Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
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
-
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
Q75IQ9
-
-
-
?
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
-
-
-
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
-
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
Q75IQ9
-
-
-
?
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
-
5,6,7,8-tetrahydroxy-2-(4-hydroxyphenyl)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-(N-(8-methoxy-4-quinolyl)amino)pentyl nitrate
-
-
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-1-benzopyran-4-one
-
-
7,8-dihydroxy-3-(4-hydroxyphenyl)-4H-chromen-4-one
-
AZ67
potent and specific PFKFB3 inhibitor
-
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
-
ethyl 7-hydroxy-2-oxo-2H-1-benzopyran-3-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
N-bromoacetylethanolamine phosphate
-
o-phthalaldehyde
-
kinetics, DTT or substrates do not protect
PFK-15
i.e. 1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
-
PFK-158
potent and specific inhibitor
-
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-(3-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
-
1-(3-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
-
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
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
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
not inhibited by up to 0.75 mM 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
-
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.
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
-
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.
0.026
(2E)-3-(pyridin-3-yl)-1-(pyridin-4-yl)prop-2-en-1-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
1
2-((5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)amino)acetamide
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.5
2-(5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)-1,2,3,4-tetrahydroisoquinoline-5-carbonitrile
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.027
2-hydroxy-4-[(naphthalen-1-ylsulfonyl)amino]benzoic acid
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
1
3H-benzo[e]indol-2-yl(pyridin-4-yl)methanone
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0084
4-(4-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-5-bromo-6-oxopyridazin-1(6H)-yl)benzonitrile
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
1
4-bromo-2-phenyl-5-(((tetrahydrofuran-2-yl)methyl)amino)pyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
1
4-bromo-2-phenyl-5-(2-oxa-6-azaspiro[3.3]heptan-6-yl)pyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
1
4-bromo-5-morpholino-2-phenylpyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0034
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzyl-4-bromopyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
10
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzylpyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.011
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(3-phenylpropyl)pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.5
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
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0091
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-(trifluoromethoxy)phenyl)-pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.007
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-chlorophenyl)pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0087
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-iodobenzyl)pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0096
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(pyrimidin-5-yl)pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0026
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenethylpyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0074
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenylpyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.026
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-chloro-2-phenylpyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
1
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-ethoxy-2-phenylpyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.013
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-iodo-2-phenylpyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.5
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-isopropyl-2-phenylpyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.055
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
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged 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.
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.
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.
evolution
