Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Petrotoga mobilis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
3-phospho-D-glycerate | progressively inhibitory above 5 mM | Petrotoga mobilis | |
ADP | strong inhibitor | Petrotoga mobilis | |
EDTA | 0.1 mM, completely inhibits the enzyme activity | Petrotoga mobilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.5 | - |
3-phospho-D-glycerate | pH 7.0, 70°C | Petrotoga mobilis | |
0.7 | - |
3-phospho-D-glycerate | pH 7.0, 60°C | Petrotoga mobilis | |
0.9 | - |
UDP-glucose | pH 7.0, 70°C | Petrotoga mobilis | |
1 | - |
UDP-glucose | pH 7.0, 60°C | Petrotoga mobilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) is dependent on divalent cations for activity: Co2+, Mn2+, Ni2+, Mg2+, and Zn2+. Co2+ (5 mM) has a more pronounced stimulatory effect | Petrotoga mobilis | |
Mg2+ | the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) is dependent on divalent cations for activity: Co2+, Mn2+, Ni2+, Mg2+, and Zn2+. Co2+ (5 mM) has a more pronounced stimulatory effect | Petrotoga mobilis | |
Mn2+ | the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) is dependent on divalent cations for activity: Co2+, Mn2+, Ni2+, Mg2+, and Zn2+. Co2+ (5 mM) has a more pronounced stimulatory effect | Petrotoga mobilis | |
Ni2+ | the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) is dependent on divalent cations for activity: Co2+, Mn2+, Ni2+, Mg2+, and Zn2+. Co2+ (5 mM) has a more pronounced stimulatory effect | Petrotoga mobilis | |
Zn2+ | the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) is dependent on divalent cations for activity: Co2+, Mn2+, Ni2+, Mg2+, and Zn2+. Co2+ (5 mM) has a more pronounced stimulatory effect | Petrotoga mobilis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
37100 | - |
2 * 37100, calculated from sequence | Petrotoga mobilis |
80000 | - |
gel filtration | Petrotoga mobilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-glucose + 3-phospho-D-glycerate | Petrotoga mobilis | the enzyme is involved in the phosphorylating pathway for synthesis of the solute mannosylglucosylglycerate. In Petrotoga mobilis two alternative pathways for the synthesis of mannosylglucosylglycerate are proposed. The first one is a a phosphorylating pathway (with a phosphorylated intermediate) from 3-phosphoglycerate and UDP-glucose to the final solute. The second nonphosphorylating pathway (no phosphorylated intermediates) could represent an alternative route for the synthesis of mannosylglucosylglycerate in Petrotoga mobilis that could lead to the direct conversion of glucosylglycerate and GDP-mannose to mannosylglucosylglycerate. Pathway multiplicity likely reflects a crucial role for mannosylglucosylglycerate in the physiology of Petrotoga mobilis mobilis during stress adaptation | UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Petrotoga mobilis | A9BHI9 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme | Petrotoga mobilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP-glucose + 3-phospho-D-glycerate | UDP-glucose is the preferred substrate, but it could be partially replaced by ADP-glucose. D-3-phosphoglycerate is the only acceptor for the synthesis of glucosyl-3-phosphoglycerate | Petrotoga mobilis | ADP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate | - |
? | |
UDP-glucose + 3-phospho-D-glycerate | the enzyme is involved in the phosphorylating pathway for synthesis of the solute mannosylglucosylglycerate. In Petrotoga mobilis two alternative pathways for the synthesis of mannosylglucosylglycerate are proposed. The first one is a a phosphorylating pathway (with a phosphorylated intermediate) from 3-phosphoglycerate and UDP-glucose to the final solute. The second nonphosphorylating pathway (no phosphorylated intermediates) could represent an alternative route for the synthesis of mannosylglucosylglycerate in Petrotoga mobilis that could lead to the direct conversion of glucosylglycerate and GDP-mannose to mannosylglucosylglycerate. Pathway multiplicity likely reflects a crucial role for mannosylglucosylglycerate in the physiology of Petrotoga mobilis mobilis during stress adaptation | Petrotoga mobilis | UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate | - |
? | |
UDP-glucose + 3-phospho-D-glycerate | UDP-glucose is the preferred substrate, but it could be partially replaced by ADP-glucose. D-3-phosphoglycerate is the only acceptor for the synthesis of glucopyranosyl-3-phosphoglycerate | Petrotoga mobilis | UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 37100, calculated from sequence | Petrotoga mobilis |
Synonyms | Comment | Organism |
---|---|---|
GpgS | - |
Petrotoga mobilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
- |
Petrotoga mobilis |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | 75 | 60°C: about 85% of maximal activity, 75°C: about 60% of maximal activity | Petrotoga mobilis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | - |
half-life: 6 min, addition of Co2+ had a negligible stabilizing effect, addition of both substrates increased the half-life of the enzyme to about 16 min | Petrotoga mobilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
60°C | Petrotoga mobilis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 8 | pH 6.0: about 80% of maximal activity, pH 8.0: about 50% of maximal activity | Petrotoga mobilis |