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Literature summary extracted from

  • Empadinhas, N.; Marugg, J.D.; Borges, N.; Santos, H.; Da Costa, M.S.
    Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes (2001), J. Biol. Chem., 276, 43580-43588.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.217 overexpression in Escherichia coli Pyrococcus horikoshii
3.1.3.70
-
 Pyrococcus horikoshii

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.217 KCl 150 mM, 18% inhibition Pyrococcus horikoshii
2.4.1.217 NaCl 150 mM, 35% inhibition Pyrococcus horikoshii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.217 0.14
-
 3-phospho-D-glycerate
-
 Pyrococcus horikoshii
2.4.1.217 0.17
-
 GDPmannose
-
 Pyrococcus horikoshii
3.1.3.70 0.134
-
 2(alpha-D-mannosyl)-3-phosphoglycerate
-
 Pyrococcus horikoshii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.217 Mg2+ activity in absence is 46% of that in presence of 15 mM Mg2+ Pyrococcus horikoshii
3.1.3.70 Mg2+ activity without Mg2+ is 58% of the activity with 15 mM Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.217 GDPmannose + 3-phospho-D-glycerate Pyrococcus horikoshii involved in a pathway for synthesis of mannosylglycerate GDP + 2-(1-D-mannosyl)-3-phosphoglycerate mannosyl-3-phosphoglycerate is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70, producing mannosylglycerate ?
2.7.7.22 GDPmannose + phosphate Pyrococcus horikoshii reverse reaction involved in synthesis of the compatible solute alpha-mannosylglycerate GDP + mannose 1-phosphate
-
 r
3.1.3.70 2(alpha-D-mannosyl)-3-phosphoglycerate + H2O Pyrococcus horikoshii enzyme is involved in biosynthesis of alpha-mannosylglycerate 2(alpha-D-mannosyl)-D-glycerate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.217 Pyrococcus horikoshii
-
-
-
2.7.7.22 Pyrococcus horikoshii O58649 hyperthermophilic archeon
-
3.1.3.70 Pyrococcus horikoshii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.217
-
 Pyrococcus horikoshii
3.1.3.70
-
 Pyrococcus horikoshii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.217 GDPmannose + 3-phospho-D-glycerate transfer of the mannosyl group with retention of configuration Pyrococcus horikoshii GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
 ?
2.4.1.217 GDPmannose + 3-phospho-D-glycerate involved in a pathway for synthesis of mannosylglycerate Pyrococcus horikoshii GDP + 2-(1-D-mannosyl)-3-phosphoglycerate mannosyl-3-phosphoglycerate is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70, producing mannosylglycerate ?
2.7.7.22 GDPmannose + phosphate
-
 Pyrococcus horikoshii GDP + mannose 1-phosphate
-
 r
2.7.7.22 GDPmannose + phosphate reverse reaction involved in synthesis of the compatible solute alpha-mannosylglycerate Pyrococcus horikoshii GDP + mannose 1-phosphate
-
 r
3.1.3.70 2(alpha-D-mannosyl)-3-phosphoglycerate + H2O enzyme is highly specific for D-mannosyl-3-phosphoglycerate Pyrococcus horikoshii 2(alpha-D-mannosyl)-D-glycerate + phosphate
-
 ?
3.1.3.70 2(alpha-D-mannosyl)-3-phosphoglycerate + H2O enzyme is involved in biosynthesis of alpha-mannosylglycerate Pyrococcus horikoshii 2(alpha-D-mannosyl)-D-glycerate + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.22 More bifunctional enzyme, phosphomannose isomerase activity as well as mannose 1-phosphate guanylyltransferase activity Pyrococcus horikoshii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.217 90 100 recombinant enzyme Pyrococcus horikoshii
3.1.3.70 95 100
-
 Pyrococcus horikoshii

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.4.1.217 80 105 80°C: about 60% of maximal activity, 105°C: about 70% of maximal activity Pyrococcus horikoshii
3.1.3.70 70 108 70°C: about 45% of maximal activity, 108°C: about 20% of maximal activity Pyrococcus horikoshii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.217 98
-
 half-life: 16 min Pyrococcus horikoshii
3.1.3.70 98
-
 half-life: 15.6 min Pyrococcus horikoshii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.217 6.4 7.4 recombinant enzyme Pyrococcus horikoshii
3.1.3.70 5.2 6.4
-
 Pyrococcus horikoshii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.4.1.217 6 8 pH 6.0: about 60% of maximal activity, pH 8.0: about 75% of maximal activity Pyrococcus horikoshii
3.1.3.70 4.2 7.5 pH 4.2: 60% of maximal actuvity, pH 7.5: about 45% of maximal activity Pyrococcus horikoshii