Literature summary for 2.4.1.217 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.

Search for more literature for 2.4.1.217

Cloned(Commentary)

Cloned (Comment)	Organism
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

Cloned (Comment)

Organism

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

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

KM Value [mM]

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

Metals/Ions

Metals/Ions	Comment	Organism
Co2+	most effective in enzyme activation	Dehalococcoides mccartyi
Mg2+	activates	Dehalococcoides mccartyi
Mn2+	activates	Dehalococcoides mccartyi
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]

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

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

Organism

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

Purification (Commentary)

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

Reaction

Reaction	Comment	Organism	Reaction ID
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)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

pH Range

pH Minimum	pH Maximum	Comment	Organism
5.5	8.5	pH-profile	Dehalococcoides mccartyi