Pfkfb (6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase) enzymes are bi-functional enzymes encoded by four different genes (pfkfb1, pfkfb2, pfkfb3, pfkfb4) in vertebrates, phylogenetic analysis of Pfkfb enzymes in vertebrates, overview
malfunction
PFKFB3 enzymes are activated in human cancers
malfunction
Akt inactivation blocks PFKFB2 phosphorylation and fructose 2,6-bisphosphate production
malfunction
Akt inactivation blocks PFKFB2 phosphorylation and fructose 2,6-bisphosphate production
malfunction
knockdown of PFKFB3/iPFK2 in N-43/5 neurons causes a decrease in rates of glycolysis, which is accompanied by increased AMPK phosphorylation, increased AgRP mRNA levels and decreased CART mRNA levels. Overexpression of PFKFB3/iPFK2 in N-43/5 neurons causes an increase in glycolysis, which is accompanied by decreased AMPK phosphorylation and decreased AgRP mRNA levels and increased CART mRNA levels
malfunction
knockdown of PFKFB4 in prostate cancer cells increases p62 and reactive oxygen species, but surprisingly increases autophagic flux. Addition of the reactive oxygen species scavenger N-acetyl cysteine prevents p62 accumulation in PFKFB4-depleted cells. PFKFB4 depletion acts upstream of ATG7 consistent with increased oxidative stress that induces autophagy and p62 upregulation
malfunction
Mb transgenic mice have reduced fructose 2,6-bisphosphate levels, due to cardiac expression of a transgene for a mutant, kinase deficient form of the enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2) which controls the level of fructose 2,6-bisphosphate. Mb hearts are markedly more sensitive to transverse aortic constriction-induced damage showing lower fractional shortening in Mb-TAC mice as well as larger left ventricular end diastolic and end systolic diameters. Cardiac hypertrophy and pulmonary congestion are more severe in Mb-transverse aortic constriction mice, Mb transgene exacerbates transverse aortic constriction-induced increases in cardiac hypertrophy and lung weight, detailed phenotype, overview
malfunction
PFKFB4 inhibition in H-460 cells reduces glycolytic flux to lactate and glutamate. PFKFB4 inhibition in H-460 cells increases apoptosis under normoxic and hypoxic conditions
malfunction
silencing of PFKFB4 results in increased levels of Fru-2,6-P2 in prostate cancer cells, knockdown of PFKFB4 blocks prostate cancer cell growth and remarkably induced regression of prostate tumor xenografts
malfunction
siRNA silencing of endogenous PFKFB3 inhibits Cdk1 activity, which in turn stabilizes p27 protein levels causing cell cycle arrest at G1/S and increased apoptosis in HeLa cells. PFKFB3 inhibition completely suppresses cell proliferation and results in increased early and late apoptotic cells. PFKFB3 inhibition results in increased nuclear and cytoplasmic p27 protein but has no effect on p57 or p21. Blockade of cell cycle progression and stimulation of apoptosis by PFKFB3 inhibition is mediated by p27
malfunction
enzyme knockdown inhibits clonogenic growth and enhances paclitaxel sensitivity in ovarian and breast cancer cell lines with wild type TP53
malfunction
-
mutations in the phosphatase but not in the kinase domain of PFK-2/FBPase-2 alter sexual development and lead to suppression of the respiratory deficient DELTAcox phenotype
malfunction
-
Akt inactivation blocks PFKFB2 phosphorylation and fructose 2,6-bisphosphate production
-
malfunction
-
knockdown of PFKFB3/iPFK2 in N-43/5 neurons causes a decrease in rates of glycolysis, which is accompanied by increased AMPK phosphorylation, increased AgRP mRNA levels and decreased CART mRNA levels. Overexpression of PFKFB3/iPFK2 in N-43/5 neurons causes an increase in glycolysis, which is accompanied by decreased AMPK phosphorylation and decreased AgRP mRNA levels and increased CART mRNA levels
-
metabolism
-
glycolytic enzyme is present as testis-specific isoforms, these isoforms are expressed specifically or predominantly in spermatogenic cells, often during the post-meiotic phase, and replace the ubiquitous isozymes that are also present in somatic cells
metabolism
cancer cells use control of PFKFB3 of the important glycolytic pathway to generate ATP
metabolism
expression level of some PFKFB and PFK1 genes in normoxic and hypoxic conditions in glioma cells is mediated by ERN1 signaling system of endoplasmic reticulum stress. Effect of hypoxia on the expression of genes encoded different 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB1, PFKFB2, PFKFB3 and PFKFB4) and 6-phosphofructo-1-kinase (PFKL, PFKM and PFKP) as well as lactate dehydrogenase in glioma U-87 cells and its subline with suppressed function of ERN1 signaling enzyme, overview
metabolism
