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Literature summary for 2.7.1.105 extracted from
- Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence His444-Arg-Glu-Arg in modulation of the bisphosphatase activity by its kinase domain (2001), Biochem. J., 357, 513-520.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 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 | Gallus gallus |  |
| 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 | Rattus norvegicus | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Gallus gallus |
| expression in Escherichia coli | Rattus norvegicus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | - |
Rattus norvegicus |
| additional information | the chicken enzyme in which the C-termini tail were replaced with that of rat enzyme is not activated by ATP | Gallus gallus |
| additional information | a series of C-terminal deletion mutants are generated: 15, 20, 25 and 30 amino acids, the deletion of the C-terminal 25 or 30 residues of enzyme increases Km of beta-D-fructose 6-phosphate by approximately 2fold. The mutations E446A, H444A, H444K, H444E, R445E, R445L prove the importance of His444 and Arg445.The C-terminal region I involves in the activation of enzyme by ATP. | Gallus gallus |
| R279A | mutation eliminates both the binding of ATP to the bisphosphatase domain of the bifunctional enzyme and the activation of enzyme by ATP | Gallus gallus |
| R359A | mutation eliminates both the binding of ATP to the bisphosphatase domain of the bifunctional enzyme and the activation of enzyme by ATP | Gallus gallus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme | Gallus gallus | |
| additional information | phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme | Rattus norvegicus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | comparison of Km of wild-type and mutant enzyme | Gallus gallus | |
| additional information | - |
additional information | comparison of Km of wild-type and mutant enzyme | Rattus norvegicus | |
| 0.022 | - |
beta-D-fructose 6-phosphate | pH 7.5, 30°C, comparison of Km of wild-type, mutant and mutant phosphorylated enzyme | Gallus gallus | |
| 0.11 | - |
ATP | pH 7.5, 30°C | Gallus gallus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Rattus norvegicus | |
| Mg2+ | inhibition of enzyme at 2 mM, but no effect on activation by ATP | Gallus gallus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + beta-D-fructose 6-phosphate | Gallus gallus | - |
ADP + beta-D-fructose 2,6-bisphosphate | - |
? | |
| ATP + beta-D-fructose 6-phosphate | Rattus norvegicus | responsible for regulation of fructose 2,6-bisphosphate-concentration | ADP + beta-D-fructose 2,6-bisphosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Gallus gallus | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme | Gallus gallus |
| phosphoprotein | phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme | Rattus norvegicus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 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 | Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Gallus gallus | - |
| liver | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + beta-D-fructose 6-phosphate | - |
Gallus gallus | ADP + beta-D-fructose 2,6-bisphosphate | - |
? | |
| ATP + beta-D-fructose 6-phosphate | - |
Gallus gallus | ADP + beta-D-fructose 2,6-bisphosphate | - |
r | |
| ATP + beta-D-fructose 6-phosphate | - |
Rattus norvegicus | ADP + beta-D-fructose 2,6-bisphosphate | - |
r | |
| ATP + beta-D-fructose 6-phosphate | responsible for regulation of fructose 2,6-bisphosphate-concentration | Rattus norvegicus | ADP + beta-D-fructose 2,6-bisphosphate | - |
? | |
| additional information | also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) | Gallus gallus | ? | - |
? | |
| additional information | also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) | Rattus norvegicus | ? | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Gallus gallus |
| 30 | - |
assay at | Rattus norvegicus |
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