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ADP + beta-D-fructose 2,6-bisphosphate
ATP + beta-D-fructose 6-phosphate
-
reverse reaction, at 50% the rate of forward reaction
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
ATP + D-fructose 6-phosphate
ADP + D-fructose 2,6-bisphosphate
-
-
-
?
ATP + D-psicose 6-phosphate
?
-
-
-
?
ATP + D-tagatose 6-phosphate
?
-
-
-
?
ATP + L-sorbose 6-phosphate
?
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
GTP + beta-D-fructose 6-phosphate
GDP + beta-D-fructose 2,6-bisphosphate
ITP + beta-D-fructose 6-phosphate
IDP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
MgATP2- + beta-D-fructose 6-phosphate
?
UTP + D-fructose 6-phosphate
UDP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
additional information
?
-
ATP + beta-D-fructose 6-phosphate

ADP + beta-D-fructose 2,6-bisphosphate
-
carbon-partitioning in Arabidopsis is regulated by fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?, r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
activity determined spectrophotometrically by coupling the fructose-1,6-bisphosphate production to the oxidation of NADH
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
regulation of glycolysis
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
the inducible enzyme is an important regulator of glycolysis that may be responsible for sustaining the high glycolytic flux of rapidly proliferating leukemia cells
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
bifunctional enzyme catalyzes the forward and reverse reaction using different catalytic sites
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways even under severe hypoxic conditions
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli, role in the progression of cancerous cells, antiproliferative effects during inhibitor incubation determined
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
transgene causes changes in cardiac metabolite concentrations, increased glycolysis, reduced palmitate oxidation, protection from hypoxia
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
transfers gamma-phosphoryl group of ATP to hydroxyl group at C-2 of fructose 6-phosphate
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
transfers gamma-phosphoryl group of ATP to hydroxyl group at C-2 of fructose 6-phosphate
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
no substrates are diphosphate, glucose 6-phosphate
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
sugar phosphate specificity
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
not: ribose 5-phosphate
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
not: ribose 5-phosphate
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
not: 1-O-methyl-D-fructose 6-phosphate, alpha-/beta-methyl-D-fructofuranoside 6-phosphate, 2,5-anhydro-D-mannitol 6-phosphate, D-arabinose 5-phosphate
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an important role in the regulation of hepatic carbohydrate metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
bifunctional enzyme catalyzes the forward and reverse reaction using different catalytic sites
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
site-directed mutant study and inhibition kinetics suggest that the reaction will be catalyzed most efficiently by the protein when the substrates bind to the active pocket in an ordered manner in which ATP binds first
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
phosphorylation of PFK-2 on Ser-32, inhibition of hepatic glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?, r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an important role in the regulation of hepatic carbohydrate metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
bifunctional enzyme catalyzes the forward and reverse reaction using different catalytic sites
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
GTP + beta-D-fructose 6-phosphate

GDP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
GTP + beta-D-fructose 6-phosphate
GDP + beta-D-fructose 2,6-bisphosphate
-
less effective than ATP
-
?
MgATP2- + beta-D-fructose 6-phosphate

?
-
-
-
?
MgATP2- + beta-D-fructose 6-phosphate
?
-
-
-
?
MgATP2- + beta-D-fructose 6-phosphate
?
-
-
-
?
MgATP2- + beta-D-fructose 6-phosphate
?
-
analysis of MgATP-induced tetramer formation
-
?
MgATP2- + beta-D-fructose 6-phosphate
?
-
-
-
?
MgATP2- + beta-D-fructose 6-phosphate
?
-
-
-
?
MgATP2- + beta-D-fructose 6-phosphate
?
-
-
-
?
additional information