expression level of some PFKFB and PFK1 genes in normoxic and hypoxic conditions in glioma cells is mediated by ERN1 signaling system of endoplasmic reticulum stress. Effect of hypoxia on the expression of genes encoded different 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB1, PFKFB2, PFKFB3 and PFKFB4) and 6-phosphofructo-1-kinase (PFKL, PFKM and PFKP) as well as lactate dehydrogenase in glioma U-87 cells and its subline with suppressed function of ERN1 signaling enzyme, overview. Increased expression of PFKFB3 and PFKFB4 under hypoxic conditions correlates with strong induction of PFKL expression in control glioma cells only
metabolism
fructose 2,6-bisphosphate is an important metabolite for the dynamic regulation of glycolytic flux by allosterically activating the rate-limiting enzyme of glycolysis phosphofructokinase-1, fructose 2,6-bisphosphate is a powerful allosteric activator of phosphofructokinase 1, PFK-1
metabolism
glucose causes decreased binding of glucokinase to glucokinase regulatory protein, GKRP, translocation from the nucleus and increased binding to 6-phosphofructo 2-kinase/fructose 2,6 bisphosphatase-2 (PFK2/FBPase2) in the cytoplasm, while glucagon causes dissociation of glucokinase from PFK2/FBPase2, concomitant with phosphorylation of PFK2/FBPase2 on Ser32, uptake of glucokinase into the nucleus and increased interaction with GKRP
metabolism
-
moderate grade hyperammonemia activates lactate dehydrogenase-4 and 6-phosphofructo-2-kinase to support increased lactate turnover in the brain slices
metabolism
re-feeding increases plasma levels of glucose and insulin and stimulates PFKFB3 expression. Glucose and insulin stimulate PFKFB3 expression, increase glycolysis, and decrease AMPK phosphorylation in clonal hypothalamic neurons
metabolism
the family of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatases (PFKFB1-4) comprises well established regulators of glucose metabolism via their synthesis of fructose-2,6 bisphosphate, a potent allosteric activator of 6-phosphofructo-1-kinase. But PFKFB3 and fructose-2,6 bisphosphate function not only as regulators of Pfk-1 but also of Cdk1 activity, and therefore serve to couple glucose metabolism with cell proliferation and survival in transformed cells
metabolism
upregulation of p62 and autophagy is a response to oxidative stress caused by PFKFB4. PFKFB4 is an autophagy regulator
metabolism
enzyme PFKFB3 is an essential target of epidermal growth factor receptor signaling. PFKFB3 activation is required for glycolysis stimulation upon epidermal growth factor receptor activation. PFKFB3 has a key role in mediating glucose metabolism and survival of NSCLC cells in response to epidermal growth factor receptor signaling
metabolism
PFKFB3 has the highest kinase:phosphatase ratio (710:1) to shunt glucose toward glycolysis, whereas PFKFB4 has more fructose-2,6-bisphosphatase-2 activity (kinase:phosphatase ratio of 4.6:1), redirecting glucose toward the pentose phosphate pathway, providing reducing power for lipid biosynthesis and scavenging reactive oxygen species. Co-expression of PFKFB3 and PFKFB4 provides sufficient glucose metabolism to satisfy the bioenergetics demand and redox homeostasis requirements of cancer cells
metabolism
PFKFB3 has the highest kinase:phosphatase ratio (710:1) to shunt glucose toward glycolysis, whereas PFKFB4 has more fructose-2,6-bisphosphatase-2 activity (kinase:phosphatase ratio of 4.6:1), redirecting glucose toward the pentose phosphate pathway, providing reducing power for lipid biosynthesis and scavenging reactive oxygen species. Co-expression of PFKFB3 and PFKFB4 provides sufficient glucose metabolism to satisfy the bioenergetics demand and redox homeostasis requirements of cancer cells. PFKFB4 acts as a protein kinase, regulates steroid receptor coactivator-3 activity and is involved in transcriptional regulation
metabolism
the enzyme binds and activates glucokinase
metabolism
-
re-feeding increases plasma levels of glucose and insulin and stimulates PFKFB3 expression. Glucose and insulin stimulate PFKFB3 expression, increase glycolysis, and decrease AMPK phosphorylation in clonal hypothalamic neurons
-
metabolism
-
glucose causes decreased binding of glucokinase to glucokinase regulatory protein, GKRP, translocation from the nucleus and increased binding to 6-phosphofructo 2-kinase/fructose 2,6 bisphosphatase-2 (PFK2/FBPase2) in the cytoplasm, while glucagon causes dissociation of glucokinase from PFK2/FBPase2, concomitant with phosphorylation of PFK2/FBPase2 on Ser32, uptake of glucokinase into the nucleus and increased interaction with GKRP
-
physiological function
PFKFB3 has a role in nuclear signaling
physiological function
-
spermatogenesis, both PFK-2 isozymes have specific roles in testis metabolism and physiology, PFK-2 isozyme expression switches from the ubiquitous form, required during proliferative phases, to the testicular form, which is the germ cell-specific one
