Literature summary 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.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
2.4.1.266	expression in Escherichia coli	Petrotoga mobilis
2.4.1.268	expression in Escherichia coli	Petrotoga mobilis
2.4.1.270	expression in Escherichia coli	Petrotoga mobilis
3.1.3.B8	expression in Escherichia coli	Petrotoga mobilis

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.4.1.266	3-phospho-D-glycerate	progressively inhibitory above 5 mM	Petrotoga mobilis
2.4.1.266	ADP	strong inhibitor	Petrotoga mobilis
2.4.1.266	EDTA	0.1 mM, completely inhibits the enzyme activity	Petrotoga mobilis
2.4.1.268	EDTA	1 mM, complete inhibition	Petrotoga mobilis
2.4.1.268	Zn2+	strong inhibition	Petrotoga mobilis
2.4.1.270	EDTA	in the presence of 0.1, 2.0, or 5.0 mM EDTA, the enzyme retaines 85, 30, and 23% of its maximal activity, respectively	Petrotoga mobilis
3.1.3.B8	EDTA	addition of 20 mM EDTA leads to a residual activity of 14% in the presence of 20 mM Mn2+	Petrotoga mobilis

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
2.4.1.266	0.5	-	3-phospho-D-glycerate	pH 7.0, 70°C	Petrotoga mobilis
2.4.1.266	0.7	-	3-phospho-D-glycerate	pH 7.0, 60°C	Petrotoga mobilis
2.4.1.266	0.9	-	UDP-glucose	pH 7.0, 70°C	Petrotoga mobilis
2.4.1.266	1	-	UDP-glucose	pH 7.0, 60°C	Petrotoga mobilis
2.4.1.268	0.9	-	D-glycerate	pH 6.7, 60°C, native enzyme	Petrotoga mobilis
2.4.1.268	1.9	-	D-glycerate	pH 6.7, 70°C, native enzyme	Petrotoga mobilis
2.4.1.268	2	-	ADP-glucose	pH 6.7, 70°C, native enzyme	Petrotoga mobilis
2.4.1.268	2.9	-	ADP-glucose	pH 6.7, 60°C, native enzyme	Petrotoga mobilis
2.4.1.268	3.4	-	D-glycerate	pH 6.7, 60°C, recombinant enzyme	Petrotoga mobilis
2.4.1.268	9.3	-	ADP-glucose	pH 6.7, 60°C, recombinant enzyme	Petrotoga mobilis
2.4.1.270	0.8	-	2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate	pH 8.5, 60°C	Petrotoga mobilis
2.4.1.270	1	-	GDP-mannose	pH 8.5, 60°C	Petrotoga mobilis
3.1.3.B8	0.5	-	2-O-[2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl]-3-phospho-D-glycerate	60°C, pH 7.0, partially purified enzyme	Petrotoga mobilis
3.1.3.B8	2.6	-	2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate	60°C, pH 7.0, partially purified enzyme	Petrotoga mobilis
3.1.3.B8	2.8	-	2-O-alpha-D-mannopyranosyl-3-phosphoglycerate	60°C, pH 7.0, partially purified enzyme	Petrotoga mobilis

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
2.4.1.266	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
2.4.1.266	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
2.4.1.266	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
2.4.1.266	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
2.4.1.266	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
2.4.1.268	Mn2+	20 mM, stimulation. No stimulation by Mg2+, Ni2+, Co2+	Petrotoga mobilis
2.4.1.268	additional information	NaCl and KCl have no effect on Ggs activity	Petrotoga mobilis
2.4.1.270	Ca2+	not strictly dependent on divalent cations, but the presence of 1 mM Mn2+, Ca2+, Mg2+, or Co2+ stimulates its activity in this order of efficiency	Petrotoga mobilis
2.4.1.270	Co2+	not strictly dependent on divalent cations, but the presence of 1 mM Mn2+, Ca2+, Mg2+, or Co2+ stimulates its activity in this order of efficiency	Petrotoga mobilis
2.4.1.270	Mg2+	not strictly dependent on divalent cations, but the presence of 1 mM Mn2+, Ca2+, Mg2+, or Co2+ stimulates its activity in this order of efficiency	Petrotoga mobilis
2.4.1.270	Mn2+	not strictly dependent on divalent cations, but the presence of 1 mM Mn2+, Ca2+, Mg2+, or Co2+ stimulates its activity in this order of efficiency	Petrotoga mobilis
3.1.3.B8	Ca2+	divalent cations are not required for activity, but Mn2+, Mg2+, and Ca2+ (each 20 mM) leads to an increase in the activity by 100, 52, and 47%, respectively	Petrotoga mobilis
3.1.3.B8	Mg2+	divalent cations are not required for activity, but Mn2+, Mg2+, and Ca2+ (each 20 mM) leads to an increase in the activity by 100, 52, and 47%, respectively	Petrotoga mobilis
3.1.3.B8	Mn2+	divalent cations are not required for activity, but Mn2+, Mg2+, and Ca2+ (each 20 mM) leads to an increase in the activity by 100, 52, and 47%, respectively	Petrotoga mobilis
3.1.3.B8	additional information	NaCl and KCl concentrations between 50 and 300 mM had no effect on the enzyme activity	Petrotoga mobilis

