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Enzyme Nomenclature
Information on EC 2.7.1.105 - 6-phosphofructo-2-kinase
for references in articles please use BRENDA:EC2.7.1.105
Word Map on EC 2.7.1.105
- 2.7.1.105
- 2,6-bisphosphate
- fructose-2,6-bisphosphate
- 6-phosphofructo-1-kinase
- pfkfb3
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camp-dependent
- glucagon
- phosphofructokinase-1
- mgatp
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gluconeogenic
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phosphoenzyme
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cyclic-amp-dependent
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fru-6-p
- medicine
- sn-glycerol
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3-3hglucose
- fbpase-2
- pharmacology
- drug development
- diagnostics
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.7.1.105
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RECOMMENDED NAME
GeneOntology No.
6-phosphofructo-2-kinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46; mechanism
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46; random mechanism
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46; kinetic mechanism
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
HBP1 and HBP2 both show a random order equilibrium bi bi mechanism, bifunctional enzyme comprises both 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase, EC 3.1.3.46, activities
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
ordered bi bi mechanism, structural and functional roles of Cys-238 and Cys-295
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional enzyme comprises both 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase, EC 3.1.3.46, activities
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional enzyme comprises both 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase, EC 3.1.3.46, activities, residues K51, T52, D128, and K172 are key catalytic residues for the 6-phosphofructo-2-kinase activity
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46; high 6-phosphofructo-2-kinase activity compared to the fructose 2,6-bisphosphatase
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46; high 6-phosphofructo-2-kinase activity compared to the fructose 2,6-bisphosphatase
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ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
ATP:beta-D-fructose-6-phosphate 2-phosphotransferase
Not identical with EC 2.7.1.11 6-phosphofructokinase. The enzyme co-purifies with EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.
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CAS REGISTRY NUMBER
COMMENTARY
78689-77-7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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potato plant, enzyme of Solanum tuberosum is 83% identical with enzyme of Zea mays and 72% identical with enzyme of Pinus taeda
SwissProt
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bifunctional 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4
SwissProt
Pfkfb3 gene; overexpression of the Pfkfb3 gene in Mus musculus, generation of uPFK-2 transgenic line
SwissProt
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640281, 640282, 640283, 640284, 640285, 640286, 640287, 640288, 640289, 640290, 640291, 640294, 640295, 640297, 640298, 640300, 640302, 640303, 640305, 640306, 640307, 640324, 640325, 640327, 640328, 640329, 640330, 640335, 640336, 640339, 640342, 640344, 674911, 676005, 94932, 94935, 94948
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bifunctional 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
SwissProt
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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; 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; 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
metabolism
physiological function
malfunction
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Akt inactivation blocks PFKFB2 phosphorylation and fructose 2,6-bisphosphate production
malfunction
Akt inactivation blocks PFKFB2 phosphorylation and fructose 2,6-bisphosphate production
malfunction
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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
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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
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
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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
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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
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malfunction
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Akt inactivation blocks PFKFB2 phosphorylation and fructose 2,6-bisphosphate production
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metabolism
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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
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cancer cells use control of PFKFB3 of the important glycolytic pathway to generate ATP
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
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; 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; 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; 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
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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
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
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moderate grade hyperammonemia activates lactate dehydrogenase-4 and 6-phosphofructo-2-kinase to support increased lactate turnover in the brain slices
metabolism
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upregulation of p62 and autophagy is a response to oxidative stress caused by PFKFB4. PFKFB4 is an autophagy regulator
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; 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; 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; 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
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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
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metabolism
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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
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physiological function
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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
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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
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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
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
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
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; 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; 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
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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
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
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; role of PFKFB proteins in the control of cancer metabolism; 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; 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
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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
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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
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
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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
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the PFK2 domain of PFK2/FBPase2 regulates glycolysis to maintain the pyruvate pool for lactate synthesis
physiological function
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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
fructose 2,6-bisphosphate is a positive regulator of the glycolytic enzyme phosphofructokinase
physiological function
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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
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physiological function
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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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + beta-D-fructose 2,6-bisphosphate
ATP + beta-D-fructose 6-phosphate
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reverse reaction, at 50% the rate of forward reaction
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r
CTP + D-fructose 6-phosphate
CDP + beta-D-fructose 2,6-bisphosphate
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-
-
-
?
ITP + beta-D-fructose 6-phosphate
IDP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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carbon-partitioning in Arabidopsis is regulated by fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase
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-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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-
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
-
-
-
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
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
regulation of glycolysis
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
the inducible enzyme is an important regulator of glycolysis that may be responsible for sustaining the high glycolytic flux of rapidly proliferating leukemia cells
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
bifunctional enzyme catalyzes the forward and reverse reaction using different catalytic sites
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways even under severe hypoxic conditions
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli, role in the progression of cancerous cells, antiproliferative effects during inhibitor incubation determined
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
transgene causes changes in cardiac metabolite concentrations, increased glycolysis, reduced palmitate oxidation, protection from hypoxia
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
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
?
