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.
ADP-alpha-D-glucose + D-3-phosphoglycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
GDP-glucose + D-3-phosphoglycerate
GDP + 2-(beta-D-glucosyl)-sn-glycerol 3-phosphate
-
-
-
?
TDP-glucose + 3-phospho-D-glycerate
TDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
the recombinant GpgS protein of Persephonella marina catalyzes the synthesis of 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate from UDP-glucose, GDP-glucose, ADP-glucose, and TDP-glucose (in order of decreasing efficiency) and from D-3-phosphoglycerate
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate
in Persephonella marina two pathways for synthesis of glucosylglycerate are present: 1. the single-step pathway in with glucosylglycerate synthase (Ggs) catalyzes the synthesis of 2-O-(alpha-D-glucosyl)-D-glycerate in one-step fop, ADP-glucose and D-glycerate, and 2. the two-step pathway in which glucosyl-3-phosphoglycerate synthase (GpgS) catalyzes the conversion of NDP-glucose and D-3-phosphoglycerate into glucosyl-3-phosphoglycerate, which is then converted to 2-O-(alpha-D-glucosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase (GpgP)
-
-
?
UDP-glucose + D-3-phosphoglycerate
UDP + 2-(beta-D-glucosyl)-sn-glycerol 3-phosphate
additional information
?
-
ADP-alpha-D-glucose + D-3-phosphoglycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
-
?
ADP-alpha-D-glucose + D-3-phosphoglycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
-
?
ADP-alpha-D-glucose + D-3-phosphoglycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
-
?
ADP-alpha-D-glucose + D-3-phosphoglycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
ADP-alpha-D-glucose + D-3-phosphoglycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
ADP-alpha-D-glucose + D-3-phosphoglycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-(O-alpha-D-glucopyranosyl)-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
-
-
?
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
-
?
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
the recombinant GpgS protein of Persephonella marina catalyzes the synthesis of 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate from UDP-glucose, GDP-glucose, ADP-glucose, and TDP-glucose (in order of decreasing efficiency) and from D-3-phosphoglycerate
-
-
?
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate
-
-
-
?
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate
-
-
-
?
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
synthesis of the solute glucosylglycerate proceeds via a two-step pathway involving glucosyl-3-phosphoglycerate synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP). An mpgS gene coding for mannosyl-3-phosphoglycerate synthase (MpgS) is absent
-
-
?
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
-
?
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
the recombinant GpgS protein of Persephonella marina catalyzes the synthesis of 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate from UDP-glucose, GDP-glucose, ADP-glucose, and TDP-glucose (in order of decreasing efficiency) and from D-3-phosphoglycerate
-
-
?
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 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 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-glucose + 3-phospho-D-glycerate
UDP + 2-(O-alpha-D-glucopyranosyl)-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
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
three-dimensional structures provide a molecular explanation for the enzymes preference for UDP-containing donor substrates, as well as for its glucose versus mannose discrimination, and uncover the structural determinants for acceptor substrate selectivity
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
involved in biosynthesis of methylated polysaccharides
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
involved in biosynthesis of methylated polysaccharides
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
involved in biosynthesis of methylated polysaccharides
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
the recombinant GpgS protein of Persephonella marina catalyzes the synthesis of 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate from UDP-glucose, GDP-glucose, ADP-glucose, and TDP-glucose (in order of decreasing efficiency) and from D-3-phosphoglycerate
-
-
?
UDP-glucose + D-3-phosphoglycerate
UDP + 2-(beta-D-glucosyl)-sn-glycerol 3-phosphate
-
best substrates
-
-
?
UDP-glucose + D-3-phosphoglycerate
UDP + 2-(beta-D-glucosyl)-sn-glycerol 3-phosphate
-
best substrates
-
-
?
UDP-glucose + D-3-phosphoglycerate
UDP + 2-(beta-D-glucosyl)-sn-glycerol 3-phosphate
-
best substrates
-
-
?
UDP-glucose + D-3-phosphoglycerate
UDP + 2-(beta-D-glucosyl)-sn-glycerol 3-phosphate
best substrates
-
-
?
UDP-glucose + D-3-phosphoglycerate
UDP + 2-(beta-D-glucosyl)-sn-glycerol 3-phosphate
best substrates
-
-
?
UDP-glucose + D-3-phosphoglycerate
UDP + 2-(beta-D-glucosyl)-sn-glycerol 3-phosphate
-
-
-
?
additional information
?
-
no activity with: ADP-ribose, UDP-acetylgalactosamine, UDP-glucuronic acid, UDP-galactose, GDP-fucose, GDP-mannose, UDP-mannose, ADP-mannose, UDP-glucose, TDP-glucose, and ADP-glucose as sugar donors and glycerol, D-2-phosphoglycerate, L-glycerol-3-phosphate, 2,3-diphospho-D-glycerate, and phosphoenolpyruvate
-
-
?
additional information
?
