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Literature summary extracted from

  • Mizanur, R.M.; Pohl, N.L.B.
    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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.13 expressed in Escherichia coli BL21 Codon Plus (DE3)-RIPL strain Pyrococcus furiosus
5.3.1.8 expressed in Escherichia coli BL21 Codon Plus (DE3)-RIPL strain Pyrococcus furiosus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.13 0.062
-
 alpha-D-mannose 1-phosphate cosubstrate GTP, Vmax: 0.63 micromol/min/mg Pyrococcus furiosus
2.7.7.13 0.072
-
 alpha-D-mannose 1-phosphate cosubstrate GTP, Vmax: 50 micromol/min/mg Pyrococcus furiosus
2.7.7.13 0.094
-
 alpha-D-glucose 1-phosphate cosubstrate GTP, Vmax: 14 micromol/min/mg Pyrococcus furiosus
2.7.7.13 0.12
-
 alpha-D-mannose 1-phosphate cosubstrate ATP, Vmax: 11 micromol/min/mg Pyrococcus furiosus
2.7.7.13 0.15
-
 alpha-D-mannose 1-phosphate cosubstrate UTP, Vmax: 14 micromol/min/mg Pyrococcus furiosus
2.7.7.13 0.16
-
 alpha-D-mannose 1-phosphate cosubstrate CTP, Vmax: 11 micromol/min/mg Pyrococcus furiosus
2.7.7.13 0.19
-
 alpha-D-mannose 1-phosphate cosubstrate TTP, Vmax: 6 micromol/min/mg Pyrococcus furiosus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.13 Ca2+ the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+ Pyrococcus furiosus
2.7.7.13 Co2+ the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+ Pyrococcus furiosus
2.7.7.13 Cu2+ the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+ Pyrococcus furiosus
2.7.7.13 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
2.7.7.13 Mn2+ the efficiency of the metal ions on the enzyme decreases in the following order Mg2+, Cu2+, Zn2+, Co2+, Ca2+, and Mn2+ Pyrococcus furiosus
2.7.7.13 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.7.13 53000
-
 SDS-PAGE Pyrococcus furiosus
5.3.1.8 53000
-
 SDS-PAGE Pyrococcus furiosus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.13 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

EC Number Organism UniProt Comment Textmining
2.7.7.13 Pyrococcus furiosus
-
 DSM 3638
-
5.3.1.8 Pyrococcus furiosus
-
 DSM 3638
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.13 Ni-affinity column Pyrococcus furiosus
5.3.1.8 Ni-affinity column Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.13 ATP + alpha-D-mannose 1-phosphate
-
 Pyrococcus furiosus alpha-ADP-mannose + diphosphate
-
 ?
2.7.7.13 CTP + alpha-D-mannose 1-phosphate
-
 Pyrococcus furiosus alpha-CDP-mannose + diphosphate
-
 ?
2.7.7.13 dTTP + alpha-D-mannose 1-phosphate
-
 Pyrococcus furiosus alpha-dTDP-mannose + diphosphate
-
 ?
2.7.7.13 GTP + alpha-D-galactose 1-phosphate
-
 Pyrococcus furiosus GDP-alpha-D-galactose + diphosphate
-
 ?
2.7.7.13 GTP + alpha-D-glucosamine 1-phosphate
-
 Pyrococcus furiosus alpha-GDP-glucosamine + diphosphate
-
 ?
2.7.7.13 GTP + alpha-D-glucose 1-phosphate
-
 Pyrococcus furiosus diphosphate + GDP-glucose
-
 ?
2.7.7.13 GTP + alpha-D-glucose 1-phosphate
-
 Pyrococcus furiosus alpha-GDP-glucose + diphosphate
-
 ?
2.7.7.13 GTP + alpha-D-mannose 1-phosphate
-
 Pyrococcus furiosus diphosphate + GDP-mannose
-
 ?
2.7.7.13 GTP + alpha-D-mannose 1-phosphate in the presence of diphosphatase Pyrococcus furiosus alpha-GDP-mannose + diphosphate
-
 r
2.7.7.13 GTP + alpha-L-fucose 1-phosphate
-
 Pyrococcus furiosus GDP-alpha-L-fucose + diphosphate
-
 ?
2.7.7.13 GTP + alpha-N-acetyl-D-glucosamine 1-phosphate
-
 Pyrococcus furiosus GDP-alpha-N-acetyl-D-glucosamine + diphosphate
-
 ?
2.7.7.13 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 ?
-
 ?
2.7.7.13 UTP + alpha-D-mannose 1-phosphate
-
 Pyrococcus furiosus alpha-UDP-mannose + diphosphate
-
 ?
5.3.1.8 alpha-D-fructose 6-phosphate
-
 Pyrococcus furiosus alpha-D-mannose 6-phosphate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.7.7.13 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
5.3.1.8 Phosphomannose isomerase 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]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.13 80
-
-
 Pyrococcus furiosus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.7.7.13
-
 100 temperature dependence of the enzymatic activity is analyzed between 0 and 100°C Pyrococcus furiosus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.7.13 80
-
 hyperthermostable, the enzyme remains stable for over 300 min without losing its activity when stored at 80°C Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.13 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