?
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
with discrete catalytic sites
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
with discrete catalytic sites
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
Cys-295 is involved in allosteric regulation
-
?
additional information
?
-
-
mechanism of enzyme inhibition by ATP analyzed by structure determination
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
the bifunctional enzyme catalyzes the synthesis, 6-phosphofructo-2-kinase, and hydrolysis, fructose-2,6-bisphosphatase, of beta-D-fructose 2,6-bisphosphate, an activator of glycolysis and an inhibitor of gluconeogenesis
-
?
additional information
?
-
-
it is unlikely that protein kinase Czeta is required for activation of 6-phosphofructo-2-kinase by insulin in heart
-
?
additional information
?
-
-
PFKFB3 is activated by mitogenic inflammatory and hypoxic stimuli. PFKFB4 controls glycolytic flux to lactate and the nonoxidatibe pentose shunt, and is selectively required for the tumorigenic growth of ras-transformed cells
-
?
additional information
?
-
-
the expression of the inducible PFK2/FBPase is selectively necessary for the control of glycolytic flux in cells transformed with ras
-
?
additional information
?
-
expression analysis in different tumor specimens with high and low malignity grades, high expression of the PFKFB3 protein as an explanation for high glycolytic flux and lactate production in these tumors
-
?
additional information
?
-
expression analysis in different tumor specimens with high and low malignity grades, high expression of the PFKFB3 protein as an explanation for high glycolytic flux and lactate production in these tumors
-
?
additional information
?
-
expression analysis in different tumor specimens with high and low malignity grades, high expression of the PFKFB3 protein as an explanation for high glycolytic flux and lactate production in these tumors
-
?
additional information
?
-
expression analysis in different tumor specimens with high and low malignity grades, high expression of the PFKFB3 protein as an explanation for high glycolytic flux and lactate production in these tumors
-
?
additional information
?
-
recombinant human PFKFB4 kinase activity is 4.3-fold greater than its phosphatase activity
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
the expression of the inducible PFK2/FBPase is selectively necessary for the control of glycolytic flux in cells transformed with ras
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
isotope exchange reaction between ATP and ADP in the absence of fructose 6-phosphate
-
?
additional information
?
-
-
isotope exchange reaction between ATP and ADP in the absence of fructose 6-phosphate
-
?
additional information
?
-
-
with discrete catalytic sites
-
?
additional information
?
-
-
with discrete catalytic sites
-
?
additional information
?
-
-
with discrete catalytic sites
-
?
additional information
?
-
-
allosteric bifunctional enzyme, not heart
-
?
additional information
?
-
-
isotope exchange between fructose 6-phosphate and fructose 2,6-bisphosphate in the absence of adenine nucleotides
-
?
additional information
?
-
-
role of the enzyme in catalysis and regulation of glycolysis/gluconeogenesis and related enzymes, overview
-
?
additional information
?
-
-
coordinate roles for glucokinase and PFK2 in the elevated hepatic glycolysis in fa/fa rats
-
?
additional information
?
-
the enzyme binds to glucokinase in the cytoplasm
-
?
additional information
?
-
the enzyme binds to glucokinase in the cytoplasm
-
?
additional information
?
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
?
additional information
?
-
-
sterol regulatory element binding protein-1a binds to a sterol regulatory element box and transcriptionally activates Sparus aurata liver PFKFB1
-
?
additional information
?
-
evolution of the bifunctional enzyme
-
?
additional information
?
-
evolution of the bifunctional enzyme
-
?
additional information
?
-
-
evolution of the bifunctional enzyme
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
additional information
?
-
ATP + beta-D-fructose 6-phosphate

ADP + beta-D-fructose 2,6-bisphosphate
-
carbon-partitioning in Arabidopsis is regulated by fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
regulation of glycolysis
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
the inducible enzyme is an important regulator of glycolysis that may be responsible for sustaining the high glycolytic flux of rapidly proliferating leukemia cells
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways even under severe hypoxic conditions
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an important role in the regulation of hepatic carbohydrate metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
enzyme plays an important role in the regulation of hepatic carbohydrate metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
additional information

