| + |
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-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. |
|
| 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 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
PFKFB3 | up-regulates quantity
chemical modification
|
beta-D-fructofuranose 2,6-bisphosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267260 |
|
|
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: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
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 |
| + |
beta-D-fructofuranose 2,6-bisphosphate | up-regulates activity
binding
|
PFKL |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267266 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19454274 |
The PFKFB enzymes synthesize fructose-2,6-bisphosphate (F2,6BP) which allosterically activates 6-phosphofructo-1-kinase (PFK-1), a rate-limiting enzyme and essential control point in the glycolytic pathway. PFK-1 is inhibited by ATP when energy stores are abundant and F2,6BP can override this inhibition and enhance glucose uptake and glycolytic flux |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
PFKFB4 | up-regulates quantity
chemical modification
|
beta-D-fructofuranose 2,6-bisphosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267264 |
|
|
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 |
| + |
beta-D-fructofuranose 2,6-bisphosphate | up-regulates activity
binding
|
PFK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267262 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19454274 |
The PFKFB enzymes synthesize fructose-2,6-bisphosphate (F2,6BP) which allosterically activates 6-phosphofructo-1-kinase (PFK-1), a rate-limiting enzyme and essential control point in the glycolytic pathway. PFK-1 is inhibited by ATP when energy stores are abundant and F2,6BP can override this inhibition and enhance glucose uptake and glycolytic flux |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
beta-D-fructofuranose 2,6-bisphosphate | up-regulates activity
binding
|
PFKP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267268 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19454274 |
The PFKFB enzymes synthesize fructose-2,6-bisphosphate (F2,6BP) which allosterically activates 6-phosphofructo-1-kinase (PFK-1), a rate-limiting enzyme and essential control point in the glycolytic pathway. PFK-1 is inhibited by ATP when energy stores are abundant and F2,6BP can override this inhibition and enhance glucose uptake and glycolytic flux |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
PFKFB4 | down-regulates quantity 
chemical modification
|
beta-D-fructofuranose 2,6-bisphosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267272 |
|
|
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 |
| + |
beta-D-fructofuranose 2,6-bisphosphate | up-regulates activity
binding
|
PFKM |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267267 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19454274 |
The PFKFB enzymes synthesize fructose-2,6-bisphosphate (F2,6BP) which allosterically activates 6-phosphofructo-1-kinase (PFK-1), a rate-limiting enzyme and essential control point in the glycolytic pathway. PFK-1 is inhibited by ATP when energy stores are abundant and F2,6BP can override this inhibition and enhance glucose uptake and glycolytic flux |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
3.0
beta-D-fructofuranose 2,6-bisphosphate