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Literature summary extracted from

  • Empadinhas, N.; Albuquerque, L.; Costa, J.; Zinder, S.H.; Santos, M.A.; Santos, H.; da Costa, M.S.
    A gene from the mesophilic bacterium Dehalococcoides ethenogenes encodes a novel mannosylglycerate synthase (2004), J. Bacteriol., 186, 4075-4084.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.217 gene mgsD, DNA and amino acid sequence determination and analysis, genetic organization, overexpression of the holoenzyme and of the isolated mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase domains of the bifunctional enzyme in Escherichia coli, the recombinant Escherichia coli strain does not accumulate mannosylglycerate, expression of active bifunctional enzyme in Saccharomyces cerevisiae Dehalococcoides mccartyi

General Stability

EC Number General Stability Organism
2.4.1.217 recombinant monofunctional mannosyl-3-phosphoglycerate synthase domain is unstable Dehalococcoides mccartyi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.217 0.7
-
 GDP-mannose pH 7.5, 30°C, recombinant holoenzyme Dehalococcoides mccartyi
2.4.1.217 2.18
-
 3-phospho-D-glycerate pH 7.5, 30°C, recombinant holoenzyme Dehalococcoides mccartyi

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.217 Co2+ most effective in enzyme activation Dehalococcoides mccartyi
2.4.1.217 Mg2+ activates Dehalococcoides mccartyi
2.4.1.217 Mn2+ activates Dehalococcoides mccartyi
2.4.1.217 additional information enzyme requires divalent cations, Co2+ is preferred and can partially be substituted by Mg2+ or Mn2+, no activation by other cations Dehalococcoides mccartyi

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.217 50000
-
 x * 78000, recombinant bifunctional holoenzyme, SDS-PAGE, x * 50000, about, recombinant mannosyl-3-phosphoglycerate synthase domain, SDS-PAGE Dehalococcoides mccartyi
2.4.1.217 78000
-
 x * 78000, recombinant bifunctional holoenzyme, SDS-PAGE, x * 50000, about, recombinant mannosyl-3-phosphoglycerate synthase domain, SDS-PAGE Dehalococcoides mccartyi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.217 GDP-mannose + 3-phospho-D-glycerate Dehalococcoides mccartyi
-
 GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
 ?
2.4.1.217 additional information Dehalococcoides mccartyi the bifunctional enzyme catalyzes the consecutive synthesis and dephosphorylation of mannosyl-3-phosphoglycerate in mannosylglycerate biosynthesis, enzyme evolution ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.217 Dehalococcoides mccartyi
-
 gene mgsD, bifunctional enzyme
-
2.4.1.217 no activity in Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.217 recombinant enzyme and enzyme domains from Escherichia coli Dehalococcoides mccartyi

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.1.217 GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate the enzyme is bifunctional exhibiting both mannosyl-3-phosphoglycerate synthase, EC 2.4.1.217, and mannosyl-3-phosphoglycerate phosphatase, EC 3.1.3.70, activities, catalyzing the consecutive synthesis and dephosphorylation of mannosyl-3-phosphoglycerate in mannosylglycerate biosynthesis Dehalococcoides mccartyi
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.217 GDP-mannose + 3-phospho-D-glycerate
-
 Dehalococcoides mccartyi GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
 ?
2.4.1.217 GDP-mannose + 3-phospho-D-glycerate the enzyme is absolute specific for GDP-mannose and 3-phospho-D-glycerate as substrates Dehalococcoides mccartyi GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
 ?
2.4.1.217 additional information the bifunctional enzyme catalyzes the consecutive synthesis and dephosphorylation of mannosyl-3-phosphoglycerate in mannosylglycerate biosynthesis, enzyme evolution Dehalococcoides mccartyi ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.217 ? x * 78000, recombinant bifunctional holoenzyme, SDS-PAGE, x * 50000, about, recombinant mannosyl-3-phosphoglycerate synthase domain, SDS-PAGE Dehalococcoides mccartyi

Synonyms

EC Number Synonyms Comment Organism
2.4.1.217 mannosylglycerate synthase
-
 Dehalococcoides mccartyi
2.4.1.217 MGSD
-
 Dehalococcoides mccartyi
2.4.1.217 MPGS mannosyl-3-phosphoglycerate synthase domain of the bifunctional enzyme Dehalococcoides mccartyi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.217 50
-
 recombinant enzyme Dehalococcoides mccartyi

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.4.1.217 10 60 temperature-profile, recombinant enzyme Dehalococcoides mccartyi

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.1.217 3.9
-
 3-phospho-D-glycerate pH 7.5, 30°C, recombinant holoenzyme Dehalococcoides mccartyi
2.4.1.217 3.9
-
 GDP-mannose pH 7.5, 30°C, recombinant holoenzyme Dehalococcoides mccartyi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.217 7
-
 recombinant enzyme Dehalococcoides mccartyi

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.4.1.217 5.5 8.5 pH-profile Dehalococcoides mccartyi