?
-
-
Cys-295 is involved in allosteric regulation
-
-
?
additional information
?
-
the bifunctional enzyme catalyzes the synthesis, 6-phosphofructo-2-kinase, and hydrolysis, fructose-2,6-bisphosphatase, of beta-D-fructose 2,6-bisphosphate, an activator of glycolysis and an inhibitor of gluconeogenesis
-
-
?
additional information
?
-
-
it is unlikely that protein kinase Czeta is required for activation of 6-phosphofructo-2-kinase by insulin in heart
-
-
?
additional information
?
-
-
PFKFB3 is activated by mitogenic inflammatory and hypoxic stimuli. PFKFB4 controls glycolytic flux to lactate and the nonoxidatibe pentose shunt, and is selectively required for the tumorigenic growth of ras-transformed cells
-
-
?
additional information
?
-
-
the expression of the inducible PFK2/FBPase is selectively necessary for the control of glycolytic flux in cells transformed with ras
-
-
?
additional information
?
-
-
the expression of the inducible PFK2/FBPase is selectively necessary for the control of glycolytic flux in cells transformed with ras
-
-
?
additional information
?
-
-
role of the enzyme in catalysis and regulation of glycolysis/gluconeogenesis and related enzymes, overview
-
-
?
additional information
?
-
-
coordinate roles for glucokinase and PFK2 in the elevated hepatic glycolysis in fa/fa rats
-
-
?
additional information
?
-
the enzyme binds to glucokinase in the cytoplasm
-
-
?
additional information
?
-
the enzyme binds to glucokinase in the cytoplasm
-
-
?
additional information
?
-
-
sterol regulatory element binding protein-1a binds to a sterol regulatory element box and transcriptionally activates Sparus aurata liver PFKFB1
-
-
?
additional information
?
-
evolution of the bifunctional enzyme
-
-
?
additional information
?
-
evolution of the bifunctional enzyme
-
-
?
additional information
?
-
-
evolution of the bifunctional enzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2E)-1-(pyridin-4-yl)-3-(quinolin-2-yl)prop-2-en-1-one
-
(2E)-3-(pyridin-3-yl)-1-(pyridin-4-yl)prop-2-en-1-one
-
1-(3-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
-
1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
2,5-anhydro-D-mannitol 6-phosphate
-
-
2-((5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)amino)acetamide
-
2-(2-bromoacetamido)ethyl phosphate
an irreversible inhibitor of PFK-2 in several cancer cell lines
2-(5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)-1,2,3,4-tetrahydroisoquinoline-5-carbonitrile
-
2-hydroxy-4-[(naphthalen-1-ylsulfonyl)amino]benzoic acid
-
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
3H-benzo[e]indol-2-yl(pyridin-4-yl)methanone
-
4-(4-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-5-bromo-6-oxopyridazin-1(6H)-yl)benzonitrile
-
4-bromo-2-phenyl-5-(((tetrahydrofuran-2-yl)methyl)amino)pyridazin-3(2H)-one
-
4-bromo-2-phenyl-5-(2-oxa-6-azaspiro[3.3]heptan-6-yl)pyridazin-3(2H)-one
-
4-bromo-5-morpholino-2-phenylpyridazin-3(2H)-one
-
5,6,7,8-tetrahydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzyl-4-bromopyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzylpyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(3-phenylpropyl)pyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-((2-(dimethylamino)ethyl)-amino)benzyl)pyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-(trifluoromethoxy)phenyl)-pyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-chlorophenyl)pyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-iodobenzyl)pyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(pyrimidin-5-yl)pyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenethylpyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenylpyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-chloro-2-phenylpyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-ethoxy-2-phenylpyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-iodo-2-phenylpyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-isopropyl-2-phenylpyridazin-3(2H)-one
-
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
AICAR, associated with phosphorylation of PFK-2 on Ser-32, phosphorylation increased of both wild-type and overexpressed PFK-2 protein in hepatocytes
7,8-dihydroxy-3-(4-hydroxyphenyl)-4H-chromen-4-one
-
beta-D-fructose 2,6-bisphosphate
beta-D-fructose 6-phosphate
modeling of beta-D-fructose 6-phosphate as inhibitor
dibutyryl cAMP
slightly inhibits the complex formation between the enzyme and glucokinase
dihydroxyacetone phosphate
ethyl 1-(6-oxo-1-phenyl-5-(2-oxa-6-azaspiro[3.3]heptan-6-yl)-1,6-dihydropyridazin-4-yl)-1H-1,2,3-triazole-4-carboxylate
-
glycerol 3-phosphate
20% inhibition at 2mM
glycolate 2-phosphate
-
-
guanidine
-
inactivation, unfolding
m-periodate
-
strong, DTT protects or reverses
MgATP
-
inhibited by, structure determination reveals substrate inhibition due to sequential binding of two MgATP molecules per subunit, the first at the usual site occupied by the nucleotide in homologous enzymes and the second at the allosteric site, making a number of direct and Mg-mediated interactions with the first, two configurations observed for the second MgATP, one of which involves interactions with Tyr-23 from the adjacent subunit in the dimer and the other making an unusual non-Watson-Crick base pairing with the adenine in the substrate ATP
MgNTP
-
strain DF903, substrate inhibition, most effective: MgATP2, at low fructose concentration
N-(1-pyrenil)maleimide
-
complete loss of catalytic activity, but modified enzyme is able to bind beta-D-fructose 6-phosphate, the presence of MgATP2- completely protects the enzyme activity, the modified enzyme elutes as a monomer
N-bromoacetylethanolamine
o-phthalaldehyde
-
kinetics, DTT or substrates do not protect
phosphate
-
inhibits wild-type and mutant enzym E190Q. E190 contributs to the mechanism of phosphate inhibition in Pfk-2. E190Q mutant presents alterations in the inhibition by MgATP2- and phosphate
protein kinase A
inactivation via a 7fold increase in Km for fructose 6-phosphate without alteration of Vmax
-
pyrene maleimide
-
incorporation of 2 mol per mol of enzyme subunit, modifiying Cys-238 and Cys-295, leads to rapid inactivation, MgATP2- protects Cys295, modification of Cys238 does not abolish activity
1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one

