Literature summary for 2.4.1.266 extracted from

Fernandes, C.; Mendes, V.; Costa, J.; Empadinhas, N.; Jorge, C.; Lamosa, P.; Santos, H.; da Costa, M.S.
Two alternative pathways for the synthesis of the rare compatible solute mannosylglucosylglycerate in Petrotoga mobilis (2010), J. Bacteriol., 192, 1624-1633.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Petrotoga mobilis

Inhibitors

Inhibitors	Comment	Organism	Structure
3-phospho-D-glycerate	progressively inhibitory above 5 mM	Petrotoga mobilis
ADP	strong inhibitor	Petrotoga mobilis
EDTA	0.1 mM, completely inhibits the enzyme activity	Petrotoga mobilis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.5	-	3-phospho-D-glycerate	pH 7.0, 70°C	Petrotoga mobilis
0.7	-	3-phospho-D-glycerate	pH 7.0, 60°C	Petrotoga mobilis
0.9	-	UDP-glucose	pH 7.0, 70°C	Petrotoga mobilis
1	-	UDP-glucose	pH 7.0, 60°C	Petrotoga mobilis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) is dependent on divalent cations for activity: Co2+, Mn2+, Ni2+, Mg2+, and Zn2+. Co2+ (5 mM) has a more pronounced stimulatory effect	Petrotoga mobilis
Mg2+	the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) is dependent on divalent cations for activity: Co2+, Mn2+, Ni2+, Mg2+, and Zn2+. Co2+ (5 mM) has a more pronounced stimulatory effect	Petrotoga mobilis
Mn2+	the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) is dependent on divalent cations for activity: Co2+, Mn2+, Ni2+, Mg2+, and Zn2+. Co2+ (5 mM) has a more pronounced stimulatory effect	Petrotoga mobilis
Ni2+	the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) is dependent on divalent cations for activity: Co2+, Mn2+, Ni2+, Mg2+, and Zn2+. Co2+ (5 mM) has a more pronounced stimulatory effect	Petrotoga mobilis
Zn2+	the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) is dependent on divalent cations for activity: Co2+, Mn2+, Ni2+, Mg2+, and Zn2+. Co2+ (5 mM) has a more pronounced stimulatory effect	Petrotoga mobilis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
37100	-	2 * 37100, calculated from sequence	Petrotoga mobilis
80000	-	gel filtration	Petrotoga mobilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
UDP-glucose + 3-phospho-D-glycerate	Petrotoga mobilis	the enzyme is involved in the phosphorylating pathway for synthesis of the solute mannosylglucosylglycerate. In Petrotoga mobilis two alternative pathways for the synthesis of mannosylglucosylglycerate are proposed. The first one is a a phosphorylating pathway (with a phosphorylated intermediate) from 3-phosphoglycerate and UDP-glucose to the final solute. The second nonphosphorylating pathway (no phosphorylated intermediates) could represent an alternative route for the synthesis of mannosylglucosylglycerate in Petrotoga mobilis that could lead to the direct conversion of glucosylglycerate and GDP-mannose to mannosylglucosylglycerate. Pathway multiplicity likely reflects a crucial role for mannosylglucosylglycerate in the physiology of Petrotoga mobilis mobilis during stress adaptation	UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate	-	?

Organism

Organism	UniProt	Comment	Textmining
Petrotoga mobilis	A9BHI9	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Petrotoga mobilis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ADP-glucose + 3-phospho-D-glycerate	UDP-glucose is the preferred substrate, but it could be partially replaced by ADP-glucose. D-3-phosphoglycerate is the only acceptor for the synthesis of glucosyl-3-phosphoglycerate	Petrotoga mobilis	ADP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate	-	?
UDP-glucose + 3-phospho-D-glycerate	the enzyme is involved in the phosphorylating pathway for synthesis of the solute mannosylglucosylglycerate. In Petrotoga mobilis two alternative pathways for the synthesis of mannosylglucosylglycerate are proposed. The first one is a a phosphorylating pathway (with a phosphorylated intermediate) from 3-phosphoglycerate and UDP-glucose to the final solute. The second nonphosphorylating pathway (no phosphorylated intermediates) could represent an alternative route for the synthesis of mannosylglucosylglycerate in Petrotoga mobilis that could lead to the direct conversion of glucosylglycerate and GDP-mannose to mannosylglucosylglycerate. Pathway multiplicity likely reflects a crucial role for mannosylglucosylglycerate in the physiology of Petrotoga mobilis mobilis during stress adaptation	Petrotoga mobilis	UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate	-	?
UDP-glucose + 3-phospho-D-glycerate	UDP-glucose is the preferred substrate, but it could be partially replaced by ADP-glucose. D-3-phosphoglycerate is the only acceptor for the synthesis of glucopyranosyl-3-phosphoglycerate	Petrotoga mobilis	UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 37100, calculated from sequence	Petrotoga mobilis

Synonyms

Synonyms	Comment	Organism
GpgS	-	Petrotoga mobilis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
70	-	-	Petrotoga mobilis

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
60	75	60°C: about 85% of maximal activity, 75°C: about 60% of maximal activity	Petrotoga mobilis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
60	-	half-life: 6 min, addition of Co2+ had a negligible stabilizing effect, addition of both substrates increased the half-life of the enzyme to about 16 min	Petrotoga mobilis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	60°C	Petrotoga mobilis

pH Range

pH Minimum	pH Maximum	Comment	Organism
6	8	pH 6.0: about 80% of maximal activity, pH 8.0: about 50% of maximal activity	Petrotoga mobilis

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Release 2023.1 (January 2023)