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Literature summary for 2.4.1.266 extracted from
- Glucosylglycerate biosynthesis in the deepest lineage of the bacteria: characterization of the thermophilic proteins GpgS and GpgP from Persephonella marina (2007), J. Bacteriol., 189, 1648-1654.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpressed as His-tagged proteins in Escherichia coli | Persephonella marina |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | - |
Persephonella marina |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.09 | - |
3-phospho-D-glycerate | pH 8.0, 70°C | Persephonella marina | |
| 0.25 | - |
3-phospho-D-glycerate | pH 8.0, 85°C | Persephonella marina | |
| 0.3 | - |
3-phospho-D-glycerate | pH 8.0, 90°C | Persephonella marina | |
| 1.47 | - |
UDP-glucose | pH 8.0, 70°C | Persephonella marina | |
| 1.55 | - |
UDP-glucose | pH 8.0, 85°C | Persephonella marina | |
| 1.58 | - |
UDP-glucose | pH 8.0, 90°C | Persephonella marina | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | strictly dependent on divalent cations, in the following order of efficiency: Mn2+, Co2+, Mg2+, Ni2+ | Persephonella marina | |
| Mg2+ | strictly dependent on divalent cations, in the following order of efficiency: Mn2+, Co2+, Mg2+, Ni2+ | Persephonella marina | |
| Mn2+ | strictly dependent on divalent cations, in the following order of efficiency: Mn2+, Co2+, Mg2+, Ni2+. The maximum activation is obtained with 1.0 mM Mn2+. 50% of the maximum activity is reached with 0.19 mM Mn2+ | Persephonella marina | |
| additional information | K+, Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+, do not stimulate GpgS activity at any concentration | Persephonella marina | |
| Ni2+ | strictly dependent on divalent cations, in the following order of efficiency: Mn2+, Co2+, Mg2+, Ni2+. The specific activities obtained with Ni2+ are similar for both the His-tagged enzyme and the nontagged recombinant enzyme | Persephonella marina | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 46700 | - |
2 * 46700, calculated from sequence | Persephonella marina |
| 105400 | - |
gel filtration | Persephonella marina |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-glucose + 3-phospho-D-glycerate | Persephonella marina | in Persephonella marina two pathways for synthesis of glucosylglycerate are present: 1. the single-step pathway in with glucosylglycerate synthase (Ggs) catalyzes the synthesis of 2-O-(alpha-D-glucosyl)-D-glycerate in one-step fop, ADP-glucose and D-glycerate, and 2. the two-step pathway in which glucosyl-3-phosphoglycerate synthase (GpgS) catalyzes the conversion of NDP-glucose and D-3-phosphoglycerate into glucosyl-3-phosphoglycerate, which is then converted to 2-O-(alpha-D-glucosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase (GpgP) | UDP + 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Persephonella marina | A9QXB4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant GpgS protein | Persephonella marina |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 5 | - |
substrate: TDP-glucose, pH 8.0, 90°C | Persephonella marina |
| 10 | - |
substrate: ADP-glucose, pH 8.0, 90°C | Persephonella marina |
| 41 | - |
substrate: GDP-glucose, pH 8.0, 90°C | Persephonella marina |
| 94 | - |
substrate: UDP-glucose, pH 8.0, 90°C | Persephonella marina |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP-glucose + 3-phospho-D-glycerate | the recombinant GpgS protein of Persephonella marina catalyzes the synthesis of 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate from UDP-glucose, GDP-glucose, ADP-glucose, and TDP-glucose (in order of decreasing efficiency) and from D-3-phosphoglycerate | Persephonella marina | ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate | - |
? | |
| GDP-glucose + 3-phospho-D-glycerate | the recombinant GpgS protein of Persephonella marina catalyzes the synthesis of 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate from UDP-glucose, GDP-glucose, ADP-glucose, and TDP-glucose (in order of decreasing efficiency) and from D-3-phosphoglycerate | Persephonella marina | GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate | - |
? | |
| additional information | no activity with: ADP-ribose, UDP-acetylgalactosamine, UDP-glucuronic acid, UDP-galactose, GDP-fucose, GDP-mannose, UDP-mannose or ADP-mannose | Persephonella marina | ? | - |
? | |
| TDP-glucose + 3-phospho-D-glycerate | the recombinant GpgS protein of Persephonella marina catalyzes the synthesis of 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate from UDP-glucose, GDP-glucose, ADP-glucose, and TDP-glucose (in order of decreasing efficiency) and from D-3-phosphoglycerate | Persephonella marina | TDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate | - |
? | |
| UDP-glucose + 3-phospho-D-glycerate | the recombinant GpgS protein of Persephonella marina catalyzes the synthesis of 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate from UDP-glucose, GDP-glucose, ADP-glucose, and TDP-glucose (in order of decreasing efficiency) and from D-3-phosphoglycerate | Persephonella marina | UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate | - |
? | |
| UDP-glucose + 3-phospho-D-glycerate | in Persephonella marina two pathways for synthesis of glucosylglycerate are present: 1. the single-step pathway in with glucosylglycerate synthase (Ggs) catalyzes the synthesis of 2-O-(alpha-D-glucosyl)-D-glycerate in one-step fop, ADP-glucose and D-glycerate, and 2. the two-step pathway in which glucosyl-3-phosphoglycerate synthase (GpgS) catalyzes the conversion of NDP-glucose and D-3-phosphoglycerate into glucosyl-3-phosphoglycerate, which is then converted to 2-O-(alpha-D-glucosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase (GpgP) | Persephonella marina | UDP + 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 46700, calculated from sequence | Persephonella marina |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GpgS | - |
Persephonella marina |
| GpgS protein | - |
Persephonella marina |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 90 | - |
- |
Persephonella marina |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | 100 | the enzyme is inactive at 40°C, 60°C: about 60% of maximal activity, 100°C: 33% of maximal activity | Persephonella marina |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
half-life is 14 min | Persephonella marina |
| 90 | - |
half-life is 2.3 min | Persephonella marina |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Persephonella marina |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | 9.5 | pH 7.5: about 60% of maximal activity, pH 9.5: about 80% of maximal activity | Persephonella marina |
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