physiological function
-
enzyme acts as an endogenous glucokinase activator. Binding and activation of glucokinase by bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in beta-cells is promoted by glucose, resulting in an enhancement of insulin secretion at stimulatory glucose concentrations, without affecting basal insulin secretion
physiological function
enzyme is required to balance glycolytic activity and antioxidant production to maintain cellular redox balance in prostate cancer cells. Depletion of the enzyme inhibits tumor growth in a xenograft model, indicating that it is required under physiologic nutrient levels. Enzyme mRNA expression is greater in metastatic prostate cancer compared with primary tumors
physiological function
-
is an antagonist of glucokinase inhibition by the competitive glucokinase inhibitor mannoheptulose at increasing glucose concentrations. In combination with chemical activator LY2121260, the enzyme shows additive activation of glucokinase
physiological function
knockdown of isoform PFKFB3/iPFK2 in N-43/5 neurons causes a decrease in rates of glycolysis, which is accompanied by increased AMP-activated protein kinase phosphorylation, increased agouti-related protein mRNA levels and decreased cocaine-amphetamine-related transcript mRNA levels. Overexpression of PFKFB3/iPFK2 in N-43/5 neurons causes an increase in glycolysis, which is accompanied by decreased AMP-activated protein kinase phosphorylation and decreased agouti-related protein mRNA levels and increased cocaine-amphetamine-related transcript mRNA levels
physiological function
enzyme PFKFB3 belongs to the family of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatases (PFKFBs) that controls the conversion of fructose-6-phosphate to and from fructose-2,6-bisphosphate, a key regulator of the glycolytic enzyme phosphofructokinase-1
physiological function
fructose 2,6-bisphosphate is a positive regulator of the glycolytic enzyme phosphofructokinase
physiological function
in human cancers, loss of PTEN, stabilization of HIF-1alpha and activation of Ras and AKT converge to increase the activity of a key regulator of glycolysis, 6-phosphofructo-2-kinase(PFKFB3). This enzyme synthesizes fructose 2,6-bisphosphate, which is an activator of 6-phosphofructo-1-kinase, a key step of glycolysis
physiological function
isozyme PFKFB4 expressed in multiple transformed cells and tumors functions to synthesize fructose 2,6-bisphosphate, PFKFB4 is required for cancer cell survival during the metabolic response to hypoxia, presumably to enable glycolytic production of ATP when the electron transport chain is not fully operational. Isozyme PFKFB4 is overexpressed in human cancers, induced by hypoxia and required for survival and growth of several cancer cell lines
physiological function
PFKFB3 is overexpressed in human cancers, regulated by HIF-1alpha, Akt and PTEN, and required for the survival and growth of multiple cancer types. Role of PFKFB3 in regulating Cdk1- and p27-mediated G1/S blockade and apoptosis
physiological function
possible role of different isozyme PFKFB4 splice variants in cell-specific and/or tissue-specific regulation of glycolysis, role of PFKFB proteins in the control of cancer metabolism. PFKFB4 may be important for cancer cell survival, PFKFB4 plays an essential role in the survival of glioma stem-like cells and of prostate cancer cells. PFKFB4 is known to be a component of the HIF-mediated response to hypoxia, hypoxic induction of PFKFB4 is mediated by a hypoxia response element (HRE) in the promoter region of the PFKFB4 gene
physiological function
role for PFKFB3/iPFK2 in regulating glycolysis in hypothalamic neurons, in the context of neuronal glucose sensing and neuropeptide expression. PFKFB3/iPFK2 responds to re-feeding, which in turn stimulates hypothalamic glycolysis and decreases hypothalamic AMPK phosphorylation and alters neuropeptide expression in a pattern that is associated with suppression of food intake
physiological function
role for phosphofructo 2-kinase/fructose 2,6-bisphosphate (PFK2/FBPase2) as a cytoplasmic binding partner of glucokinase and glucagon-induced uptake of glucokinase to the nucleus
physiological function
role of PFKFB proteins in the control of cancer metabolism
physiological function
role of PFKFB proteins in the control of cancer metabolism. Liver, muscle and fetal isoform variants of PFKFB1 (L-PFK2, M-PFK2 and F-PFK2 respectively) are transcribed from the same gene, but only L-PFK2 contains a serine residue in position 32 of its C-terminal regulatory domain. This is consistent with its specific physiological role as liver cells need to modulate Fru-2,6-P2 levels to facilitate the production of glucose to fulfill the metabolic demand of other tissues. Response to glucagon, cyclic AMP-dependent protein kinase (PKA) phosphorylates Ser32 in the liver isoform of PFKFB1, leads to inactivation of its PFK-2 activity while activating its FBPase-2 function. This decreases glycolytic flux while increasing gluconeogenesis in liver cells While phosphorylation of L-PFK2 results in a decrease in its kinase activity, phosphorylation of H-PFK2 results in an increase in this activity
