Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GDP-alpha-D-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-glucosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(1-D-mannosyl)-3-phosphoglycerate
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
additional information
?
-
GDP-alpha-D-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-alpha-D-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
the enzyme is absolute specific for GDP-mannose and 3-phospho-D-glycerate as substrates
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
the enzyme is involved in synthesis of mannosylglycerate
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
the enzyme is highly specific for the substrates GDP-mannose and 3-phospho-D-glycerate
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
the enzyme is involved in synthesis of mannosylglycerate
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
the enzyme is highly specific for the substrates GDP-mannose and 3-phospho-D-glycerate
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
2 pathways for mannosylglycerate biosynthesis, a one-step and a two-step pathway, with specialized roles in osmoadaptation and thermoadaptation, the isozyme involved in the two-step pathway is upregulated by osmotic stress, the isozyme involved in the one-step pathway is upregulated by heat stress, regulatory mechanisms, overview
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(1-D-mannosyl)-3-phosphoglycerate
-
involved in a pathway for synthesis of mannosylglycerate
mannosyl-3-phosphoglycerate is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70, producing mannosylglycerate
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(1-D-mannosyl)-3-phosphoglycerate
-
involved in a pathway for synthesis of mannosylglycerate
-
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
transfer of the mannosyl group with retention of configuration
-
?
GDPmannose + 3-phospho-D-glycerate
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
-
-
?
additional information
?
-
-
substrate binding structure, overview
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
-
substrate binding structure, overview
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
-
substrate binding structure, overview
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold
-
-
?
additional information
?
-
-
the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
-
besides its physiological substrate D-glycerate, RmaMGS is also able to use D-lactate and glycolate as sugar acceptors, thus displaying some acceptor plasticity. Substrate binding structure, overview
-
-
?
additional information
?
-
-
substrate binding structure, overview
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. The enzyme from Rubrobacter xylanophilus is promiscuous and produces the phosphorylated form of glucosylglycerate (GPG) from GDP-glucose plus 3-D-phosphoglycerate with high efficiency. In spite of the less favorable parameters for the synthesis of mannosylglycerate, this is the only free glyceryl glycoside found in Rubrobacter xylanophilus cells
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. Substrate binding structure, overview
-
-
?
additional information
?
-
-
the enzyme is highly specific for 3-phospho-D-glycerate
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. Substrate binding structure, overview
-
-
?
additional information
?
-
-
the enzyme is highly specific for 3-phospho-D-glycerate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-glucosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(1-D-mannosyl)-3-phosphoglycerate
additional information
?
-
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
the enzyme is involved in synthesis of mannosylglycerate
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
the enzyme is involved in synthesis of mannosylglycerate
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
2 pathways for mannosylglycerate biosynthesis, a one-step and a two-step pathway, with specialized roles in osmoadaptation and thermoadaptation, the isozyme involved in the two-step pathway is upregulated by osmotic stress, the isozyme involved in the one-step pathway is upregulated by heat stress, regulatory mechanisms, overview
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(1-D-mannosyl)-3-phosphoglycerate
-
involved in a pathway for synthesis of mannosylglycerate
mannosyl-3-phosphoglycerate is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70, producing mannosylglycerate
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(1-D-mannosyl)-3-phosphoglycerate
-
involved in a pathway for synthesis of mannosylglycerate
-
?
additional information
?
-
-
the bifunctional enzyme catalyzes the consecutive synthesis and dephosphorylation of mannosyl-3-phosphoglycerate in mannosylglycerate biosynthesis, enzyme evolution
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold
-
-
?
additional information
?
