| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| D-Glucose 1,6-bisphosphate | 0.1 mM used in assay conditions | Laminaria digitata |
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) cells | Laminaria digitata |
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | has a negative effect on phosphomannomutase activity relative to the control | Laminaria digitata | |
| Co2+ | has a negative effect on phosphomannomutase activity relative to the control | Laminaria digitata | |
| Li2+ | has a negative effect on phosphomannomutase activity relative to the control | Laminaria digitata | |
| Na+ | has a negative effect on phosphomannomutase activity relative to the control | Laminaria digitata | |
| NaCl | both the enzyme's phosphoglucomutase and phosphomannomutase activities decrease at increased NaCl concentrations, with phosphomannomutase displaying slightly higher levels of relative activity (55% relative activity at 0.2 M NaCl) than phosphoglucomutase (43% relative activity at 0.2 M); but as NaCl concentrations increase, similar decreases in relative phosphoglucomutase and phosphomannomutase activities are evident | Laminaria digitata |
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | promotes both phosphoglucomutase and phosphomannomutase activities of the enzyme. 10 mM is used in assay conditions | Laminaria digitata | |
| Mn2+ | enhances the phosphoglucomutase activity of the enzyme | Laminaria digitata | |
| Zn2+ | enhances the phosphoglucomutase activity of the enzyme | Laminaria digitata |
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-D-glucose 1-phosphate | Laminaria digitata | - |
D-glucose 6-phosphate | - |
? | |
| alpha-D-mannose 1-phosphate | Laminaria digitata | - |
D-mannose 6-phosphate | - |
? |
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Laminaria digitata | - |
- |
- |
| Purification (Comment) | Organism |
|---|---|
| maltose-binding protein Trap column chromatography and Superdex 200 gel filtration | Laminaria digitata |
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-D-glucose 1-phosphate | - |
Laminaria digitata | D-glucose 6-phosphate | - |
? | |
| alpha-D-mannose 1-phosphate | - |
Laminaria digitata | D-mannose 6-phosphate | - |
? |
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 92180, maltose-binding protein-tagged enzyme, SDS-PAGE | Laminaria digitata |
| Synonyms | Comment | Organism |
|---|---|---|
| 10L6AlgC | bifunctional enzyme with phosphomannomutase/phosphoglucomutase activities | Laminaria digitata |
| PGM | - |
Laminaria digitata |
| PMM | - |
Laminaria digitata |
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
- |
Laminaria digitata |
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 50 | more than 50% activity between 25 and 50°C | Laminaria digitata |
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | 70 | the enzyme is stable at 45°C, with a reduction in relative phosphoglucomutase activity of 61.36%. 19.7, 7.17, 1.43, and 0.72%, respectively, being observed for every 5°C increase in temperature up to 70°C. In contrast, the phosphomannomutase activity is slightly less influenced by increases in temperature, with relative activities being reduced to 93.84, 51.66, 5.21, 4.98, and 3.79%, respectively, over the sample temperature range | Laminaria digitata |
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Laminaria digitata |
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | 8.5 | more than 50% activity between pH 7.5 and 8.5 | Laminaria digitata |