the inhibitor causes a rapid induction of apoptosis in transformed cells, has adequate pharmacokinetic properties, suppresses the glucose uptake and growth of Lewis lung carcinomas in syngeneic mice and yields anti-tumor effects in three human xenograft models of cancer in athymic mice that are comparable to FDA-approved chemotherapeutic agents
1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
-
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one

(3PO), small-molecule inhibitor, mixed inhibition mechanism, both competitive and uncompetitive inhibition, suppresses glycolytic flux and is cytostatic to neoplastic cells, inhibits activity of recombinantly expressed PFKFB3
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
the PFKFB3 inhibitor, 3PO, increases p27 protein in Lewis lung carcinoma cells in vitro and in vivo
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
3PO, a weak competitive inhibitor of PFKFB3, reduces the glucose metabolism and proliferation of cancer cells
ADP

-
AMP

not
ATP

not
ATP
-
at low concentrations of Mg2+ and fructose 6-phosphate
beta-D-fructose 2,6-bisphosphate

-
product inhibition
beta-D-fructose 2,6-bisphosphate
-
kinetics
beta-D-fructose 2,6-bisphosphate
-
-
citrate

-
weak
citrate
-
heart enzyme is more sensitive than liver enzyme
citrate
-
at physiological concentrations
citrate
-
skeletal muscle enzyme is more sensitive than liver enzyme
citrate
-
heart enzyme is more sensitive than liver enzyme
citrate
-
skeletal muscle enzyme is more sensitive than liver enzyme
citrate
-
phosphorylation enhances sensitivity
citrate
60% inhibition at 1 mM
dihydroxyacetone phosphate

-
dihydroxyacetone phosphate
-
weak
dihydroxyacetone phosphate
-
diphosphate

not phosphate
diphosphate
-
not phosphate
diphosphate
-
not phosphate
diphosphate
not phosphate
glucagon

-
the native and the recombinant wild-type and mutant enzymes are phosphorylated after incubation with glucagon inactivating the enzyme
glucagon
phosphorylation of PFK2 on Ser-32 in liver
glycerate 2-phosphate

-
glycerate 2-phosphate
-
-
MgATP2-

-
allosteric inhibition, important regulation of in vivo carbohydrate metabolism under gluconeogenic conditions
MgATP2-
-
E190Q mutant presents alterations in the inhibition by MgATP2- and phosphate
MgATP2-
-
allosteric inhibition
N-bromoacetylethanolamine

-
repetitive administration affects inhibition of glycolysis and lipid metabolism, causing suppression of body weight gain
N-bromoacetylethanolamine
-
specific active site-directed inactivator of enzyme, in vitro and in vivo
phosphoenolpyruvate

