the tertiary structure, overview
additional information
-
secondary structure determination by circular dichroism spectrometry. Effect of pH on the tertiary structure, overview
additional information
-
structure overview
additional information
-
structure overview
additional information
-
structure overview
additional information
-
M2 pyruvate kinase is a substrate of delta protein kinase C. delta Protein kinase C activation in vitro or in cells does not appear to alter the enzyme activity or polymerization of M2 pyruvate kinase
additional information
-
M2-type enzyme directly interacts with promyelocytic leukemia tumor suppressor protein
additional information
the hepatitis C virus RNA-dependent RNA polymerase interacts with M2-type pyruvate kinase, but not with L-type pyruvate kinase
additional information
-
in tumors, the dimeric form of M2-PK is predominant due to direct interaction with different oncoproteins and components of the protein kinase cascade, such as HPV-16 E7, the tyrosine kinases pp60v-src, BCR-ABL, ETV6-NTRK3, FGFR-1, FLT3 and JAK-2, the serine/threonine kinase A-Raf, cytoplasmic promyelocytic leukemia tumor suppressor protein as well as phosphotyrosine peptides
additional information
the dimeric isozyme PKM2 is inactive
additional information
-
the dimeric isozyme PKM2 is inactive
additional information
although found to exist in different oligomeric forms in cells, like other pyruvate kinases, PKM2 is considered to have maximal pyruvate kinase activity as a tetramer. Prevalence of dimeric PKM2 in cancer
additional information
-
although found to exist in different oligomeric forms in cells, like other pyruvate kinases, PKM2 is considered to have maximal pyruvate kinase activity as a tetramer. Prevalence of dimeric PKM2 in cancer
additional information
-
structure overview
additional information
-
structure overview
additional information
-
overview
additional information
-
structure overview
additional information
secondary structure analysis by circular dichroism spectroscopy revealing a content of 17% alpha-helix, 34% beta-sheet, and 49% turns in the enzyme
additional information
-
secondary structure analysis by circular dichroism spectroscopy revealing a content of 17% alpha-helix, 34% beta-sheet, and 49% turns in the enzyme
additional information
-
secondary structure analysis by circular dichroism spectroscopy revealing a content of 17% alpha-helix, 34% beta-sheet, and 49% turns in the enzyme
-
additional information
-
secondary structure analysis by circular dichroism spectroscopy revealing a content of 17% alpha-helix, 34% beta-sheet, and 49% turns in the enzyme
-
additional information
-
structure overview
additional information
-
structure overview
additional information
-
structure overview
additional information
-
structure overview
additional information
structure-function analysis, overview
additional information
-
structure-function analysis, overview
additional information
-
structure overview
additional information
-
overview
additional information
-
structure overview
additional information
-
structure overview
additional information
-
overview
additional information
the C-terminal domain is not required for the tetramerization of the enzyme, homotetramerization also occurs in a truncated enzyme lacking the domain
additional information
-
the C-terminal domain is not required for the tetramerization of the enzyme, homotetramerization also occurs in a truncated enzyme lacking the domain
additional information
-
the C-terminal domain is not required for the tetramerization of the enzyme, homotetramerization also occurs in a truncated enzyme lacking the domain
-
additional information
-
structure overview
additional information
-
structure overview
additional information
-
structure overview
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K314L
-
no increased activity at pH 7.0
K325L
-
no increased activity at pH 7.0
K344L
-
no increased activity at pH 7.0
C9S/C268S/K221C
-
10000 times less active than the wild type enzyme
H425A
the A0.5 values for H425A are increased 8.0- and 60fold for D-ribose 5-phosphate and AMP
K221C
-
10000 to 100000 times less active than the wild-type enzyme
K221D
-
10000 to 100000 times less active than the wild-type enzyme
K221L
-
10000 to 100000 times less active than the wild-type enzyme
K221R
-
10000 to 100000 times less active than the wild-type enzyme
V435E
about fourfold increase in A0.5 values for D-ribose 5-phosphate compared with that of the wild-type enzyme. The A0.5 values for AMP and the S0.5 values are essentially identical
V435K
about fourfold increase in A0.5 values for D-ribose 5-phosphate compared with that of the wild-type enzyme. The A0.5 values for AMP and the S0.5 values are essentially identical
V435R
about fourfold increase in A0.5 values for D-ribose 5-phosphate compared with that of the wild-type enzyme. The A0.5 values for AMP and the S0.5 values are essentially identical
