Any feedback?
Literature summary for 2.7.1.11 extracted from
- Phosphofructo-1-kinase: role of charge neutralization in the active site (1995), Biochem. Biophys. Res. Commun., 214, 765-770.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D127/R252Q | very low activity, unchanged Km for fructose 6-phosphate | Escherichia coli |
| D127S | almost no activity | Escherichia coli |
| R252Q | 50fold decrease in Kcat, 1600fold increase in Km for fructose 6-phosphate | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.14 | - |
D-fructose 6-phosphate | pH 8.5, 30°C, D127/R252Q double mutant PFK | Escherichia coli |  |
| 0.16 | - |
D-fructose 6-phosphate | pH 8.5, 30°C | Escherichia coli | |
| 0.2 | - |
ATP | pH 8.5, 30°C | Escherichia coli | |
| 0.2 | - |
D-fructose 6-phosphate | pH 8.5, 30°C, D127S mutant PFK | Escherichia coli | |
| 254 | - |
D-fructose 6-phosphate | pH 8.5, 30°C, R252Q mutant PFK | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 3.7 | - |
fructose 6-phosphate | pH 8.5, 30°C, R252Q mutant PFK | Escherichia coli | |
| 167 | - |
fructose 6-phosphate | pH 8.5, 30°C | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.2 | - |
R72H mutant PFK, strong decrease in activiy above | Escherichia coli |
| 9 | 10.5 | - |
Escherichia coli |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 10.5 | approx. 10% of maximal activity at pH 5.5, approx. 50% at pH 7.0 | Escherichia coli |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
