EC Number   |
Metals/Ions |
Reference |
|---|
    3.1.3.85 | Co2+ |
at 50°C, divalent cations are absolutely required for GpgP activity with 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate as the substrate. However, when 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate is the substrate, 3% activity is detected without cations, and the preferred metal ion with both substrates is Co2+ (10 mM). At 30°C, GpgP retains 37% of its enzyme activity towards 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate and 12% activity towards 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate in a reaction mixture without cations compared to the activity with 10 mM K+ and Co2+ |
680455 |
| 3.1.3.85 | Co2+ |
stimulates activity with 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate or 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate |
674318 |
| 3.1.3.85 | K+ |
at 30°C, GpgP retains 37% of its enzyme activity towards 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate and 12% activity towards 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate in a reaction mixture without cations compared to the activity with 10 mM K+ and Co2+. Potassium chloride, in the concentration range of 10 to 100 mM, stimulates enzyme activity about 40% at 50°C, but only when 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate is the substrate. However, at 30°C, K+ has a stimulatory effect towards 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate, but not with 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate as the substrate |
680455 |
| 3.1.3.85 | Mg2+ |
0.1 mM is sufficient to promote the dephosphorylation of 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate. Maximal activation of dephosphorylation of 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate at 0.1 mM Mg2+. Maximal activation of dephosphorylation of 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate at 10 mM Mg2+ |
674318 |
| 3.1.3.85 | Mg2+ |
at 50°C, divalent cations are absolutely required for GpgP activity with 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate as the substrate. Mg2+ and, to a lesser extent, Ni2+ can replace Co2+ |
680455 |
| 3.1.3.85 | Mn2+ |
enzyme activity is not detected with Mn2+ when 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate is used, while Mn2+ had a strong stimulatory effect (85% of the maximal activity with Co2+) with 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate |
680455 |
| 3.1.3.85 | Mn2+ |
stimulates activity with 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate or 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate |
674318 |
| 3.1.3.85 | more |
Ca2+, Sr2+, Ba2+, Cu2+, and Zn2+, have no effect on GpgP activity at any concentration |
680455 |
| 3.1.3.85 | more |
K+, Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+, do not stimulate GpgP activity at any concentration |
674318 |
| 3.1.3.85 | Ni2+ |
at 50°C, divalent cations are absolutely required for GpgP activity with 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate as the substrate. Mg2+ and, to a lesser extent, Ni2+ can replace Co2+ |
680455 |