W416F/V435W
-
high affinity for phosphoenolpyruvate compared to the wild-type enzyme, but its saturation curve is still sigmoidal and hyperbolic in the presence of allosteric activators
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
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
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
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
E117K
-
decreased activity
E407G
-
the mutation is associated with pyruvate kinase deficiency
F24A
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme
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)
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
K367M
site-directed mutagenesis, the mutant lacks pyruvate kinase activity
K433E
the point mutant of PKM2 lacks phosphotyrosine peptide -binding ability
L167M/D331G
-
the mutation is associated with pyruvate kinase deficiency
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
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
Q18A
site-directed mutagenesis, the mutant shows strengthened phosphoenolpyruvate affinity compared to the wild-type enzyme
R163L
-
the mutation is associated with pyruvate kinase deficiency
R40W
-
the mutation is associated with pyruvate kinase deficiency
R479H/R486W
-
the mutation is associated with pyruvate kinase deficiency
R486W
-
the mutation is associated with pyruvate kinase deficiency
R504L
-
extreme instability
R532W
-
loss of allosteric response to the normal activator
S12A
site-directed mutagenesis, the mutant shows strengthened phosphoenolpyruvate affinity compared to the wild-type enzyme
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
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
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
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
Y235A
site-directed mutagenesis
Y235F
site-directed mutagenesis
Y235S
site-directed mutagenesis
Y593F
-
the mutant cannot be phosphorylated
H480Q
site-directed mutagenesis of putative binding site of fructose 2,6-bisphosphate. Mutant displays hyperbolic kinetics that is not changed by addition of the allosteric effector fructose 2,6-bisphosphate
K453L
site-directed mutagenesis of putative binding site of fructose 2,6-bisphosphate. Mutant retains a sigmoidal kinetics and is little affected by addition of fructose 2,6-bisphosphate
K453L/H480Q
site-directed mutagenesis of putative binding sites of fructose 2,6-bisphosphate. Mutant displays hyperbolic kinetics
D315N
3.7% of wild-type activity. S0.5 value for fructose 2,6-bisphosphate 0.001 mM
D315S
1.4% of wild-type activity. S0.5 value for fructose 2,6-bisphosphate 0.00161 mM
E451W
72% of wild-type activity. S0.5 value for fructose 2,6-bisphosphate 0.000177 mM
K335R
-
site-directed mutagenesis, structure compared to the wild-type, overview
S314N
69% of wild-type activity. S0.5 value for fructose 2,6-bisphosphate 0.000403 mM
S314Q
48% of wild-type activity. S0.5 value for fructose 2,6-bisphosphate 0.000122 mM
G338D
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loss-of-function mutation in the erythrocyte-specific pyruvate kinase gene resulting in hemolytic anemia with dramatic reduction in the half-life of eryhtrocytes. Mice carrying the mutation are highly resistant to infection with Plasmodium chabaudi. Mutation G338D has more severe effects on pyruvate kinase as well as higher protection against malaria infection than less severe mutation I90N
I90N
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loss-of-function mutation in the reythrocyte-specific pyruvate kinase gene, protective against blood-stage malaria. Mutation G338D has more severe effects on pyruvate kinase as well as higher protection against malaria infection than less severe mutation I90N
S240P
the mutant exhibits steady-state kinetic behavior that indicates that it is more responsive to regulation by effectors
T340M
the mutant is half as active as the wild type enzyme
W157A
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site-directed mutagenesis, Trp157 is located in domain B and close to the active site
W481A/W514A
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site-directed mutagenesis, Trp481 and Trp514 are located in domain C and close to the Y-interface
S22A
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mutant protein activity is decreased by as much as 90% when compared with wild-type, is more active in the absence of fructose 1,6-bisphosphate
T94A
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activity similar to the wild type enzyme
S22A
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mutant protein activity is decreased by as much as 90% when compared with wild-type, is more active in the absence of fructose 1,6-bisphosphate
-
T94A
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activity similar to the wild type enzyme
-
F463V
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reduced affinity for fructose 1,6-diphosphate and fructose 2,6-diphosphate