physiological function
role of PFKFB proteins in the control of cancer metabolism. PFKFB3 is known to be a component of the HIF-mediated response to hypoxia. PFKFB3 is a hypoxia-inducible gene that is stimulated through the interaction of HIF-1alpha with a consensus HRE within its promoter region
physiological function
the enzyme is involved in the regulation of glycolysis, it catalyzes the synthesis and the degradation of beta-D-fructose 2,6-bisphosphate, the most potent allosteric activator of phosphofructokinase 1 (Pfk1), a key glycolytic enzyme. By producing fructose 2,6-bisphosphate, Pfkfb enzymes allow glycolysis to proceed, while by degrading fructose 2,6-bisphosphate they block glycolysis. As major regulators of glycolysis, Pfkfb enzymes are involved in cancer: tumor cells have a higher glycolytic rate compared to normal cells, even in the presence of adequate oxygen levels (Warburg effect) and several cancer cell lines express elevated levels of Pfkfb enzymes
physiological function
-
the PFK2 domain of PFK2/FBPase2 regulates glycolysis to maintain the pyruvate pool for lactate synthesis
physiological function
the putative autophagy stimulator, isozyme PFKFB4, drives flux through pentose phosphate pathway. PFKFB4 suppresses oxidative stress and p62 accumulation, without which autophagy is stimulated likely as a reactive oxygen species detoxification response. Genes whose loss enhanced p62 elimination are putative negative regulators of autophagy and the bi-functional enzyme PFKFB4 highly inhibits p62 elimination. PFKFB4 is an autophagy regulator. PFKFB4 suppresses autophagy and p62 accumulation by mitigating reactive oxygen species
physiological function
both a PFKFB3 inhibitor or PFKFB3 silencing by siRNA suppress the basal and the H2O2-induced autophagy concomitantly with the inhibition of AMPK activity. Overexpression of wild-type PFKFB3 promotes H2O2-induced autophagy, but mutant K472/473A, which lost nuclear localizing property, inhibits the autophagic process. The K472/473A mutant stimulates more lactate production, and decreases the activity of AMPK compared to the wild-type
physiological function
overexpression of microRNA miR-26b represses PFKFB3 mRNA and protein levels followed by modulation of the expression of glycolytic components such as LDHA, GLUT-1 and markers of invasion and cell cycle such as MMP-9, MMP-2, cyclin D1 and p27. The binding site for miR-26b is predicted in the 3'-untranslated region of the PFKFB3 gene
physiological function
Transforming growth factor TGFbeta1 induces isoform PFKFB3 expression and stimulates glycolysis in Panc1 cells. siRNA silencing of PFKFB3 prevents the stimulation of glycolysis and in vitro invasion ability of Panc1 cells by TGFbeta1. PFKFB3 silencing suppresses the TGFbeta1-mediated induction of the Snail protein
physiological function
tumor suppressor p53 regulates the expression of PFKFB4 and p53-deficient cancer cells are highly dependent on the function of the enzyme. Depletion of PFKFB4 from p53-deficient cancer cells increases levels of fructose-2,6-bisphosphate, leading to increased glycolytic activity but decreased routing of metabolites through the oxidative arm of the pentose-phosphate pathway. PFKFB4 is also required to support the synthesis and regeneration of nicotinamide adenine dinucleotide phosphate (NADPH) in p53-deficient cancer cells. Depletion of PFKFB4-attenuates cellular biosynthetic activity and results in the accumulation of reactive oxygen species and cell death in the absence of p53. Silencing of PFKFB4-induces apoptosis in p53-deficient cancer cells in vivo and interferes with tumor growth
physiological function
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase-2 regulates TP53-dependent paclitaxel sensitivity in ovarian and breast cancers
physiological function
-
role for PFKFB3/iPFK2 in regulating glycolysis in hypothalamic neurons, in the context of neuronal glucose sensing and neuropeptide expression. PFKFB3/iPFK2 responds to re-feeding, which in turn stimulates hypothalamic glycolysis and decreases hypothalamic AMPK phosphorylation and alters neuropeptide expression in a pattern that is associated with suppression of food intake
-
physiological function
-
role for phosphofructo 2-kinase/fructose 2,6-bisphosphate (PFK2/FBPase2) as a cytoplasmic binding partner of glucokinase and glucagon-induced uptake of glucokinase to the nucleus
-
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.