-
-
no activity with: ADP-ribose, UDP-acetylgalactosamine, UDP-glucuronic acid, UDP-galactose, GDP-fucose, GDP-mannose, UDP-mannose, ADP-mannose, UDP-glucose, TDP-glucose, and ADP-glucose as sugar donors and glycerol, D-2-phosphoglycerate, L-glycerol-3-phosphate, 2,3-diphospho-D-glycerate, and phosphoenolpyruvate
-
-
?
additional information
?
-
a single ionizable residue is involved catalysis (pKa = 6.3) that must be deprotonated for full activity. A solvent kinetic isotope effect of 2.0 on kcat is consistent with a proton in flight during the rate-determining step
-
-
?
additional information
?
-
-
a single ionizable residue is involved catalysis (pKa = 6.3) that must be deprotonated for full activity. A solvent kinetic isotope effect of 2.0 on kcat is consistent with a proton in flight during the rate-determining step
-
-
?
additional information
?
-
a single ionizable residue is involved catalysis (pKa = 6.3) that must be deprotonated for full activity. A solvent kinetic isotope effect of 2.0 on kcat is consistent with a proton in flight during the rate-determining step
-
-
?
additional information
?
-
cosubstrate efficiency in decreasing order: UDP-glucose,ADP-glucose and GDP-glucose. No cosubstrate: GDP-mannose
-
-
-
additional information
?
-
-
cosubstrate efficiency in decreasing order: UDP-glucose,ADP-glucose and GDP-glucose. No cosubstrate: GDP-mannose
-
-
-
additional information
?
-
cosubstrate efficiency in decreasing order: UDP-glucose,ADP-glucose and GDP-glucose. No cosubstrate: GDP-mannose
-
-
-
additional information
?
-
the genes for glucosyl-3-phosphoglycerate synthase, GpgS, and glucosyl-3-phosphoglycerate phosphatase, GpgP, the enzymes that lead to the synthesis of glucosylglycerol through the formation of glucosyl-3-phosphoglycerate, are organized in anoperon-like structure with the gene encoding a putative glycosyltransferase, the glucosylglycerate synthase, Ggs, overview, biosynthetic pathway overview
-
-
?
additional information
?
-
-
the genes for glucosyl-3-phosphoglycerate synthase, GpgS, and glucosyl-3-phosphoglycerate phosphatase, GpgP, the enzymes that lead to the synthesis of glucosylglycerol through the formation of glucosyl-3-phosphoglycerate, are organized in anoperon-like structure with the gene encoding a putative glycosyltransferase, the glucosylglycerate synthase, Ggs, overview, biosynthetic pathway overview
-
-
?
additional information
?
-
no activity with: ADP-ribose, UDP-acetylgalactosamine, UDP-glucuronic acid, UDP-galactose, GDP-fucose, GDP-mannose, UDP-mannose or ADP-mannose
-
-
?
additional information
?
-
-
no activity with: ADP-ribose, UDP-acetylgalactosamine, UDP-glucuronic acid, UDP-galactose, GDP-fucose, GDP-mannose, UDP-mannose or ADP-mannose
-
-
?
additional information
?
-
key enzyme of glucosylglycerate synthesis
-
-
?
additional information
?
-
key enzyme of glucosylglycerate synthesis
-
-
?
additional information
?
-
enzyme is rather non-specific for glucosyl donors using several glucose diphosphate nucleosides, with ADP-glucose being by far the preferred substrate, followed by UDP-glucose and GDP-glucose. Only 3-PGA can used as glucosyl acceptor leading to the formation of glucosyl 3-phosphoglycerate
-
-
?
additional information
?
-
-
enzyme is rather non-specific for glucosyl donors using several glucose diphosphate nucleosides, with ADP-glucose being by far the preferred substrate, followed by UDP-glucose and GDP-glucose. Only 3-PGA can used as glucosyl acceptor leading to the formation of glucosyl 3-phosphoglycerate
-
-
?
additional information
?
-
enzyme is rather non-specific for glucosyl donors using several glucose diphosphate nucleosides, with ADP-glucose being by far the preferred substrate, followed by UDP-glucose and GDP-glucose. Only 3-PGA can used as glucosyl acceptor leading to the formation of glucosyl 3-phosphoglycerate
-
-
?
additional information
?
-
key enzyme of glucosylglycerate synthesis
-
-
?
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-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
synthesis of the solute glucosylglycerate proceeds via a two-step pathway involving glucosyl-3-phosphoglycerate synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP). An mpgS gene coding for mannosyl-3-phosphoglycerate synthase (MpgS) is absent
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 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 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-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate
in Persephonella marina two pathways for synthesis of glucosylglycerate are present: 1. the single-step pathway in with glucosylglycerate synthase (Ggs) catalyzes the synthesis of 2-O-(alpha-D-glucosyl)-D-glycerate in one-step fop, ADP-glucose and D-glycerate, and 2. the two-step pathway in which glucosyl-3-phosphoglycerate synthase (GpgS) catalyzes the conversion of NDP-glucose and D-3-phosphoglycerate into glucosyl-3-phosphoglycerate, which is then converted to 2-O-(alpha-D-glucosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase (GpgP)
-
-
?
additional information
?
