BRENDA - Enzyme Database
show all sequences of 3.1.3.B8

Two alternative pathways for the synthesis of the rare compatible solute mannosylglucosylglycerate in Petrotoga mobilis

Fernandes, C.; Mendes, V.; Costa, J.; Empadinhas, N.; Jorge, C.; Lamosa, P.; Santos, H.; da Costa, M.S.; J. Bacteriol. 192, 1624-1633 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Petrotoga mobilis
Inhibitors
Inhibitors
Commentary
Organism
Structure
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]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.5
-
2-O-[2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl]-3-phospho-D-glycerate
60C, pH 7.0, partially purified enzyme
Petrotoga mobilis
2.6
-
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
60C, pH 7.0, partially purified enzyme
Petrotoga mobilis
2.8
-
2-O-alpha-D-mannopyranosyl-3-phosphoglycerate
60C, pH 7.0, partially purified enzyme
Petrotoga mobilis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
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
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
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
additional information
NaCl and KCl concentrations between 50 and 300 mM had no effect on the enzyme activity
Petrotoga mobilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Petrotoga mobilis
-
-
-
Purification (Commentary)
Commentary
Organism
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]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.3
-
60C, pH 7.0, partially purified enzyme, substrate: mannosyl-3-phosphoglycerate
Petrotoga mobilis
0.5
-
60C, pH 7.0, partially purified enzyme, substrate: 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
Petrotoga mobilis
0.6
-
60C, 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)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
-
708933
Petrotoga mobilis
?
-
-
-
?
2-O-alpha-D-mannopyranosyl-3-phosphoglycerate + H2O
-
708933
Petrotoga mobilis
?
-
-
-
?
2-O-[2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl]-3-phospho-D-glycerate + H2O
-
708933
Petrotoga mobilis
2-O-[2-O-(alpha-D-mannopranosyl)-alpha-D-glucopyranosyl]-D-glycerate + phosphate
-
-
-
?
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
708933
Petrotoga mobilis
2-O-[2-O-(alpha-D-mannopranosyl)-alpha-D-glucopyranosyl]-D-glycerate + phosphate
-
-
-
?
additional information
UDP-glucose, ADP-glucose, GDP-mannose, ADP, GDP and UDP are dephosphorylated be the partially purified enzyme
708933
Petrotoga mobilis
?
-
-
-
-
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
80
-
-
Petrotoga mobilis
Temperature Range [C]
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
55
90
55C: about 40% of maximal activity, 90C: about 60% of maximal activity
Petrotoga mobilis
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
60
-
half-life: 120 h
Petrotoga mobilis
70
-
half-life: 2.8 h
Petrotoga mobilis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7.5
-
Petrotoga mobilis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
8
pH 6.0: about 50% of maximal activity, pH 8.0: about 70% of maximal activity
Petrotoga mobilis
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Petrotoga mobilis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
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] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.5
-
2-O-[2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl]-3-phospho-D-glycerate
60C, pH 7.0, partially purified enzyme
Petrotoga mobilis
2.6
-
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
60C, pH 7.0, partially purified enzyme
Petrotoga mobilis
2.8
-
2-O-alpha-D-mannopyranosyl-3-phosphoglycerate
60C, pH 7.0, partially purified enzyme
Petrotoga mobilis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
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
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
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
additional information
NaCl and KCl concentrations between 50 and 300 mM had no effect on the enzyme activity
Petrotoga mobilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
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] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.3
-
60C, pH 7.0, partially purified enzyme, substrate: mannosyl-3-phosphoglycerate
Petrotoga mobilis
0.5
-
60C, pH 7.0, partially purified enzyme, substrate: 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
Petrotoga mobilis
0.6
-
60C, 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) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
-
708933
Petrotoga mobilis
?
-
-
-
?
2-O-alpha-D-mannopyranosyl-3-phosphoglycerate + H2O
-
708933
Petrotoga mobilis
?
-
-
-
?
2-O-[2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl]-3-phospho-D-glycerate + H2O
-
708933
Petrotoga mobilis
2-O-[2-O-(alpha-D-mannopranosyl)-alpha-D-glucopyranosyl]-D-glycerate + phosphate
-
-
-
?
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
708933
Petrotoga mobilis
2-O-[2-O-(alpha-D-mannopranosyl)-alpha-D-glucopyranosyl]-D-glycerate + phosphate
-
-
-
?
additional information
UDP-glucose, ADP-glucose, GDP-mannose, ADP, GDP and UDP are dephosphorylated be the partially purified enzyme
708933
Petrotoga mobilis
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
80
-
-
Petrotoga mobilis
Temperature Range [C] (protein specific)
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
55
90
55C: about 40% of maximal activity, 90C: about 60% of maximal activity
Petrotoga mobilis
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
60
-
half-life: 120 h
Petrotoga mobilis
70
-
half-life: 2.8 h
Petrotoga mobilis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7.5
-
Petrotoga mobilis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
8
pH 6.0: about 50% of maximal activity, pH 8.0: about 70% of maximal activity
Petrotoga mobilis
Other publictions for EC 3.1.3.B8
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
732910
Cunha
Mannosylglucosylglycerate bios ...
Rhodopirellula baltica, Rhodopirellula baltica DSM 10527
Sci. Rep.
3
2378
2013
-
-
1
-
-
-
1
4
-
3
2
-
-
8
-
-
-
-
-
-
1
-
5
1
1
3
3
-
1
1
-
-
-
1
-
-
-
2
-
-
-
-
-
1
-
4
-
5
2
-
-
-
-
-
-
-
1
-
5
1
2
3
5
-
2
1
-
1
-
-
-
-
-
-
708933
Fernandes
Two alternative pathways for t ...
Petrotoga mobilis
J. Bacteriol.
192
1624-1633
2010
-
-
1
-
-
-
1
3
-
4
-
1
-
1
-
-
1
-
-
-
3
-
5
-
1
1
2
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
3
-
4
-
1
-
-
-
1
-
-
3
-
5
-
1
1
2
-
1
1
-
-
-
-
-
-
-
-