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.
S466E
-
mutant is phosphorylated by protein kinase B with a stoichiometry to about half that of wild-type enzyme in vitro
S466E/S483E
-
the double mutant is not phosphorylated by protein kinase B, mutation decreases Km of beta-D-fructose 6-phosphate in vitro
S483E
-
mutant is phosphorylated by protein kinase B with a stoichiometry to about half that of wild-type enzyme and mutation decreases citrate inhibition in vitro
C238A
-
site-directed mutagenesis, the mutation does not affect the kinetic parameters, allosteric inhibition, dimer stability, nor oligomeric structure of the enzyme
C238F
-
site-directed mutagenesis, the mutation does not affect the kinetic parameters, allosteric inhibition, dimer stability, nor oligomeric structure of the enzyme
C295A
-
site-directed mutagenesis, decreased kcat and increased Km for ATP and beta-D-fructose 6-phosphate compared to the wild-type enzyme
C295F
-
site-directed mutagenesis, decreased kcat and increased Km for ATP and beta-D-fructose 6-phosphate compared to the wild-type enzyme
E190Q
-
mutant presents a 50fold decrease in the kcat value and a 15fold increment in the apparent Km for MgATP2+. E190Q mutant presents alterations in the inhibition by MgATP2- and phosphate
L307A
-
site-directed mutagenesis, C-terminal point mutant, further mutants analyzed that reveal successive deletions of up to 10 residues at the C-terminal end
Y306A
-
site-directed mutagenesis, C-terminal point mutant, no dimer-tetramer conversion in presence of MgATP, inhibition pattern almost undistinguishable from the wild-type, conformational changes leading to allosteric inhibition can be uncoupled from tetramer formation at least in the Y306A mutant
R279A
-
mutation eliminates both the binding of ATP to the bisphosphatase domain of the bifunctional enzyme and the activation of enzyme by ATP
R359A
-
mutation eliminates both the binding of ATP to the bisphosphatase domain of the bifunctional enzyme and the activation of enzyme by ATP
H253A
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
H253A/S460D
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
K472/473A
mutant fails to localize in nucleus, mainly localizes in cytoplasm. The mutant inhibits the autophagic process, stimulates lactate production, and decreases the activity of AMPK compared to the wild-type
K472A/K473A
cytoplasmic mutant
P2R
-
kinetic properties of human liver mutant and rat wild-type enzyme are very similar
R75A/R76A
kinase inactive
S302R
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
S460D
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
S460D/T470D
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
S477D
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
T470D
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
A44G
-
the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by approximately 20fold compared to wilde-type values
A44V
-
the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by 8fold and 20fold compared to wilde-type values
K172A
-
increase in Km of beta-D-fructose 6-phosphate
K172E
-
increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
K172H
-
increase in Km of MgATP2-
K172R
-
increase in Km of beta-D-fructose 6-phosphate
K51A
-
increase in Km of beta-D-fructose 6-phosphate
K51H
-
increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
L148N
-
inactive mutant enzyme
L168A
-
inactive mutant enzyme
L168R
-
mutant enzyme shows 0.2% of wild-type activity
P2R
-
kinetic properties of human liver mutant and rat wild-type enzyme are very similar
R136K
-
increase in Km of MgATP2-
R136L
-
increase in Km of beta-D-fructose 6-phosphate
R193H
-
increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
R193L
-
increase in Km of beta-D-fructose 6-phosphate
R78H
-
increase in Km of MgATP2-
R78L
-
increase in Km of MgATP2-
R79H
-
increase in Km of MgATP2-
R79L
-
increase in Km of MgATP2-
S32A/H258A
-
