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Literature summary for 2.7.7.13 extracted from
- Phosphomannose isomerase/GDP-mannose pyrophosphorylase from Pyrococcus furiosus: a thermostable biocatalyst for the synthesis of guanidinediphosphate-activated and mannose-containing sugar nucleotides (2009), Org. Biomol. Chem., 7, 2135-2139.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21 Codon Plus (DE3)-RIPL strain | Pyrococcus furiosus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.062 | - |
alpha-D-mannose 1-phosphate | cosubstrate GTP, Vmax: 0.63 micromol/min/mg | Pyrococcus furiosus |  |
| 0.072 | - |
alpha-D-mannose 1-phosphate | cosubstrate GTP, Vmax: 50 micromol/min/mg | Pyrococcus furiosus | |
| 0.094 | - |
alpha-D-glucose 1-phosphate | cosubstrate GTP, Vmax: 14 micromol/min/mg | Pyrococcus furiosus | |
| 0.12 | - |
alpha-D-mannose 1-phosphate | cosubstrate ATP, Vmax: 11 micromol/min/mg | Pyrococcus furiosus | |
| 0.15 | - |
alpha-D-mannose 1-phosphate | cosubstrate UTP, Vmax: 14 micromol/min/mg | Pyrococcus furiosus | |
| 0.16 | - |
alpha-D-mannose 1-phosphate | cosubstrate CTP, Vmax: 11 micromol/min/mg | Pyrococcus furiosus | |
| 0.19 | - |
alpha-D-mannose 1-phosphate | cosubstrate TTP, Vmax: 6 micromol/min/mg | Pyrococcus furiosus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+ | Pyrococcus furiosus | |
| Co2+ | the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+ | Pyrococcus furiosus | |
| Cu2+ | the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+ | Pyrococcus furiosus | |
| Mg2+ | no product formation is observed in the absence of sugar phosphates, Mg2+ or NTP. The enzyme activity remains high between 2-15 mM concentrations. The efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+ | Pyrococcus furiosus | |
| Mn2+ | the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+ | Pyrococcus furiosus | |
| Zn2+ | the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+ | Pyrococcus furiosus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 53000 | - |
SDS-PAGE | Pyrococcus furiosus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Pyrococcus furiosus | truncated GDP-mannose pyrophosphorylase domain of the whole length enzyme shows almost 100fold less sugar nucleotidyltransferase activity with only GTP and mannose 1-phosphate as substrates. The enzyme accepts all five naturally occurring NTPs (ATP, CTP, GTP, dTTP and UTP) and a range of sugar-1-phosphates (glucose-, mannose-, galactose-, glucosamine-, N-acetylglucosamine- and fucose-1-phosphate) | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | - |
DSM 3638 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni-affinity column | Pyrococcus furiosus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + alpha-D-mannose 1-phosphate | - |
Pyrococcus furiosus | alpha-ADP-mannose + diphosphate | - |
? | |
| CTP + alpha-D-mannose 1-phosphate | - |
Pyrococcus furiosus | alpha-CDP-mannose + diphosphate | - |
? | |
| dTTP + alpha-D-mannose 1-phosphate | - |
Pyrococcus furiosus | alpha-dTDP-mannose + diphosphate | - |
? | |
| GTP + alpha-D-galactose 1-phosphate | - |
Pyrococcus furiosus | GDP-alpha-D-galactose + diphosphate | - |
? | |
| GTP + alpha-D-glucosamine 1-phosphate | - |
Pyrococcus furiosus | alpha-GDP-glucosamine + diphosphate | - |
? | |
| GTP + alpha-D-glucose 1-phosphate | - |
Pyrococcus furiosus | diphosphate + GDP-glucose | - |
? | |
| GTP + alpha-D-glucose 1-phosphate | - |
Pyrococcus furiosus | alpha-GDP-glucose + diphosphate | - |
? | |
| GTP + alpha-D-mannose 1-phosphate | - |
Pyrococcus furiosus | diphosphate + GDP-mannose | - |
? | |
| GTP + alpha-D-mannose 1-phosphate | in the presence of diphosphatase | Pyrococcus furiosus | alpha-GDP-mannose + diphosphate | - |
r | |
| GTP + alpha-L-fucose 1-phosphate | - |
Pyrococcus furiosus | GDP-alpha-L-fucose + diphosphate | - |
? | |
| GTP + alpha-N-acetyl-D-glucosamine 1-phosphate | - |
Pyrococcus furiosus | GDP-alpha-N-acetyl-D-glucosamine + diphosphate | - |
? | |
| additional information | truncated GDP-mannose pyrophosphorylase domain of the whole length enzyme shows almost 100fold less sugar nucleotidyltransferase activity with only GTP and mannose 1-phosphate as substrates. The enzyme accepts all five naturally occurring NTPs (ATP, CTP, GTP, dTTP and UTP) and a range of sugar-1-phosphates (glucose-, mannose-, galactose-, glucosamine-, N-acetylglucosamine- and fucose-1-phosphate) | Pyrococcus furiosus | ? | - |
? | |
| UTP + alpha-D-mannose 1-phosphate | - |
Pyrococcus furiosus | alpha-UDP-mannose + diphosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GDP-mannose pyrophosphorylase | type II phosphomannose isomerase, bifunctional phosphomannose isomerase/GDP-mannose pyrophosphorylase (manC), with both PMI (E.C. 5.3.1.8) and GMP (E.C.2.7.7.13) activities | Pyrococcus furiosus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
- |
Pyrococcus furiosus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
- |
100 | temperature dependence of the enzymatic activity is analyzed between 0 and 100°C | Pyrococcus furiosus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
hyperthermostable, the enzyme remains stable for over 300 min without losing its activity when stored at 80°C | Pyrococcus furiosus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 8 | recombinant protein exhibits relatively high activity around pH 6.0 and 9.5, with a maximum in the range of pH 7.0-8.0 in phosphate buffer | Pyrococcus furiosus |
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Release 2023.1 (January 2023)
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