-
phosphoenolpyruvate
-
weak
phosphoenolpyruvate
-
not
phosphoenolpyruvate
HBP1 and HBP2, the bifunctional enzyme is regulated via inhibition by phosphoenolpyruvate, uncompetitive against ATP, noncompetitive against beta-D-fructose 6-phosphate
phosphoenolpyruvate
-
strong
phosphoenolpyruvate
-
kinetics
phosphoenolpyruvate
-
mixed-type inhibitory effect, phosphorylation enhances sensitivity
sn-glycerol 3-phosphate

-
sn-glycerol 3-phosphate
-
heart enzyme is less sensitive than liver
sn-glycerol 3-phosphate
-
i.e. alpha-glycerol phosphate
sn-glycerol 3-phosphate
-
not
sn-glycerol 3-phosphate
-
heart enzyme is less sensitive than liver
sn-glycerol 3-phosphate
-
not
sn-glycerol 3-phosphate
-
-
sn-glycerol 3-phosphate
-
stimulates phosphatase activity
sn-glycerol 3-phosphate
-
heart enzyme is less sensitive than liver
sn-glycerol 3-phosphate
-
-
sn-glycerol 3-phosphate
-
heart enzyme is less sensitive than liver; liver enzyme
sn-glycerol 3-phosphate
-
75% decrease in activity of liver enzyme but not hepatoma cells
sn-glycerol 3-phosphate
-
most potent inhibitor of phosphorylated liver enzyme, phosphorylation enhances sensitivity
sn-glycerol 3-phosphate
-
most potent inhibitor of phosphorylated liver enzyme, phosphorylation enhances sensitivity; skeletal muscle enzyme is not sensitive to inhibition
sn-glycerol 3-phosphate
-
-
sn-glycerol 3-phosphate
-
additional information

-
no inhibition by protein kinase C; phosphorylation by cAMP-dependent protein kinase, but no inhibition
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase, but not rat skeletal muscle, bovine and rat heart enzyme
-
additional information
-
no inhibition by protein kinase C; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase but not rat kidney, testis and skeletal muscle enzyme and bovine and rat heart enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
-
-
additional information
-
no inhibition by protein kinase C; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
not: ITP, GTP, UTP, CTP, strain DF905; phosphorylation by cAMP-dependent protein kinase causes inactivation
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
phosphorylation site: Ser-32
-
additional information
enzyme structure-activity relationships, screening of a small-molecule library, and design and synthesis of 5-triazolo-2-arylpyridazinone analogus inhibitors, molecular docking using the X-ray structure for human PFKFB3, PDB ID 2AXN, overview
-
additional information
synthesis and screening of 3PO inhibitor derivatives for inhibitory potency against isozyme PFKFB3, overview. 1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one displays improved pharmacokinetic properties relative to 3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
additional information
-
synthesis and screening of 3PO inhibitor derivatives for inhibitory potency against isozyme PFKFB3, overview. 1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one displays improved pharmacokinetic properties relative to 3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
additional information
-
no inhibition by phosphorylation with Ca2+/calmodulin dependent protein kinase; no inhibition by protein kinase C
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation at lower pH-values; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation site: Ser-32
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; phosphorylation of foetal liver enzyme by protein kinase C, but no effect on adult liver cells
-
additional information
-
not: cAMP or protein kinase alone; phosphorylation at pH 6.6, not at pH 8; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; phosphorylation by cAMP-dependent protein kinase of liver enzyme, not of skeletal muscle enzyme, since the phosphorylation site target Ser-32 of the liver isozyme is replaced by Ala in the muscle isozyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase, but not rat skeletal muscle, bovine and rat heart enzyme
-
additional information
-
no inhibition by protein kinase C; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase but not rat kidney, testis and skeletal muscle enzyme and bovine and rat heart enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not of heart and skeletal muscle enzyme
-
additional information
-
loss of phosphorylation-dependent reduction of enzyme by deletion of the N-terminal residues of enzyme. The deletion of 7 N-terminal amino acids causes a 75% decrease in activity; phosphorylation site: Ser-32
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes 35% inactivation of isozyme L of adipose tissue, not isozyme M
-
additional information
-
kinetic of phosphorylation by cAMP-dependent protein kinase
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes 80% decrease in activity of the liver cells but not of hepatoma cells; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not of kidney, testis and heart enzyme
-
additional information
-
the islet enzyme lacks protein kinase A and C phosphorylation sites
-
additional information
-
phosphorylation by cAMP-dependent protein kinase, but no inhibition
-
additional information
-
no inhibition by lactate, glyceraldehyde 3-phosphate, beta-D-fructose 1,6-bisphosphate
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not skeletal muscle enzyme
-
additional information
-
-
-
additional information
-
-
-
additional information
enzyme is not affected by protein kinase C
-
additional information
enzyme is not affected by protein kinase C
-
additional information
-
enzyme is not affected by protein kinase C
-
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0.02 - 0.21
beta-D-fructose 2,6-bisphosphate
0.0038 - 39
beta-D-fructose 6-phosphate
0.0094 - 0.1
D-fructose 6-phosphate
7.4
D-psicose 6-phosphate
-
pH 7.5, 30°C
15
D-tagatose 6-phosphate
-
pH 7.5, 30°C
0.3
ITP
-
pH 8.2, 30°C, strain DF903
0.175
L-Sorbose 6-phosphate
-
pH 7.5, 30°C
additional information
additional information
-
0.00087
ATP