-
analysis of MgATP-induced tetramer formation
-
-
?
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
?
-
-
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
?
-
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
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
Q9MB58
-
-
-
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
P16118
-
-
?
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
Q16875
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
O60825, P16118, Q16875, Q16877
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
Q16875
-
-
-
?
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
P16118, Q16877
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
Q16877
-
-
-
?
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
O60825
-
-
-
?
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
Q16875
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
P16118
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
P70265
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
A7UAK5
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
A7UAK5
-
-
-
?
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
Q9JJH5
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
P07953
-
-
-
?
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
P25114
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
P25114
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
Q9JJH5
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
P07953
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
O81398
-
-
?
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
O64983
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
Q52MQ5, Q6PY95
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
Q5U4Z6, Q6NRY0
-
-
-
?
additional information
?
-
-
Cys-295 is involved in allosteric regulation
-
-
-
additional information
?
-
Q16875
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
?
-
P07953
the enzyme binds to glucokinase in the cytoplasm
-
-
-
additional information
?
-
P07953
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
?
-
Q52MQ5
evolution of the bifunctional enzyme
-
-
-
additional information
?
-
Q6PY95
evolution of the bifunctional enzyme
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
AsO43-
Mg2+
phosphate
Mg2+
-
inhibits at higher concentrations, strain DF903; MgATP2; MgGTP2; requirement, active substrate: MgNTP
Mg2+
-
requirement of a Mg2+ ion, besides the one present in the metal-nucleotide complex, for catalysis in the wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
-
-
4-(4-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-5-bromo-6-oxopyridazin-1(6H)-yl)benzonitrile
-
-
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)-4-bromo-2-(3-phenylpropyl)pyridazin-3(2H)-one
-
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-((2-(dimethylamino)ethyl)-amino)benzyl)pyridazin-3(2H)-one
-
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-(trifluoromethoxy)phenyl)-pyridazin-3(2H)-one
-
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-chlorophenyl)pyridazin-3(2H)-one
-
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-iodobenzyl)pyridazin-3(2H)-one
-
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(pyrimidin-5-yl)pyridazin-3(2H)-one
-
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenethylpyridazin-3(2H)-one
-
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenylpyridazin-3(2H)-one
-
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-chloro-2-phenylpyridazin-3(2H)-one
-
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-ethoxy-2-phenylpyridazin-3(2H)-one
-
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-iodo-2-phenylpyridazin-3(2H)-one
-
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-isopropyl-2-phenylpyridazin-3(2H)-one
-
-
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
AICAR, associated with phosphorylation of PFK-2 on Ser-32, phosphorylation increased of both wild-type and overexpressed PFK-2 protein in hepatocytes
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
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
-
-
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
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
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
-
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
glucagon
-
the native and the recombinant wild-type and mutant enzymes are phosphorylated after incubation with glucagon inactivating the enzyme
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
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
HBP1 and HBP2, the bifunctional enzyme is regulated via inhibition by phosphoenolpyruvate, uncompetitive against ATP, noncompetitive against beta-D-fructose 6-phosphate
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
mixed-type inhibitory effect, phosphorylation enhances sensitivity
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
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
-
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
-
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
-
no inhibition by phosphorylation with Ca2+/calmodulin dependent protein kinase; no inhibition by protein kinase C
-
additional information
-
phosphorylation at lower pH-values; 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 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
enzyme is not affected by protein kinase C
-
additional information
enzyme is not affected by protein kinase C
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
the binding of ATP to the fructose 2,6-bisphosphatase domain of chicken liver 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase leads to activation of enzyme, but no activation of rat liver enzyme
ATP
-
the binding of ATP to the fructose 2,6-bisphosphatase domain of chicken liver 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase leads to activation of enzyme, but no activation of rat liver enzyme
Insulin
-
activation of transfected heart enzyme in human embryonic kidney 293 cells by inducing the phosphorylation of Ser466 and Ser483, activation is mediated by 3-phosphoinositide-dependent kinase-1, protein kinase B is in vivo not essential, activation is sensitive to LY294002 and wortmannin and insensitive to rapaycin and PD98059
-
Insulin
stimulates glycolysis in the heart by increasing glucose transport and activating H-PFK2 by phosphorylating Ser466 and Ser483 through protein kinase B within the C-terminal regulatory domain. Phosphorylation of Ser466 or Thr475 by protein kinase C does not change the enzyme activity. Phosphorylation at Ser84 possibly counteracts the effects of phosphorylation at the activating C-terminal sites
