| + |
β-D-fructose 6-phosphate | up-regulates quantity 
precursor of
|
beta-D-fructofuranose 1,6-bisphosphate(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266465 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Phosphofructokinase catalyzes the rate-limiting, ATP-mediated phosphorylation of F6P to FBP. PFK is a homo- or heterotetramer with a molecular mass of approximately 380 kDa, and the enzyme is allosterically regulated, among other metabolites, by 2,3-DPG.35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266464 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Phosphofructokinase catalyzes the rate-limiting, ATP-mediated phosphorylation of F6P to FBP. PFK is a homo- or heterotetramer with a molecular mass of approximately 380 kDa, and the enzyme is allosterically regulated, among other metabolites, by 2,3-DPG.35 Three different subunits have been identified in humans: PFK-M (muscle), PFK-L (liver), and PFK-P (platelet).The subunits are expressed in a tissue-specific manner and, in erythrocytes, 5 isoenzymes of varying subunit composition (M4, M3L1, M2L2, ML3, and L4) can be identified. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266466 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Phosphofructokinase catalyzes the rate-limiting, ATP-mediated phosphorylation of F6P to FBP. PFK is a homo- or heterotetramer with a molecular mass of approximately 380 kDa, and the enzyme is allosterically regulated, among other metabolites, by 2,3-DPG.35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266463 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Phosphofructokinase catalyzes the rate-limiting, ATP-mediated phosphorylation of F6P to FBP. PFK is a homo- or heterotetramer with a molecular mass of approximately 380 kDa, and the enzyme is allosterically regulated, among other metabolites, by 2,3-DPG.35 Three different subunits have been identified in humans: PFK-M (muscle), PFK-L (liver), and PFK-P (platelet).The subunits are expressed in a tissue-specific manner and, in erythrocytes, 5 isoenzymes of varying subunit composition (M4, M3L1, M2L2, ML3, and L4) can be identified. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
TALDO1 | up-regulates quantity
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267091 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19401148 |
Transaldolase (TAL, sedoheptulose 7-phosphate: d-glyceraldehyde 3-phosphate dihydroxyacetone transferase; EC number 2.2.1.2) is a cofactor-less enzyme of the pentose phosphate pathway (PPP) (Fig. 1A and B). It catalyzes the reversible transfer of a three carbon unit (“dihydroxyacetone”) between various sugar phosphates (from 3 to 8 carbon atoms in length). Physiological donor compounds are ketose sugar phosphates as fructose 6-phosphate or sedoheptulose 7-phosphate. Acceptor compounds are aldose sugar phosphates as glyceraldehyde 3-phosphate and erythrose 4-phosphate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pentose phosphate pathway |
| + |
GPI | up-regulates quantity
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266462 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Glucose 6-phosphate isomerase (GPI) catalyzes the interconversion of G6P into fructose-6-phosphate (F6P) in the second step of the Embden-Meyerhof pathway (Figure 1). As a result of this reversible reaction, products of the hexose-monophosphate shunt can be recycled to G6P. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
PFKL | down-regulates quantity 
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266468 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Phosphofructokinase catalyzes the rate-limiting, ATP-mediated phosphorylation of F6P to FBP. PFK is a homo- or heterotetramer with a molecular mass of approximately 380 kDa, and the enzyme is allosterically regulated, among other metabolites, by 2,3-DPG.35. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
FBP2 | up-regulates quantity
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267613 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30616754 |
FBPase converts fructose-1,6-bisphosphate (F-1,6-BP) to fructose-6-phosphate (F-6-P) and inorganic phosphate in the second rate-limiting reaction of gluconeogenesis.|FBP1 is ubiquitously present in tissues and is the key gluconeogenic enzyme in the liver and kidney, while FBP2 is restricted to the muscle |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PFKM | down-regulates quantity
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266467 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Phosphofructokinase catalyzes the rate-limiting, ATP-mediated phosphorylation of F6P to FBP. PFK is a homo- or heterotetramer with a molecular mass of approximately 380 kDa, and the enzyme is allosterically regulated, among other metabolites, by 2,3-DPG.35. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
β-D-fructose 6-phosphate | up-regulates quantity
precursor of
|
beta-D-fructofuranose 2,6-bisphosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267265 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15170386 |
Fru-2,6-P2 (fructose 2,6-bisphosphate) is a signal molecule that controls glycolysis. Since its discovery more than 20 years ago, inroads have been made towards the understanding of the structure– function relationships in PFK-2 (6-phosphofructo-2-kinase)/ FBPase-2 (fructose-2,6-bisphosphatase), the homodimeric bifunctional enzyme that catalyses the synthesis and degradation of Fru-2,6-P2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267261 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9404080 |
A full-length cDNA, which encodes a human placental fructose-6-phosphate,2-kinase/ fructose-2,6-bisphosphatase, was constructed and expressed in Escherichia coli. [...]The expressed enzyme was bifunctional with Vmax values of 142 and 0.2 milliunits/mg for the kinase and phosphatase activities, respectively. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
beta-D-fructofuranose 1,6-bisphosphate(4-) | up-regulates quantity
precursor of
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267589 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30616754 |
