Cloned (Comment) | Organism |
---|---|
- |
Staphylococcus aureus |
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 | 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | Q2FXM8 | - |
- |
Staphylococcus aureus NCTC 8325 | Q2FXM8 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Staphylococcus aureus |
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 | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Staphylococcus aureus |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Staphylococcus aureus |