R22G
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strongly reduced affinity for fructose 1,6-diphosphate and fructose 2,6-diphosphate
C9S/C268S
crystallization data
C9S/C268S
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75% activity of the wild-type enzyme
H391Y
pyruvate kinase M2 isozyme missense mutation found in cells from Bloom syndrome patients prone to develop cancer, the mutant protein maintains its homotetrameric structure, similar to the wild type protein, but shows a loss of activity of 20%, the mutant shows a 6fold increase in affinity for phosphoenolpyruvate and behaves like a non-allosteric protein with compromised cooperative binding
H391Y
naturally occuring mutation from a BS patient, mutation at intersubunit contact domain of the enzyme, the mutant shows 20% reduced activity compared to the wild-type enzyme, lost cooperativity and activation by fructose 1,6-bisphosphate, increased alpha-helical content, and 6fold increased PEP affinity
K422R
pyruvate kinase M2 isozyme missense mutation found in cells from Bloom syndrome patients prone to develop cancer, the mutant protein maintains its homotetrameric structure, similar to the wild type protein, but shows a loss of activity of 75%, the affinity for phosphoenolpyruvate is lost significantly in K422R
K422R
naturally occuring mutation at intersubunit contact domain of the enzyme, the mutant shows 75% reduced activity compared to the wild-type enzyme, 3fold reduced PEP affinity, and increased cooperativity
R479H
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mutation does not alter regulation by the activator
R479H
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the mutation is associated with pyruvate kinase deficiency
R510Q
similar kinetics as wild type, but dramatically decreased stability toward heat, more susceptible to ATP inhibition
R510Q
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increased instability, increased sensitivity to the allosteric inhibitor/product
S12D
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the introduction of S12D mutation mimics the effects of phosphorylation
S12D
site-directed mutagenesis, the S12D mutation mimics the effect of phosphorylation on L-PYK function, crystal structure analysis, overview
T298A
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mutation of the proton donor, mutant is enzymatically active, with decrease in kcat, Km, altered dissociation constants of ligands
T298A
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Tl+ can activate wild-type enzyme to 85% the activity in the presence of K+. With T298S, Tl+ is about 1.5fold better activator than is K+ based on the measured turnover number values. Mutation decreases turnover number value upon activation by Tl+ and by K+
T298C
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no catalytic activity in the absence of the heterotrophic activator fructose 1,6-bisphosphate. In the presence of Mg2+ and D-fructose 1,6-bisphosphate, T298C has approximately 20% of the activity of wild-type enzyme. The activator constant for FBP increases by 1 order of magnitude compared to this constant with the wild type enzyme. T298C shows positive cooperativity by D-fructose 1,6-bisphosphate with a Hill coefficient of 2.6. 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 fructose-1,6-bisphosphate. A pH-rate profile of T298C relative to that for wild type enzyme shows that pKa2 has shifted from 6.4 in wild type to 5.5, indicating that the thiol group elicits an acidic pK shift. Inactivation of both wild type and T298C by iodoacetate elicits a pseudo-first-order loss of activity with T298C being inactivated from 8 to 100 times faster than wild-type enzyme. A pH dependence of the inactivation rate constant for T298C gives a value of pH 8.2, consistent with the pK for a thiol. Changes in fluorescence indicate that the T298C-Mg2+ complex binds PEP, ADP, and both ligands together. This demonstrates that the lack of activity is not due to the loss of substrate binding but to the lack of ability to induce the proper conformational change. The mutation also induces changes in binding of fructose-1,6-bisphosphate to all the relevant complexes. Binding of the metal and binding of phosphoenolpyruvate to the enzyme complexes are also differentially altered. Solvent isotope effects are observed for both wild type and T298C. Proton inventory studies indicate that kcat is affected by a proton from water in the transition state and the effects are metal ion-dependent. The results are consistent with water being the active site proton donor. Active site residue T298 is not critical for activity but plays a role in the activation of the water and affects the pK that modulates catalytic activity
T298C
