Cloned (Comment) | Organism |
---|---|
expression is performed using bacterial strain G6MD3 | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
G336D | a higher activity enzyme form, 10fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme | Escherichia coli |
P295D | extremely high activity in the absence of fructose 1,6-bisphosphate, 20fold decreased affinity for AMP than wild-type enzyme | Escherichia coli |
P295D/G336D | the double mutant enzyme is more active in the absence of fructose 1,6-bisphosphate, with a higher affinity for fructose 1,6-bisphosphate and a lower apparent affinity for AMP than either single mutated enzyme | Escherichia coli |
P295E | extremely high activity in the absence of fructose 1,6-bisphosphate, 10fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme | Escherichia coli |
P295G | activity in the absence of fructose 1,6-bisphosphate is similar to wild-type enzyme | Escherichia coli |
P295G | 3fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme | Escherichia coli |
P295N | 3.4fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme | Escherichia coli |
P295Q | 3.8fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
AMP | - |
Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic parameters | Escherichia coli | |
2.2 | - |
ATP | pH 7.0, 37°C, wild-type enzyme in the absence of fructose 1,6-bisphosphate, comparison of Km of wild-type and mutant enzymes in the presence and absence of fructose 1,6-bisphosphate | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + alpha-D-glucose 1-phosphate | Escherichia coli | - |
diphosphate + ADP-glucose | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
wild-type and mutant enzymes, purification of wild-type and single mutant enzyme usually involves a 5 min/60°C heat treatment step, but the heat treatment step of the double mutant enzyme results in 20% loss of activity | Escherichia coli |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
80 | 100 | mutant enzymes | Escherichia coli |
100 | - |
wild-type enzyme | Escherichia coli |
110 | - |
double mutant enzymes | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + alpha-D-glucose 1-phosphate | - |
Escherichia coli | diphosphate + ADP-glucose | - |
? |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | - |
purification of wild-type and single mutant enzyme usually involves a 5 min/60°C heat treatment step, the heat treatment step of the double mutant enzyme results in 20% loss of activity | Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.04 | - |
AMP | pH 7.6, 37°C, wild-type enzyme | Escherichia coli | |
0.094 | - |
AMP | pH 7.0, 37°C, wild-type enzyme, in the presence of a saturating concentration of fructose 1,6-bisphosphate | Escherichia coli | |
0.3 | - |
AMP | pH 7.0, 37°C, mutant enzyme P295G, in the presence of a saturating concentration of fructose 1,6-bisphosphate, | Escherichia coli | |
0.34 | - |
AMP | pH 7.0, 37°C, mutant enzyme P295N, in the presence of a saturating concentration of fructose 1,6-bisphosphate | Escherichia coli | |
0.38 | - |
AMP | pH 7.0, 37°C, mutant enzyme P295Q, in the presence of a saturating concentration of fructose 1,6-bisphosphate | Escherichia coli | |
0.95 | - |
AMP | pH 7.0, 37°C, mutant enzyme G336D, in the presence of a saturating concentration of fructose 1,6-bisphosphate | Escherichia coli | |
0.96 | - |
AMP | pH 7.0, 37°C, mutant enzyme P295E, in the presence of a saturating concentration of fructose 1,6-bisphosphate | Escherichia coli | |
2 | - |
AMP | pH 7.0, 37°C, mutant enzyme P295D, in the presence of a saturating concentration of fructose 1,6-bisphosphate | Escherichia coli | |
4.95 | - |
AMP | pH 7.0, 37°C, double mutant enzyme P295D/G336D | Escherichia coli |