-
mutant enzyme A44G
0.0169
ATP
-
wild-type enzyme
0.018
ATP
-
pH 7.5, 30°C, in presence of phosphate
0.048
ATP
-
pH 7.5, 25°C, heart
0.048
ATP
-
pH 7.5, 30°C, comparison of Km of skeletal muscle and liver enzyme
0.061
ATP
-
pH 7.5, 30°C, liver
0.083
ATP
-
pH 7.5, 25°C, heart
0.1
ATP
-
pH 7.5, 25°C, testis
0.1
ATP
-
pH 7.5, 30°C, MgATP
0.1
ATP
-
pH 7.5, 30°C, MgATP
0.1
ATP
-
pH 7.5, 30°C, in absence of phosphate
0.1
ATP
-
pH 7.5, 30°C, testis
0.12 - 0.36
ATP
-
pH 7.5, 30°C, kinetic study
0.12 - 0.36
ATP
-
pH 7.5, 30°C, kinetic study
0.12 - 0.36
ATP
-
pH 8.2, 30°C, strain DF905
0.14
ATP
-
mutant enzyme A44V
0.19
ATP
-
pH 8.5, 30°C, foetal enzyme
0.195
ATP
-
pH 8.5, 30°C, adult enzyme
0.223
ATP
-
pH 7.4, 30°C, presence of phosphate
0.226
ATP
-
pH 7.5, 30°C, absence of phosphate
0.29 - 0.38
ATP
-
pH 7.1, 30°C, kinetic data of various enzyme forms
0.31
ATP
-
pH 7.5, 25°C, liver
0.328
ATP
-
pH 7.5, 25°C, islet
0.5
ATP
-
pH 8.0, three forms
0.7
ATP
-
pH 7.5, 30°C, isozyme I
1.32
ATP
pH 7.8, 25°C, effect of phosphate on Km
1.62
ATP
pH 7.1, 30°C, recombinant isozyme Tb1
0.02
beta-D-fructose 2,6-bisphosphate

-
pH 7.5, 30°C
0.21
beta-D-fructose 2,6-bisphosphate
-
pH 7.4, 30°C, in presence of phosphate
0.0038
beta-D-fructose 6-phosphate

