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Literature summary for 2.4.1.1 extracted from
- Purification and characterisation of an alpha-glucan phosphorylase from the thermophilic bacterium Thermus thermophilus (1996), Eur. J. Biochem., 239, 150-155 .
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| alpha-D-glucose-methylenephosphonate | competitive inhibitor | Thermus thermophilus |  |
| gluconolactone | competitive inhibitor | Thermus thermophilus | |
| NaAsO2 | competitive inhibitor with respect to phosphate | Thermus thermophilus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.2 | - |
alpha-D-glucose 1-phosphate | synthesis reaction, cosubstrate: maltotetraose, pH 6.5, 70°C | Thermus thermophilus | |
| 1.7 | - |
maltoheptaose | degradation direction, cosubstrate: phosphate, pH 6.5, 30°C | Thermus thermophilus | |
| 1.9 | - |
phosphate | degradation direction, cosubstrate: maltoheptaose, pH 6.5, 30°C | Thermus thermophilus | |
| 2.2 | - |
phosphate | degradation direction, cosubstrate: maltoheptaose, pH 6.5, 70°C | Thermus thermophilus | |
| 2.8 | - |
maltotetraose | degradation direction, cosubstrate: phosphate, pH 6.5, 30°C | Thermus thermophilus | |
| 3.6 | - |
maltoheptaose | degradation direction, cosubstrate: phosphate, pH 6.5, 70°C | Thermus thermophilus | |
| 4.8 | - |
maltotetraose | degradation direction, cosubstrate: phosphate, pH 6.5, 70°C | Thermus thermophilus | |
| 12.7 | - |
maltotetraose | synthesis reaction, cosubstrate: alpha-D-glucose 1-phosphate, pH 6.5, 70°C | Thermus thermophilus | |
| 13.4 | - |
maltotriose | synthesis reaction, cosubstrate: alpha-D-glucose 1-phosphate, pH 6.5, 70°C | Thermus thermophilus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermus thermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glycogen + phosphate | - |
Thermus thermophilus | alpha-D-glucose 1-phosphate + ? | - |
? | |
| maltoheptaose + phosphate | - |
Thermus thermophilus | maltohexaose + alpha-D-glucose 1-phosphate | - |
? | |
| maltotetraose + phosphate | - |
Thermus thermophilus | maltotriose + alpha-D-glucose 1-phosphate | - |
r | |
| maltotriose + alpha-D-glucose 1-phosphate | - |
Thermus thermophilus | maltotetraose + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 90000, While at 25°C the subunit composition of the thermophilic enzyme is an octameric form, the preferential form at the optimum temperature of 70°C seems to be a dimer | Thermus thermophilus |
| octamer | 8 * 90000, While at 25°C the subunit composition of the thermophilic enzyme is an octameric form, the preferential form at the optimum temperature of 70°C seems to be a dimer | Thermus thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
in the pH range 5.5-6.5 | Thermus thermophilus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 90 | 50°C: about 50% of maximal activity, 90°C: about 40% of maximal activity | Thermus thermophilus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | the enzyme contains 1 M pyridoxal 5'-phosphate per M of subunit | Thermus thermophilus | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.1 | - |
alpha-D-glucose-methylenephosphonate | 70°C, pH not specified in the publication | Thermus thermophilus | |
| 3.3 | - |
gluconolactone | 70°C, pH not specified in the publication | Thermus thermophilus | |
| 4.1 | - |
NaAsO2 | 70°C, pH not specified in the publication | Thermus thermophilus | |
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