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
2.4.1.266	37100	-	2 * 37100, calculated from sequence	Petrotoga mobilis
2.4.1.266	80000	-	gel filtration	Petrotoga mobilis
2.4.1.268	43700	-	4 * 43700, calculated from sequence	Petrotoga mobilis
2.4.1.268	170000	-	gel filtration	Petrotoga mobilis
2.4.1.270	51000	-	gel filtration	Petrotoga mobilis
2.4.1.270	59000	-	1 * 59000, SDS-PAGE	Petrotoga mobilis

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2.4.1.266	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	-	?
2.4.1.268	ADP-glucose + D-glycerate	Petrotoga mobilis	the enzyme is involved in the nonphosphorylating pathway for synthesis of the solute mannosylglucosylglycerate. In Petrotoga mobilis two alternative pathways for the synthesis of the solute mannosylglucosylglycerate are proposed. The first one is 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 during stress adaptation	2-O-(alpha-D-glucopyranosyl)-D-glycerate + ADP	-	?
2.4.1.270	GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-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 the rare solute 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	GDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate	-	?
3.1.3.B8	2-O-[2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl]-3-phospho-D-glycerate + H2O	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 the rare solute 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	2-O-[2-O-(alpha-D-mannopranosyl)-alpha-D-glucopyranosyl]-D-glycerate + phosphate	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.4.1.266	Petrotoga mobilis	A9BHI9	-	-
2.4.1.268	Petrotoga mobilis	A9BEU2	-	-
2.4.1.270	Petrotoga mobilis	A9BHJ0	-	-
3.1.3.B8	Petrotoga mobilis	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
2.4.1.266	recombinant enzyme	Petrotoga mobilis
2.4.1.270	recombinant enzyme	Petrotoga mobilis
3.1.3.B8	MggB could be only partially purified, because it completely loses activity after hydrophobic interaction chromatography or size-exclusion chromatography	Petrotoga mobilis

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
3.1.3.B8	0.3	-	60°C, pH 7.0, partially purified enzyme, substrate: mannosyl-3-phosphoglycerate	Petrotoga mobilis
3.1.3.B8	0.5	-	60°C, pH 7.0, partially purified enzyme, substrate: 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate	Petrotoga mobilis
3.1.3.B8	0.6	-	60°C, pH 7.0, partially purified enzyme, substrate: 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate	Petrotoga mobilis

