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Literature summary for 2.7.1.11 extracted from
- Structural insights into the regulation of Staphylococcus aureus phosphofructokinase by tetramer-dimer conversion (2018), Biochemistry, 57, 4252-4262 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Staphylococcus aureus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| sitting-drop vapor-diffusion method at 10°C. Crystal structures of SaPfk in complex with different ligands and biochemical analysis reveal that the flexibility of the Gly150-Leu151 motif in helix alpha7 plays a role in tetramer-dimer conversion | Staphylococcus aureus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G150D/L151A | the mutation stabilizes the SaPfk tetramer, with the mutant showing a higher affinity for D-fructose 6-phosphate and higher catalytic activity but less sigmoidal kinetics compared to wild-type enzyme | Staphylococcus aureus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + D-fructose 6-phosphate | Staphylococcus aureus | - |
ADP + D-fructose 1,6-bisphosphate | - |
? |  |
| ATP + D-fructose 6-phosphate | Staphylococcus aureus NCTC 8325 | - |
ADP + D-fructose 1,6-bisphosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | Q2FXM8 | - |
- |
| Staphylococcus aureus NCTC 8325 | Q2FXM8 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Staphylococcus aureus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + D-fructose 6-phosphate | - |
Staphylococcus aureus | ADP + D-fructose 1,6-bisphosphate | - |
? | |
| ATP + D-fructose 6-phosphate | - |
Staphylococcus aureus NCTC 8325 | ADP + D-fructose 1,6-bisphosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | the enzyme exists as both an active tetramer and an inactive dimer in solution. Multiple effectors, including pH, ADP, ATP, and adenylyl-imidodiphosphate, cause equilibrium shifts from the tetramer to dimer, whereas the substrate D-fructose 6-phosphate stabilizes tetrameric assembly | Staphylococcus aureus |
| tetramer | the enzyme exists as both an active tetramer and an inactive dimer in solution. Multiple effectors, including pH, ADP, ATP, and adenylyl-imidodiphosphate, cause equilibrium shifts from the tetramer to dimer, whereas the substrate D-fructose 6-phosphate stabilizes tetrameric assembly | Staphylococcus aureus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Staphylococcus aureus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 6.5 | - |
D-fructose 6-phosphate | pH 7.5, 37°C, wild-type enzyme | Staphylococcus aureus | |
| 25.2 | - |
D-fructose 6-phosphate | pH 7.5, 37°C mutant enzyme G150D/L151A | Staphylococcus aureus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Staphylococcus aureus |
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Release 2023.1 (January 2023)
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