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Literature summary for 5.4.2.2 extracted from
- Constitutive expression, purification and characterization of a phosphoglucomutase from Fusarium oxysporum (2011), Enzyme Microb. Technol., 48, 217-224.
General Stability
| General Stability | Organism |
|---|---|
| loss of activity is observed when phosphate buffer is used in the pH range of 6.0-8.0 | Fusarium oxysporum |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00103 | - |
D-glucose 1,6-diphosphate | in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C | Fusarium oxysporum |  |
| 0.1 | - |
alpha-D-glucose 1-phosphate | in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C | Fusarium oxysporum | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | the enzyme is also active with 5 mM Ca2+ but to a lesser extent as Co2+ (11.9% relative activity) | Fusarium oxysporum | |
| Co2+ | PGM requires the presence of a divalent cation for its function with maximum activity (100%) being obtained with 5 mM Co2+ | Fusarium oxysporum | |
| Mg2+ | the enzyme is also active with 5 mM Mg2+ but to a lesser extent as Co2+ (24.5% relative activity) | Fusarium oxysporum | |
| Mn2+ | the enzyme is also active with 5 mM Mn2+ but to a lesser extent as Co2+ (69.5% relative activity) | Fusarium oxysporum | |
| Ni2+ | the enzyme is also active with 5 mM Ni2+ but to a lesser extent as Co2+ (22.5% relative activity) | Fusarium oxysporum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 56000 | - |
1 * 56000, SDS-PAGE | Fusarium oxysporum |
| 60000 | - |
gel filtration | Fusarium oxysporum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Fusarium oxysporum | - |
- |
- |
| Fusarium oxysporum F3 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Q-Sepharose column chromatography and Sephacryl-S 100 gel filtration | Fusarium oxysporum |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1.1 | - |
crude enzyme, at pH 7.6, 25°C | Fusarium oxysporum |
| 5.3 | - |
after 5fold purification, at pH 7.6, 25°C | Fusarium oxysporum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-D-glucose 1-phosphate | - |
Fusarium oxysporum | alpha-D-glucose 6-phosphate | - |
? | |
| alpha-D-glucose 1-phosphate | - |
Fusarium oxysporum F3 | alpha-D-glucose 6-phosphate | - |
? | |
| D-glucose 1,6-diphosphate | - |
Fusarium oxysporum | ? | - |
? | |
| D-glucose 1,6-diphosphate | - |
Fusarium oxysporum F3 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 56000, SDS-PAGE | Fusarium oxysporum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PGM | - |
Fusarium oxysporum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
- |
Fusarium oxysporum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 15 | 50 | - |
Fusarium oxysporum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 60 | PGM is almost stable (12% loss of the activity) at 30°C for 60 min, while almost complete loss of activity is observed at 50 and 60°C after 10 min | Fusarium oxysporum |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.74 | - |
alpha-D-glucose 1-phosphate | in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C | Fusarium oxysporum | |
| 0.74 | - |
D-glucose 1,6-diphosphate | in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C | Fusarium oxysporum | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
using 3-(N-morpholino)propanesulfonic acid buffer | Fusarium oxysporum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 8 | using 3-(N-morpholino)propanesulfonic acid buffer, the enzyme retains up to 90% of its initial activity | Fusarium oxysporum |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 10 | at pH 7.0 only 17.5% of the relative activity is recovered, the enzyme retains 14% of its initial activity after incubation at pH 10.0 | Fusarium oxysporum |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Fusarium oxysporum | isoelectric focusing | - |
3.5 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | PGM is a key enzyme in carbohydrate metabolism, where it catalyzes the reversible transfer of a phosphate group between C-1 and C-6 of D-glucose via D-glucose 1,6-diphosphate | Fusarium oxysporum |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 7.38 | - |
alpha-D-glucose 1-phosphate | in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C | Fusarium oxysporum | |
| 714.3 | - |
D-glucose 1,6-diphosphate | in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C | Fusarium oxysporum | |
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