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Tl+ can activate wild-type enzyme to 85% the activity in the presence of K+. With T298S, Tl+ is about 1.5fold better activator than is K+ based on the measured turnover number values. Mutation decreases turnover number value upon activation by Tl+ and by K+
T298S
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mutation of the proton donor, mutant is enzymatically active, with decrease in kcat, Km, altered dissociation constants of ligands
T298S
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Tl+ can activate wild-type enzyme to 85% the activity in the presence of K+. With T298S, Tl+ is about 1.5fold better activator than is K+ based on the measured turnover number values. Mutation decreases turnover number value upon activation by Tl+ and by K+
additional information
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the isopropyl-beta-D-thiogalactopyranoside-inducible pyk mutant produces 3fold higher levels of recombinant protein when grown on glucose as carbon source
additional information
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the isopropyl-beta-D-thiogalactopyranoside-inducible pyk mutant produces 3fold higher levels of recombinant protein when grown on glucose as carbon source
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additional information
construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
additional information
construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
additional information
construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
additional information
construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2. Deletion of pyk1 results in marginal Pyk activity that is below the detection limit, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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construction of single deletion mutants DELTApyk1 and DELTApyk2, and of the double deletion mutant DELTApyk1DELTApyk2, complementation of the DELTApyk1DELTApyk2 strain with the pyk2 gene
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additional information
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generation of W3110 derivative strains VH33, VH34 and VH35, that lack the main phosphoenolpyruvate consumers phosphoenolpyruvate:sugar phosphotransferase system and pyruvate kinase isozymes PykA and PykF causing modifications on cell physiology, carbon flux distribution and aromatics production capacity, overview. The phosphoenolpyruvate:sugar phosphotransferase-deficient strain shows lower specific rates for growth, glucose consumption and acetate production as well as a higher biomass yield from glucose. The effects are even more pronounced by the additional inactivation of PykA or PykF. The wild-type and mutant strains are modified to overproduce L-phenylalanine. In resting cells experiments, compared to reference strain, a 10, 4 and 7fold higher aromatics yields from glucose are observed as consequence of PTS, PTS PykA and PTS PykF inactivation, overview
additional information
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generation of W3110 derivative strains VH33, VH34 and VH35, that lack the main phosphoenolpyruvate consumers phosphoenolpyruvate:sugar phosphotransferase system and pyruvate kinase isozymes PykA and PykF causing modifications on cell physiology, carbon flux distribution and aromatics production capacity, overview. The phosphoenolpyruvate:sugar phosphotransferase-deficient strain shows lower specific rates for growth, glucose consumption and acetate production as well as a higher biomass yield from glucose. The effects are even more pronounced by the additional inactivation of PykA or PykF. The wild-type and mutant strains are modified to overproduce L-phenylalanine. In resting cells experiments, compared to reference strain, a 10, 4 and 7fold higher aromatics yields from glucose are observed as consequence of PTS, PTS PykA and PTS PykF inactivation, overview
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additional information
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contruction of stable transfectants of mouse SLC-3 cells with human pyruvate kinase cDNA. Expression of pyruvate kinase significantly decreases cells at the sub G0/G1 stage in an expression-level dependent manner. Pro-apoptotic genes such as Bad, Bnip3, and Bnip31, are down-regulated in the transfectants. Peroxiredoxin 1 and other antioxidant genes such as Cat, Txnrd1, and Glrx1 are also down-regulated
additional information
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overexpression of promyelocytic leukemia tumor suppressor protein mutant PML-2KA in the cytoplasm suppresses M2-type pyruvate kinase activity and the accumulation of lactate. PML-2KA suppresses the activity of the high-affinity terameric form of M2-type pyruvate kinase, but not of the low-affinity dimeric form
additional information
specific downregulation of M2-type pyruvate kinase by shRNA inhibits the replication of hepatitis C virus in hepatitis C virus replicon 9B cells
additional information
