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Literature summary for 5.3.1.9 extracted from
- Substrate specificity of a glucose-6-phosphate isomerase from Pyrococcus furiosus for monosaccharides (2009), Appl. Microbiol. Biotechnol., 83, 295-303.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | slight inhibition at 1.5 mM | Pyrococcus furiosus |  |
| EDTA | strong inhibition | Pyrococcus furiosus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics for aldose substrates, overview | Pyrococcus furiosus | |
| 133 | - |
L-talose | pH 7.0, 95°C | Pyrococcus furiosus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | activates 5.2fold 1.5 mM | Pyrococcus furiosus | |
| Cu2+ | activates 1.3fold 1.5 mM | Pyrococcus furiosus | |
| Fe2+ | activates 3.9fold 1.5 mM | Pyrococcus furiosus | |
| Mg2+ | activates 4.7fold 1.5 mM | Pyrococcus furiosus | |
| Mn2+ | activates 1.7fold 1.5 mM | Pyrococcus furiosus | |
| Ni2+ | activates 4.5fold 1.5 mM | Pyrococcus furiosus | |
| Zn2+ | activates 4.2fold 1.5 mM | Pyrococcus furiosus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 21476 | - |
x * 21476, sequence calculation, x * 21500, SDS-PAGE | Pyrococcus furiosus |
| 21500 | - |
x * 21476, sequence calculation, x * 21500, SDS-PAGE | Pyrococcus furiosus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | P83194 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme 20fold by heat treatment and anion exchange chromatography | Pyrococcus furiosus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.39 | - |
purified native enzyme | Pyrococcus furiosus |
| 620 | - |
with substrate L-talose | Pyrococcus furiosus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glucose 6-phosphate | - |
Pyrococcus furiosus | D-fructose 6-phosphate | - |
r | |
| L-talose | best aldose substrate | Pyrococcus furiosus | L-tagatose | - |
? | |
| additional information | glucose-6-phosphate isomerase catalyzes the interconversion between two different aldoses and ketose for pentoses and hexoses via two isomerization reactions. Activity order as follows: aldose substrates with hydroxyl groups oriented in the same direction at C2, C3, and C4 better than C2 and C4 better than C2 and C3 better than C3 and C4. L-Talose and D-ribulose exhibit the most preferred substrates among the aldoses and ketoses, respectively, substrate specificity, overview | Pyrococcus furiosus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 21476, sequence calculation, x * 21500, SDS-PAGE | Pyrococcus furiosus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 95 | - |
- |
Pyrococcus furiosus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 98 | temperature profile, overview | Pyrococcus furiosus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermal inactivation follows first-order kinetics | Pyrococcus furiosus |
| 65 | - |
purified native enzyme, half-life is 170 h | Pyrococcus furiosus |
| 70 | - |
purified native enzyme, half-life is 68 h | Pyrococcus furiosus |
| 75 | - |
purified native enzyme, half-life is 41 h | Pyrococcus furiosus |
| 80 | - |
purified native enzyme, half-life is 25 h | Pyrococcus furiosus |
| 85 | - |
purified native enzyme, half-life is 19 h | Pyrococcus furiosus |
| 90 | - |
purified native enzyme, half-life is 11 h | Pyrococcus furiosus |
| 95 | - |
purified native enzyme, half-life is 7.9 h | Pyrococcus furiosus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 475.5 | - |
L-talose | pH 7.0, 95°C | Pyrococcus furiosus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
- |
Pyrococcus furiosus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 8.5 | pH profile, overview | Pyrococcus furiosus |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 3.58 | - |
L-talose | pH 7.0, 95°C | Pyrococcus furiosus | |
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