-
mutant enzyme A44G
0.006
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C and heating at 90°C for 10 min, with ATP, in presence of phosphate
0.0064
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, HBP1 mutant S477D
0.0066
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, HBP1 mutants T470D and S460D/T470D
0.0067
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, HBP1 mutant S460D
0.0071
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, HBP1 mutant H253A/S460D
0.0071
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, wild-type HBP1
0.0073
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, HBP1 mutant H253A
0.0074
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, His-tagged wild-type HBP2
0.008
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, His-tagged wild-type HBP1
0.0092
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant Hnon-phosphorylated, is-tagged HBP1 deletion mutant
0.0095
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, His-tagged HBP1 mutant S302R
0.0102
beta-D-fructose 6-phosphate
-
wild-type enzyme
0.013
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged chimeric mutant enzyme, phosphorylated or nonphosphorylated
0.016
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, kinetic study
0.016
beta-D-fructose 6-phosphate
-
pH 7.5, 25°C, liver
0.017
beta-D-fructose 6-phosphate
-
pH 7.5, 25°C, islet
0.019 - 0.021
beta-D-fructose 6-phosphate
-
pH 7.8, in presence of phosphate
0.019 - 0.021
beta-D-fructose 6-phosphate
-
pH 7.8, in presence of phosphate
0.02
beta-D-fructose 6-phosphate
-
C-terminal deletion mutant D299, 1 mM co-substrate
0.02 - 0.03
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, in presence of phosphate
0.02 - 0.03
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, in presence of phosphate
0.022
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
0.023
beta-D-fructose 6-phosphate
-
pH 7.5, 25°C, heart
0.023
beta-D-fructose 6-phosphate
-
comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
0.023
beta-D-fructose 6-phosphate
-
comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
0.025
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, liver, comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
0.027
beta-D-fructose 6-phosphate
-
pH 7.1, 30°C
0.029
beta-D-fructose 6-phosphate
-
L307A, C-terminal point mutant, 1 mM co-substrate
0.031
beta-D-fructose 6-phosphate
-
recombinant wild-type enzyme and mutant C238A
0.032
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C
0.035
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C
0.036
beta-D-fructose 6-phosphate
-
C-terminal deletion mutant A305, 1 mM co-substrate
0.04
beta-D-fructose 6-phosphate
-
pH 7.5, 25°C, testis
0.04
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, wild-type enzyme, testis
0.044
beta-D-fructose 6-phosphate
-
pH 8.5, 30°C, foetal liver enzyme
0.047
beta-D-fructose 6-phosphate
-
pH 8.5, 30°C, adult liver enzyme
0.047
beta-D-fructose 6-phosphate
-
recombinant mutant C238F
0.05
beta-D-fructose 6-phosphate
-
-
0.05
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C
0.05
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, with ATP, in presence of phosphate
0.05
beta-D-fructose 6-phosphate
-
pH 7.1, 30°C, MgATP2-, phosphorylated chicken enzyme
0.056
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, comparison of Km of skeletal muscle and liver enzyme
0.056
beta-D-fructose 6-phosphate
-
pH 7.5, 25°C, muscle
0.057
beta-D-fructose 6-phosphate
-
wild-type, 1 mM co-substrate, chosen in order avoid the effect of MgATP binding at the allosteric site to the binding of fructose-6-P to the catalytic site, that is observed above 1 mM MgATP
0.058
beta-D-fructose 6-phosphate
-
native enzyme
0.06
beta-D-fructose 6-phosphate
-
C-terminal deletion mutant L307, 1 mM co-substrate
0.062
beta-D-fructose 6-phosphate
-
Y306A, C-terminal point mutant, 1 mM co-substrate
0.063
beta-D-fructose 6-phosphate
-
C238-pyrene maleimide modified enzyme
0.07
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C
0.081
beta-D-fructose 6-phosphate
-
recombinant mutant C295F
0.088
beta-D-fructose 6-phosphate
-
recombinant mutant C295A
0.09
beta-D-fructose 6-phosphate
-
pH 6.6, 25°C
0.097
beta-D-fructose 6-phosphate
-
0.1
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C
0.1
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C
0.12
beta-D-fructose 6-phosphate
-
pH 7.8
0.14
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C
0.156
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, with ATP, in presence of phosphate
0.204
beta-D-fructose 6-phosphate
-
mutant enzyme A44V
0.33 - 0.4
beta-D-fructose 6-phosphate
-
pH 7.1, 30°C, kinetic data of various enzyme forms
0.37
beta-D-fructose 6-phosphate
-
-
0.4
beta-D-fructose 6-phosphate
-
pH 7.1, 37°C
0.5
beta-D-fructose 6-phosphate
pH 6.0, 25°C
0.5
beta-D-fructose 6-phosphate
-
pH 7.5, 22°C
0.5 - 1
beta-D-fructose 6-phosphate
-
pH 8.0, forms 1-3, kinetic data of various enzyme forms
0.6
beta-D-fructose 6-phosphate
-
-
0.94
beta-D-fructose 6-phosphate
-
pH 7.4, 30°C, presence of phosphate
1 - 1.1
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, in absence of phosphate
1 - 1.1
beta-D-fructose 6-phosphate
-
pH 7.8, absence of phosphate
1 - 1.1
beta-D-fructose 6-phosphate
-
pH 7.8, absence of phosphate
1 - 1.1
beta-D-fructose 6-phosphate
-
pH 8.2, 30°C, ITP, strain DF905
1.4
beta-D-fructose 6-phosphate
pH 7.8, 25°C, effect of phosphate on Km
1.4
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, with ATP, absence of phosphate
1.9 - 4.6
beta-D-fructose 6-phosphate
pH 7.1, 30°C, recombinant isozyme Tb1
5.8
beta-D-fructose 6-phosphate
pH 7.1, 30°C
39
beta-D-fructose 6-phosphate
pH 7.1, 30°C, protein kinase A treated enzyme
0.9
CTP