FBPase converts fructose-1,6-bisphosphate (F-1,6-BP) to fructose-6-phosphate (F-6-P) and inorganic phosphate in the second rate-limiting reaction of gluconeogenesis.|FBP1 is ubiquitously present in tissues and is the key gluconeogenic enzyme in the liver and kidney, while FBP2 is restricted to the muscle |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267588 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30616754 |
FBPase converts fructose-1,6-bisphosphate (F-1,6-BP) to fructose-6-phosphate (F-6-P) and inorganic phosphate in the second rate-limiting reaction of gluconeogenesis.|FBP1 is ubiquitously present in tissues and is the key gluconeogenic enzyme in the liver and kidney, while FBP2 is restricted to the muscle |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
FBP1 | up-regulates quantity
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267611 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30616754 |
FBPase converts fructose-1,6-bisphosphate (F-1,6-BP) to fructose-6-phosphate (F-6-P) and inorganic phosphate in the second rate-limiting reaction of gluconeogenesis.|FBP1 is ubiquitously present in tissues and is the key gluconeogenic enzyme in the liver and kidney, while FBP2 is restricted to the muscle |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
PFKP | down-regulates quantity
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266469 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Phosphofructokinase catalyzes the rate-limiting, ATP-mediated phosphorylation of F6P to FBP. PFK is a homo- or heterotetramer with a molecular mass of approximately 380 kDa, and the enzyme is allosterically regulated, among other metabolites, by 2,3-DPG.35. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
sedoheptulose 7-phosphate | up-regulates quantity
precursor of
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268133 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19401148 |
Transaldolase (TAL, sedoheptulose 7-phosphate: d-glyceraldehyde 3-phosphate dihydroxyacetone transferase; EC number 2.2.1.2) is a cofactor-less enzyme of the pentose phosphate pathway (PPP) (Fig. 1A and B). It catalyzes the reversible transfer of a three carbon unit (“dihydroxyacetone”) between various sugar phosphates (from 3 to 8 carbon atoms in length). Physiological donor compounds are ketose sugar phosphates as fructose 6-phosphate or sedoheptulose 7-phosphate. Acceptor compounds are aldose sugar phosphates as glyceraldehyde 3-phosphate and erythrose 4-phosphate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Pentose phosphate pathway |
| + |
PFKFB4 | down-regulates quantity
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268117 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15170386 |
Fru-2,6-P2 (fructose 2,6-bisphosphate) is a signal molecule that controls glycolysis. Since its discovery more than 20 years ago, inroads have been made towards the understanding of the structure– function relationships in PFK-2 (6-phosphofructo-2-kinase)/ FBPase-2 (fructose-2,6-bisphosphatase), the homodimeric bifunctional enzyme that catalyses the synthesis and degradation of Fru-2,6-P2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
alpha-D-glucose 6-phosphate(2-) | up-regulates quantity
precursor of
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266460 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Glucose 6-phosphate isomerase (GPI) catalyzes the interconversion of G6P into fructose-6-phosphate (F6P) in the second step of the Embden-Meyerhof pathway (Figure 1). As a result of this reversible reaction, products of the hexose-monophosphate shunt can be recycled to G6P. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis, Pentose phosphate pathway |
| + |
beta-D-fructofuranose 2,6-bisphosphate | up-regulates quantity
precursor of
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267274 |
|
|
in vitro |
|
| pmid |
sentence |
| 30553771 |
PFKFB3 has the highest kinase activity to shunt glucose toward glycolysis, whereas PFKFB4 has more FBPase-2 activity, redirecting glucose toward the pentose phosphate pathway, providing reducing power for lipid biosynthesis and scavenging reactive oxygen species |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
D-glyceraldehyde 3-phosphate(2-) | up-regulates quantity
precursor of
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268134 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19401148 |
Transaldolase (TAL, sedoheptulose 7-phosphate: d-glyceraldehyde 3-phosphate dihydroxyacetone transferase; EC number 2.2.1.2) is a cofactor-less enzyme of the pentose phosphate pathway (PPP) (Fig. 1A and B). It catalyzes the reversible transfer of a three carbon unit (“dihydroxyacetone”) between various sugar phosphates (from 3 to 8 carbon atoms in length). Physiological donor compounds are ketose sugar phosphates as fructose 6-phosphate or sedoheptulose 7-phosphate. Acceptor compounds are aldose sugar phosphates as glyceraldehyde 3-phosphate and erythrose 4-phosphate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis, Pentose phosphate pathway |
| + |
PFKFB4 | up-regulates quantity
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268118 |
|
|
in vitro |
|
| pmid |
sentence |
| 30553771 |
PFKFB3 has the highest kinase activity to shunt glucose toward glycolysis, whereas PFKFB4 has more FBPase-2 activity, redirecting glucose toward the pentose phosphate pathway, providing reducing power for lipid biosynthesis and scavenging reactive oxygen species |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PFK | down-regulates quantity
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266470 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Phosphofructokinase catalyzes the rate-limiting, ATP-mediated phosphorylation of F6P to FBP. PFK is a homo- or heterotetramer with a molecular mass of approximately 380 kDa, and the enzyme is allosterically regulated, among other metabolites, by 2,3-DPG.35. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
PFKFB3 | down-regulates quantity
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267271 |
|
|
in vitro |
|
| pmid |
sentence |
| 9404080 |
A full-length cDNA, which encodes a human placental fructose-6-phosphate,2-kinase/ fructose-2,6-bisphosphatase, was constructed and expressed in Escherichia coli. [...]The expressed enzyme was bifunctional with Vmax values of 142 and 0.2 milliunits/mg for the kinase and phosphatase activities, respectively. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Glycolysis and Gluconeogenesis |
3.0
β-D-fructose 6-phosphate