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.4.1.266	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	-	?
2.4.1.266	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	-	?
2.4.1.266	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	-	?
2.4.1.268	ADP-glucose + D-glycerate	the enzyme is involved in the nonphosphorylating pathway for synthesis of the solute mannosylglucosylglycerate. In Petrotoga mobilis two alternative pathways for the synthesis of the solute mannosylglucosylglycerate are proposed. The first one is 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 during stress adaptation	Petrotoga mobilis	2-O-(alpha-D-glucopyranosyl)-D-glycerate + ADP	-	?
2.4.1.268	ADP-glucose + D-glycerate	formation of 2-O-(alpha-D-glucosyl)-D-glycerate is strongly favored. ADP-glucose is the preferred substrate for the recombinant glucosylglycerate synthase, which can be partially replaced by UDP-glucose with a very low efficiency. D-Glycerate is the only acceptor	Petrotoga mobilis	2-O-(alpha-D-glucopyranosyl)-D-glycerate + ADP	-	?
2.4.1.270	GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-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 the rare solute 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	GDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate	-	?
2.4.1.270	GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate	no activity with UDP-mannose or mannose-1-phosphate as sugar donors, and 3-phospho-D-glycerate, 2-alpha-D-glucosylglycerate, and glucosyl-3-phosphoglycerate as the sugar acceptors	Petrotoga mobilis	GDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate	-	?
3.1.3.B8	2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O	-	Petrotoga mobilis	?	-	?
3.1.3.B8	2-O-alpha-D-mannopyranosyl-3-phosphoglycerate + H2O	-	Petrotoga mobilis	?	-	?
3.1.3.B8	2-O-[2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl]-3-phospho-D-glycerate + H2O	-	Petrotoga mobilis	2-O-[2-O-(alpha-D-mannopranosyl)-alpha-D-glucopyranosyl]-D-glycerate + phosphate	-	?
3.1.3.B8	2-O-[2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl]-3-phospho-D-glycerate + H2O	the enzyme is involved in the phosphorylating pathway for synthesis of the solute mannosylglucosylglycerate. In Petrotoga mobilis two alternative pathways for the synthesis of the rare solute 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	2-O-[2-O-(alpha-D-mannopranosyl)-alpha-D-glucopyranosyl]-D-glycerate + phosphate	-	?
3.1.3.B8	additional information	UDP-glucose, ADP-glucose, GDP-mannose, ADP, GDP and UDP are dephosphorylated be the partially purified enzyme	Petrotoga mobilis	?	-	?

Subunits

EC Number	Subunits	Comment	Organism
2.4.1.266	dimer	2 * 37100, calculated from sequence	Petrotoga mobilis
2.4.1.268	tetramer	4 * 43700, calculated from sequence	Petrotoga mobilis
2.4.1.270	monomer	1 * 59000, SDS-PAGE	Petrotoga mobilis

Synonyms

EC Number	Synonyms	Comment	Organism
2.4.1.266	GpgS	-	Petrotoga mobilis
2.4.1.268	Ggs	-	Petrotoga mobilis
2.4.1.270	MggA	-	Petrotoga mobilis
3.1.3.B8	MggB	-	Petrotoga mobilis
3.1.3.B8	MGPG phosphatase	-	Petrotoga mobilis

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
2.4.1.266	70	-	-	Petrotoga mobilis
2.4.1.268	70	75	-	Petrotoga mobilis
2.4.1.270	90	-	-	Petrotoga mobilis
3.1.3.B8	80	-	-	Petrotoga mobilis

Temperature Range [°C]

EC Number	Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
2.4.1.266	60	75	60°C: about 85% of maximal activity, 75°C: about 60% of maximal activity	Petrotoga mobilis
2.4.1.270	60	95	60°C: about 50% of maximal activity, 95°C: about 70% of maximal activity	Petrotoga mobilis
3.1.3.B8	55	90	55°C: about 40% of maximal activity, 90°C: about 60% of maximal activity	Petrotoga mobilis

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
2.4.1.266	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
2.4.1.268	60	-	half-life: 3.1 h, recombinant enzyme	Petrotoga mobilis
2.4.1.270	60	-	half-life: 99 min	Petrotoga mobilis
3.1.3.B8	60	-	half-life: 120 h	Petrotoga mobilis
3.1.3.B8	70	-	half-life: 2.8 h	Petrotoga mobilis

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
2.4.1.266	7	-	60°C	Petrotoga mobilis
2.4.1.268	7	-	at 60°C	Petrotoga mobilis
2.4.1.270	9	-	-	Petrotoga mobilis
3.1.3.B8	6.5	7.5	-	Petrotoga mobilis

pH Range

EC Number	pH Minimum	pH Maximum	Comment	Organism
2.4.1.266	6	8	pH 6.0: about 80% of maximal activity, pH 8.0: about 50% of maximal activity	Petrotoga mobilis
2.4.1.270	6	10	pH 6.0: about 50% of maximal activity, pH 10.0: about 75% of maximal activity	Petrotoga mobilis
3.1.3.B8	6	8	pH 6.0: about 50% of maximal activity, pH 8.0: about 70% of maximal activity	Petrotoga mobilis

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Release 2023.1 (January 2023)