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G1168A and G1529A mutations at exon 11, as well as mutations C1492T, C1456T, G1291A, C1594T, G787A, G994A, and G1010C are associated with pyruvate kinase deficiency in south Iranian population
additional information
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construction of HCT116 cells silenced in both muscle isozymes PKM1 and PKM2, increased metabolic flux into the serine and glycine biosynthetic pathway in cells with reduced pyruvate kinase activity, serine and glycine deprivation decreases PKM2 activity in cells also influencing the glucose metabolism, overview
additional information
PKM2 knockout, retroviral production is used to generate HeLa S3 cells stably expressing shRNAs specific for PKM2 or AhR, and stable clones are selected with puromycin
additional information
molecular dynamics simulations are used to guide the design of mPKM2 internal light/oxygen/voltage-sensitive domain 2 (LOV2) fusion at position D24 (PiL[D24]), resulting in an engineered pyruvate kinase M2 (PKM2) variant that harbours an insertion of the light-sensing LOV2 domain from Avena Sativa within a region implicated in allosteric regulation by fructose 1,6-bisphosphate (FBP). The LOV2 photoreaction is preserved in the PiL[D24] chimera and causes secondary structure changes that are associated with a 30% decrease in the Km of the enzyme for phosphoenolpyruvate resulting in increased pyruvate kinase activity after light exposure. Importantly, this change in activity is reversible upon light withdrawal. Expression of PiL[D24] in cells leads to light-induced increase in labelling of pyruvate from glucose. Light induces a reversible increase in the enzymatic activity of purified PiL[D24]. Steady-state Michaelis-Menten kinetic parameters for PiL[D24] under dark and lit conditions determined by NMR spectroscopy at 21°C
additional information
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various N-terminal deletions and chimeric fusions to examine translocation signlaing mechanism
additional information
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construction of Htg- host strains carrying only one htg allele by repeatedly back crossing Htg- segregants from a hybrid between HB8-3A(Htg+) and BY4742(Htg-) to the Htg+ strain (HB8-3A). Three Htg strains with the desired genotype, designated HC1-5D, HE6-8D and HE120-12A, are successfully constructed by the repeated back crossing process, phenotypes, overview. The Htg+ CDC19-C allele leads to an increase in trehalose accumulation under heat stress conditions. Strains containing a single copy of the CDC19-C and CDC19-BY allele in the HE6-8D background exhibit increased trehalose accumulation under heat stress conditions. Nevertheless, replacement with a single copy of CDC19-C in the HE6-8D background does not contribute to a further increase in trehalose accumulation as compared with the HE6-8D strain carrying the Htg- CDC19-BY allele
additional information
construction of a C-terminally truncated mutant PKCT with a stop after residue 390. The catalytic activities of PKCT toward both phophoenolpyruvate and ADP are profoundly decreased compared to those of wild-type enzyme
additional information
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construction of a C-terminally truncated mutant PKCT with a stop after residue 390. The catalytic activities of PKCT toward both phophoenolpyruvate and ADP are profoundly decreased compared to those of wild-type enzyme
additional information
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construction of a C-terminally truncated mutant PKCT with a stop after residue 390. The catalytic activities of PKCT toward both phophoenolpyruvate and ADP are profoundly decreased compared to those of wild-type enzyme
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additional information
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overexpression of pyruvate kinase resulting in about fivefold increase in enzymic activity does not affect the growth rate or formate-to-lactate ratio significantly. Disruption of the gene encoding catabolite-control protein A results in a decrease in pyruvate kinase mRNA level
additional information
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recombinant overexpression of the enzyme in Clostridium thermocellum improves carbon flux to ethanol in the transformed cells. Clostridium thermocellum strain YD01 with exogenous pyruvate kinase, in which phosphoenolpyruvate carboxykinase expression is diminished by modifying the start codon from ATG to GTG, exhibits 3.25fold higher ethanol yield than the wild-type Clostridium thermocellum strain. A second strain, YD02 with exogenous pyruvate kinase, in which the gene for malic enzyme and part of malate dehydrogenase are deleted, has over 3fold higher ethanol yield than the wild-type strain
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