-
pH 8.2, 30°C, strain DF903
2
CTP
-
pH 8.2, 30°C, strain DF905
0.0094
D-fructose 6-phosphate

-
mutant enzyme E190Q, 30 mM Mg2+
0.01
D-fructose 6-phosphate
-
mutant enzyme E190Q, 1 mM Mg2+
0.028
D-fructose 6-phosphate
-
wild-type enzyme, 30 mM Mg2+
0.1
D-fructose 6-phosphate
-
wild-type enzyme, 1 mM Mg2+
0.35
GTP

-
pH 8.2, 30°C, strain DF903
1.5
GTP
-
pH 8.2, 30°C, strain DF905
0.0072
MgATP2-

-
pH 7.1, 30°C, phosphorylated enzyme
0.0095 - 0.012
MgATP2-
-
pH 7.5, 30°C
0.0095 - 0.012
MgATP2-
-
pH 7.1, 30°C, native pigeon enzyme
0.01
MgATP2-
-
C-terminal deletion mutant L307, 1 mM co-substrate
0.0107
MgATP2-
-
recombinant mutant C295F
0.0137
MgATP2-
-
Y306A, C-terminal point mutant, 1 mM co-substrate
0.015
MgATP2-
-
wild-type, 1 mM co-substrate
0.017
MgATP2-
-
recombinant wild-type enzyme and mutant C238A
0.02
MgATP2-
-
wild-type enzyme, 1 mM Mg2+
0.021
MgATP2-
-
recombinant mutant C238F
0.022
MgATP2-
-
wild-type enzyme, 30 mM Mg2+
0.042
MgATP2-
-
native enzyme
0.044
MgATP2-
-
C238-pyrene maleimide modified enzyme
0.061
MgATP2-
-
recombinant mutant C295A
0.149
MgATP2-
-
mutant enzyme E190Q, 1 mM Mg2+
0.29
MgATP2-
-
pH 7.1, 30°C, native chicken enzyme
0.32
MgATP2-
-
mutant enzyme E190Q, 30 mM Mg2+
0.5
MgATP2-
-
pH 7.5, 30°C
0.5
MgATP2-
-
pH 7.5, 30°C
0.8
MgATP2-
-
C-terminal deletion mutant A305, 1 mM co-substrate
0.88
MgATP2-
-
C-terminal deletion mutant Y306, 1 mM co-substrate
0.954
MgATP2-
-
L307A, C-terminal point mutant, 1 mM co-substrate
2
MgATP2-
-
C-terminal deletion mutant D299, 1 mM co-substrate
0.78
UTP

-
pH 8.2, 30°C, strain DF903
2.3
UTP
-
pH 8.2, 30°C, strain DF905
additional information
additional information

-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
-
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
-
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
-
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
comparison of Km of hepatoma cells and liver enzyme
-
additional information
additional information
-
kinetics of native and pyrene maleimide modified enzyme
-
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes
-
additional information
additional information
recombinant wild-type and mutant enzymes, Km for phosphorylated wild-type enzyme and mutants with beta-D-fructose 6-phosphate and beta-D-fructose 2,6-bisphosphate, kinetics, modeling
-
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