site-directed mutagenesis, increased activity and incresaed expression level in recombinant HEK-293 cells compared to the wild-type enzyme
S32A/H258A
mutant unable to be phosphorylated
additional information
the deletion of N-terminal 318 amino acids abolishes the Michaelis-Menten kinetics of enzyme, Km of beta-D-fructose 6-phosphate is increased, whereas Km of ATP is not significantly altered. When the first 66 amino acids are deleted, the activity ration between 6-phosphofructo-2-kinase and beta-D-fructose 2,6-bisphosphatase is halved. The deletion of 125, 179, 249 and 318 amino acids results in progressive further decreases in the activity ratio and the activity ratio is reduced 4fold when N-terminus is deleted completely. The full-length enzyme is eluted as a tetramer, whereas the truncated enzymes are eluted as monomers
additional information
-
mutant enzymes of rat testis are constructed, in which its terminal peptides are replaced with those of the liver or the heart enzyme
additional information
-
the chicken enzyme in which the C-termini tail were replaced with that of rat enzyme is not activated by ATP
additional information
-
a series of C-terminal deletion mutants are generated: 15, 20, 25 and 30 amino acids, the deletion of the C-terminal 25 or 30 residues of enzyme increases Km of beta-D-fructose 6-phosphate by approximately 2fold. The mutations E446A, H444A, H444K, H444E, R445E, R445L prove the importance of His444 and Arg445.The C-terminal region I involves in the activation of enzyme by ATP.
additional information
construction of a chimeric mutant fusing the N-terminal portion of residues 1-444 of the human enzyme to the C-terminal part, residues 450-530, of the Bos taurus enzyme, i.e. HBPBHP, construction of a deletion mutant lacking the entire carboxyterminal region of residues 446-519
additional information
knockdown of PFKFB4 in prostate cancer cells by specific shRNA targeting
additional information
siRNA silencing of endogenous PFKFB3 in HeLa cells by siRNA
additional information
-
siRNA silencing of endogenous PFKFB3 in HeLa cells by siRNA
additional information
stable shRNA knockdown of PFKFB4, silencing by siRNA and genomic deletion of PFKFB4 decrease fructose 2,6-bisphosphate. PFKFB4 overexpression increases fructose 2,6-bisphosphate and selective PFKFB4 inhibition in vivo markedly reduces fructose 2,6-bisphosphate, glucose uptake, and ATP levels
additional information
-
-
additional information
-
effects of N- and C-terminal deletions of skeletal muscle and liver enzyme, e.g. ND4, ND7, ND12, ND23, CD30, comparison of the kinetic properties of deletion mutants
additional information
-
mutant enzymes of rat testis are constructed, in which its terminal peptides are replaced with those of the liver or the heart enzyme
additional information
-
ATP binding and the effect of pH on the kinetics are characterized
additional information
-
mutant enzyme, in which the four tryptophan residues in the isoenzyme are mutated to phenylalanine, structure
additional information
-
enzyme contains four tryptophan residues: Trp15, Trp64, Trp299 and Trp320, mutant enzymes contain either no Trp or a single Trp at each location, the other Trp residues having been converted to Phe, mutations do not cause large change in protein conformation and function, Trp299 and Trp320 in mutant enzymes quenched by iodide to a small extent can indicate an altered conformation, Trp64 is not accessible
additional information
-
engineering of the LKVWT glucokinase-binding motif in the FBPase-2 domain of islet PFK-2/FBPase-2 to HKEWR leads to significantly lower interaction with glucokinase compared with wild-type at 25 mmol/liter glucose
additional information
generation of a fluorescent PFK2/FBPase2-YC155 construct
additional information
-
generation of a fluorescent PFK2/FBPase2-YC155 construct
-
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.
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.
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.