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Literature summary for 2.4.1.217 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)

Cloned (Comment) Organism
overexpression in Escherichia coli Pyrococcus horikoshii

Inhibitors

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.14
-
3-phospho-D-glycerate
-
Pyrococcus horikoshii
0.17
-
GDPmannose
-
Pyrococcus horikoshii

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activity in absence is 46% of that in presence of 15 mM Mg2+ Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GDPmannose + 3-phospho-D-glycerate transfer of the mannosyl group with retention of configuration Pyrococcus horikoshii GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
?
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 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90 100 recombinant enzyme Pyrococcus horikoshii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
80 105 80°C: about 60% of maximal activity, 105°C: about 70% of maximal activity Pyrococcus horikoshii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
98
-
half-life: 16 min Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.4 7.4 recombinant enzyme Pyrococcus horikoshii

pH Range

pH Minimum pH Maximum Comment Organism
6 8 pH 6.0: about 60% of maximal activity, pH 8.0: about 75% of maximal activity Pyrococcus horikoshii