-
additional information
-
amino acids increase beta-D-fructose 2,6-bisphosphate concentration in HeLa and in MCF-7 human cells, molecular mechanisms involved differ from those observed with insulin. Only essential amino acids without glutamine are required to activate the PI3K/mTORC2 and p38/MAPKAPK-2 pathways and to increase the beta-D-fructose 2,6-bisphosphate concentration. The observed effects in signaling and metabolism are produced by a mixture of essential amino acids
-
additional information
amino acids increase beta-D-fructose 2,6-bisphosphate concentration in primary cardiomyocytes, molecular mechanisms involved differ from those observed with insulin. Only essential amino acids without glutamine are required to activate the PI3K/mTORC2 and p38/MAPKAPK-2 pathways and to increase the beta-D-fructose 2,6-bisphosphate concentration. The observed effects in signaling and metabolism are produced by a mixture of essential amino acids
-
additional information
-
one enzyme form is activated dramatically as result of modification by MgATP during preincubation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.048
ATP
-
pH 7.5, 30°C, comparison of Km of skeletal muscle and liver enzyme
0.29 - 0.38
ATP
-
pH 7.1, 30°C, kinetic data of various enzyme forms
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; 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
0.013
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged chimeric mutant enzyme, phosphorylated or nonphosphorylated
0.019 - 0.021
beta-D-fructose 6-phosphate
-
pH 7.8, in presence of phosphate
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
0.02
beta-D-fructose 6-phosphate
-
C-terminal deletion mutant D299, 1 mM co-substrate
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
-
comparison of Km of wild-type, mutant and mutant phosphorylated enzyme; pH 7.5, 25°C, heart
0.023
beta-D-fructose 6-phosphate
-
comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
0.025
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, liver, comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
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
0.036
beta-D-fructose 6-phosphate
-
C-terminal deletion mutant A305, 1 mM co-substrate
0.04
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, wild-type enzyme, testis
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
0.057
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
0.06
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
0.156
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, with ATP, in presence of phosphate
0.33 - 0.4
beta-D-fructose 6-phosphate
-
pH 7.1, 30°C, kinetic data of various enzyme forms
0.5 - 1
beta-D-fructose 6-phosphate
-
pH 8.0, forms 1-3, kinetic data of various enzyme forms
1 - 1.1
beta-D-fructose 6-phosphate
-
pH 7.5, 30°C, in absence of phosphate
1.4
beta-D-fructose 6-phosphate
pH 7.8, 25°C, effect of phosphate on Km
1.9 - 4.6
beta-D-fructose 6-phosphate
pH 7.1, 30°C, recombinant isozyme Tb1
39
beta-D-fructose 6-phosphate
pH 7.1, 30°C, protein kinase A treated 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 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
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
-
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
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
comparison of Km of hepatoma cells and liver enzyme
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.391
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant H253A
0.394
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant S460D; pH 7.5, 30°C, recombinant HBP1 mutant S460D/T470D
0.399
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged HBP1 mutant S302R
0.401
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant H253A/S460D
0.405
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant S477D
0.407
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant wild-type HBP1
0.43
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged wild-type HBP1
0.435
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant T470
0.447
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged wild-type HBP2
0.654
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, His-tagged chimeric mutant enzyme
0.678
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant phosphorylated, His-tagged chimeric mutant enzyme
0.696
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged HBP1 deletion mutant
53
D-fructose 6-phosphate
-
wild-type enzyme, 1 mM Mg2+; wild-type enzyme, 30 mM Mg2+
additional information
additional information
-
comparison of kcat/Km values of wild-type and mutant enzymes
-
additional information
additional information
-
comparison of kcat/Km values of wild-type and mutant enzymes
-
additional information
additional information
-
comparison of kcat/Km values of wild-type and mutant enzymes
-
additional information
additional information
kcat of wild-type and mutant HBP1 and of HBP2 with beta-D-fructose 2,6-bisphosphate, kcat for phosphorylated wild-type enzyme and mutants with beta-D-fructose 6-phosphate and beta-D-fructose 2,6-bisphosphate
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
inhibition of recombinant PFKFB3 protein, no inhibition of purified PFK-1 activity
8.5
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant S460D/T470D
9.2
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant S460D
9.5
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant H253A/S460D
9.6
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged HBP1 deletion mutant
9.7
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant S477D
10.9
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged HBP1 mutant S302R
11.1
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant H253A
11.8
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged wild-type HBP2
12.2
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant His-tagged wild-type HBP1
12.7
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant non-phosphorylated, His-tagged chimeric mutant enzyme
13
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant HBP1 mutant T470
13.4
beta-D-fructose 6-phosphate
pH 7.5, 30°C, recombinant phosphorylated, His-tagged chimeric mutant enzyme
0.53
phosphoenolpyruvate
-
noncompetitive to fructose 6-phosphate, pH 7.5, 30°C
0.7
phosphoenolpyruvate