-
-
the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. The enzyme from Rubrobacter xylanophilus is promiscuous and produces the phosphorylated form of glucosylglycerate (GPG) from GDP-glucose plus 3-D-phosphoglycerate with high efficiency. In spite of the less favorable parameters for the synthesis of mannosylglycerate, this is the only free glyceryl glycoside found in Rubrobacter xylanophilus cells
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. Substrate binding structure, overview
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. Substrate binding structure, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KCl
-
or NaCl required for optimal activity
NaCl
-
or KCl, required for optimal activity
Ni2+
activates, best at 1.5 mM
Co2+
-
most effective in enzyme activation
Co2+
effect of divalent cations on MpgS activity decreases in the following order Mg2+, Co2+, Mn2+
Co2+
activates, best at 2 mM
Mg2+
-
activates
Mg2+
strictly dependent on Mg2+
Mg2+
-
binding structure overview
Mg2+
-
activity in absence is 46% of that in presence of 15 mM Mg2+
Mg2+
-
binding structure overview
Mg2+
required for activity
Mg2+
-
binding structure overview
Mg2+
strictly dependent on, effect of divalent cations on MpgS activity decreases in the following order Mg2+, Co2+, Mn2+
Mg2+
-
binding structure overview
Mg2+
activates, best at 20 mM
Mg2+
-
binding structure overview
Mg2+
activity is strictly dependent on divalent cations, Mn2+ is most effective (between 0.2 and 2.0 mM), Mg2+x01has a similar effect on the activation at about 20.0 mM
Mg2+
used as single metal cofactor at 20 mM, activity dependend on
Mn2+
-
activates
Mn2+
-
binding structure overview
Mn2+
-
binding structure overview
Mn2+
-
binding structure overview
Mn2+
effect of divalent cations on MpgS activity decreases in the following order Mg2+, Co2+, Mn2+
Mn2+
-
binding structure overview
Mn2+
Mn2+ is most effective in enzyme activation, best at 1 mM
Mn2+
-
binding structure overview
Mn2+
activity is strictly dependent on divalent cations, Mn2+ is most effective, maximum activation of the enzyme by Mn2+ is between 0.2 and 2.0 mM
Zn2+
-
binding structure overview
Zn2+
-
binding structure overview
Zn2+
-
binding structure overview
Zn2+
-
binding structure overview
Zn2+
-
binding structure overview
additional information
-
enzyme requires divalent cations, Co2+ is preferred and can partially be substituted by Mg2+ or Mn2+, no activation by other cations
additional information
strictly dependent on divalent cations, no activation by Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+
additional information
-
strictly dependent on divalent cations, no activation by Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+
additional information
Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+, do not stimulate activity at any concentration
additional information
-
Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+, do not stimulate activity at any concentration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
the enzyme is included in the glycosyltransferase family GT55
evolution
-
the enzyme is included in the glycosyltransferase family GT55
evolution
-
the enzyme is included in the glycosyltransferase family GT55
evolution
-
the enzyme is included in the glycosyltransferase family GT55
evolution
-
the promiscuous MPGS/GPGS from Rubrobacter xylanophilus (RxyMPGS) is included within the retaining GT81 family, members of the GT55 and GT81 families preserved a common structural core, defined by the alpha/beta/alpha region containing 7 beta-strands in the order 3-2-1-4-6-5-7, with beta6 antiparallel to the rest, that could be included into the MGS-like family
evolution
-
the enzyme is included in the glycosyltransferase family GT55
-
evolution
-
the enzyme is included in the glycosyltransferase family GT55
-
metabolism
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS) catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
metabolism
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS) catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
metabolism
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS) catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
metabolism
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS) catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
metabolism
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS)catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
metabolism
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS) catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
-
metabolism
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS) catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
-
physiological function
the enzyme is involved in synthesis of mannosylglycerate
physiological function
-
the enzyme is involved in synthesis of mannosylglycerate
-
additional information
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
additional information
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
additional information
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
additional information
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
additional information
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
additional information
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
-
additional information
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Martins, L.O.; Empadinhas, N.; Marugg, J.D.; Miguel, C.; Ferreira, C.; Da Costa, M.S.; Santos, H.
Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus. Biochemical and genetic characterization of a mannosylglycerate synthase
J. Biol. Chem.
274
35407-35414
1999
Rhodothermus marinus
brenda
Empadinhas, N.; Marugg, J.D.; Borges, N.; Santos, H.; Da Costa, M.S.
Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes
J. Biol. Chem.
276
43580-43588
2001
Pyrococcus horikoshii
brenda
Empadinhas, N.; Albuquerque, L.; Henne, A.; Santos, H.; da Costa, M.S.
The bacterium Thermus thermophilus, like hyperthermophilic archaea, uses a two-step pathway for the synthesis of mannosylglycerate
Appl. Environ. Microbiol.
