Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Oryctolagus cuniculus | |
Calmodulin | binding of one calmodulin per monomer promotes the dimerization of the enzyme although maintaining its full catalytic activity, 30 nM calmodulin activates 6-phosphofructo-1-kinase in the presence of its inhibitors citrate and lactate | Oryctolagus cuniculus | |
D-fructose 2,6-bisphosphate | - |
Oryctolagus cuniculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ATP | the inhibition of enzyme activity by ATP (above 1 mM) is abolished in the presence of calmodulin | Oryctolagus cuniculus | |
citrate | - |
Oryctolagus cuniculus | |
Lactate | - |
Oryctolagus cuniculus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | calmodulin binding to the enzyme is stimulated by 0.01 mM Ca2+ | Oryctolagus cuniculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
skeletal muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + D-fructose 6-phosphate | - |
Oryctolagus cuniculus | ADP + D-fructose 1,6-bisphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | calmodulin-bound dimers are active and less susceptible to inhibition by allosteric ligands, 5 mM ATP stabilizes phosphofructokinase dimers | Oryctolagus cuniculus |
Synonyms | Comment | Organism |
---|---|---|
6-phosphofructo-1-kinase | - |
Oryctolagus cuniculus |
ATP:D-fructose-6-phosphate-1-phosphotransferase | - |
Oryctolagus cuniculus |
PFK | - |
Oryctolagus cuniculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Oryctolagus cuniculus |