+ |
OGA | up-regulates activity
deglycosylation
|
PFKL |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267608 |
Ser529 |
CVIPATIsNNVPGTD |
Homo sapiens |
|
pmid |
sentence |
26399441 |
Our previous investigation on O-GlcNAcylation of PFK1 has demonstrated that O-GlcNAcylation inhibits PFK1 enzyme activity|In cells, a single set of antagonistic enzymes-O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase are responsible for the addition and removal of GlcNAc moiety, respectively. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
OGT | down-regulates activity
glycosylation
|
PFKL |
0.282 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267585 |
Ser529 |
CVIPATIsNNVPGTD |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
22923583 |
O-GlcNAcylation was induced at serine 529 of phosphofructokinase 1 (PFK1) in response to hypoxia. Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway| O-GlcNAc transferase (OGT) catalyzes the transfer of N-acetylglucosamine from uridine diphospho-N-acetylglucosamine (UDP-GlcNAc) to serine or threonine residues |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
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 |
+ |
PFKL | up-regulates quantity
chemical modification
|
beta-D-fructofuranose 1,6-bisphosphate(4-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266472 |
|
|
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 |
+ |
CyclinD3/CDK6 | down-regulates activity
phosphorylation
|
PFKL |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276451 |
|
|
in vitro |
|
pmid |
sentence |
28607489 |
In vitro kinase reactions revealed that all three PFK1 isoforms (PFKP, PFKL, PFKM) and PKM2 were phosphorylated by cyclin D3-CDK6 (Extended Data Fig. 2a–d, Supplementary Table 4). |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
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 |