69
3272-3279
2003
Thermus thermophilus (Q84B24), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q84B24)
brenda
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
J. Bacteriol.
186
4075-4084
2004
Dehalococcoides mccartyi, no activity in Saccharomyces cerevisiae
brenda
Borges, N.; Marugg, J.D.; Empadinhas, N.; da Costa, M.S.; Santos, H.
Specialized roles of the two pathways for the synthesis of mannosylglycerate in osmoadaptation and thermoadaptation of Rhodothermus marinus
J. Biol. Chem.
279
9892-9898
2004
Rhodothermus marinus (Q6WSQ4), Rhodothermus marinus
brenda
Neves, C.; da Costa, M.S.; Santos, H.
Compatible solutes of the hyperthermophile Palaeococcus ferrophilus: osmoadaptation and thermoadaptation in the order Thermococcales
Appl. Environ. Microbiol.
71
8091-8098
2005
Thermococcus litoralis (Q2VPR9), Thermococcus litoralis, Palaeococcus ferrophilus (Q2VPS1), Palaeococcus ferrophilus, Palaeococcus ferrophilus DSM 13482T (Q2VPS1)
brenda
Sa-Moura, B.; Albuquerque, L.; Empadinhas, N.; da Costa, M.S.; Pereira, P.J.; Macedo-Ribeiro, S.
Crystallization and preliminary crystallographic analysis of mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus
Acta Crystallogr. Sect. F
64
760-763
2008
Rubrobacter xylanophilus (B7SY86), Rubrobacter xylanophilus
brenda
Alarico, S.; Empadinhas, N.; Mingote, A.; Simoes, C.; Santos, M.S.; da Costa, M.S.
Mannosylglycerate is essential for osmotic adjustment in Thermus thermophilus strains HB27 and RQ-1
Extremophiles
11
833-840
2007
Thermus thermophilus (Q84B24), Thermus thermophilus
brenda
Goncalves, S.; Borges, N.; Santos, H.; Matias, P.M.
Crystallization and preliminary X-ray analysis of mannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB27
Acta Crystallogr. Sect. F
65
1014-1017
2009
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
brenda
Goncalves, S.; Borges, N.; Esteves, A.M.; Victor, B.L.; Soares, C.M.; Santos, H.; Matias, P.M.
Structural analysis of Thermus thermophilus HB27 mannosyl-3-phosphoglycerate synthase provides evidence for a second catalytic metal ion and new insight into the retaining mechanism of glycosyltransferases
J. Biol. Chem.
285
17857-17868
2010
Thermus thermophilus HB27 (Q84B24), Thermus thermophilus HB27
brenda
Empadinhas, N.; Pereira, P.J.; Albuquerque, L.; Costa, J.; S-Moura, B.; Marques, A.T.; Macedo-Ribeiro, S.; da Costa, M.S.
Functional and structural characterization of a novel mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus reveals its dual substrate specificity
Mol. Microbiol.
79
76-93
2011
Rubrobacter xylanophilus (B7SY86), Rubrobacter xylanophilus
brenda
Borges, N.; Jorge, C.D.; Goncalves, L.G.; Goncalves, S.; Matias, P.M.; Santos, H.
Mannosylglycerate: structural analysis of biosynthesis and evolutionary history
Extremophiles
18
835-852
2014
Palaeococcus ferrophilus, Pyrococcus horikoshii, Pyrococcus horikoshii OT-3, Rhodothermus marinus, Rubrobacter xylanophilus, Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
brenda
Costa, J.; Empadinhas, N.; Goncalves, L.; Lamosa, P.; Santos, H.; Da Costa, M.
Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii
J. Bacteriol.
188
1022-1030
2006
Pyrococcus horikoshii (O58690), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O58690)
brenda
Empadinhas, N.; Albuquerque, L.; Henne, A.; Santos, H.; Da Costa, M.
The bacterium Thermus thermophilus, like hyperthermophilic archaea, uses a two-step pathway for the synthesis of mannosylglycerate
Appl. Environ. Microbiol.
69
3272-3279
2003
Thermus thermophilus (Q84B24), Thermus thermophilus, Thermus thermophilus DSM 7039 (Q84B24)
brenda