-
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
involved in biosynthesis of methylated polysaccharides
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
involved in biosynthesis of methylated polysaccharides
-
-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
involved in biosynthesis of methylated polysaccharides
-
-
?
additional information
?
-
the genes for glucosyl-3-phosphoglycerate synthase, GpgS, and glucosyl-3-phosphoglycerate phosphatase, GpgP, the enzymes that lead to the synthesis of glucosylglycerol through the formation of glucosyl-3-phosphoglycerate, are organized in anoperon-like structure with the gene encoding a putative glycosyltransferase, the glucosylglycerate synthase, Ggs, overview, biosynthetic pathway overview
-
-
?
additional information
?
-
-
the genes for glucosyl-3-phosphoglycerate synthase, GpgS, and glucosyl-3-phosphoglycerate phosphatase, GpgP, the enzymes that lead to the synthesis of glucosylglycerol through the formation of glucosyl-3-phosphoglycerate, are organized in anoperon-like structure with the gene encoding a putative glycosyltransferase, the glucosylglycerate synthase, Ggs, overview, biosynthetic pathway overview
-
-
?
additional information
?
-
key enzyme of glucosylglycerate synthesis
-
-
?
additional information
?
-
key enzyme of glucosylglycerate synthesis
-
-
?
additional information
?
-
key enzyme of glucosylglycerate synthesis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Co2+
strictly dependent on divalent cations in the following order of efficiency: Mn2+, Co2+, Mg2+. Maximal activity at 1 mM
Co2+
strictly dependent on divalent cations, in the following order of efficiency: Mn2+, Co2+, Mg2+, Ni2+
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
Co2+
and Mn2+, stimulation
Mg2+
strictly dependent on divalent cations in the following order of efficiency: Mn2+, Co2+, Mg2+
Mg2+
-
strictly dependent on
Mg2+
-
strictly dependent on
Mg2+
-
activity is strictly dependent on Mg2+, maximal activation at 20-75 mM
Mg2+
GpgS is dependent on divalent cations in the decreasing order of efficiency: Mg2+ (20 mM) > Mn2+ (10 mM)
Mg2+
strictly dependent on
Mg2+
activity is strictly dependent on Mg2+, maximal activation at 20 mM
Mg2+
strictly dependent on divalent cations, in the following order of efficiency: Mn2+, Co2+, Mg2+, Ni2+
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
Mg2+
maximum activtiy in presence of 1 mM Mg2+
Mn2+
strictly dependent on divalent cations in the following order of efficiency: Mn2+, Co2+, Mg2+. Maximal activity at 1 mM
Mn2+
strictly dependent on divalent cations, in the following order of efficiency: Mn2+, Co2+, Mg2+, Ni2+. The maximum activation is obtained with 1.0 mM Mn2+. 50% of the maximum activity is reached with 0.19 mM Mn2+
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
Mn2+
and Co2+, stimulation
Ni2+
strictly dependent on divalent cations, in the following order of efficiency: Mn2+, Co2+, Mg2+, Ni2+. The specific activities obtained with Ni2+ are similar for both the His-tagged enzyme and the nontagged recombinant enzyme
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
additional information
K+, Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+, do not stimulate GpgS activity at any concentration
additional information
-
K+, Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+, do not stimulate GpgS activity at any concentration
additional information
K+, Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+, do not stimulate GpgS activity at any concentration
additional information
-
K+, Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+, do not stimulate GpgS 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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Costa, J.; Empadinhas, N.; da Costa, M.S.
Glucosylglycerate biosynthesis in the deepest lineage of the bacteria: characterization of the thermophilic proteins GpgS and GpgP from Persephonella marina
J. Bacteriol.
189
1648-1654
2007
Persephonella marina (A9QXB4), Persephonella marina
brenda
Costa, J.; Empadinhas, N.; Goncalves, L.; Lamosa, P.; Santos, H.; da Costa, M.S.
Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii
J. Bacteriol.
188
1022-1030
2006
Methanococcoides burtonii (Q12XX4), Methanococcoides burtonii
brenda
Fernandes, C.; Empadinhas, N.; da Costa, M.S.
Single-step pathway for synthesis of glucosylglycerate in Persephonella marina
J. Bacteriol.
189
4014-4019
2007
Persephonella marina (A9QXB4), Persephonella marina
brenda
Empadinhas, N.; Albuquerque, L.; Mendes, V.; Macedo-Ribeiro, S.; da Costa, M.S.
Identification of the mycobacterial glucosyl-3-phosphoglycerate synthase
FEMS Microbiol. Lett.
280
195-202
2008
Mycobacterium tuberculosis, Mycobacterium tuberculosis variant bovis, Mycolicibacterium smegmatis (A0R2E6), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084 (A0R2E6), Mycobacterium tuberculosis H37Rv
brenda
Klaehn, S.; Steglich, C.; Hess, W.R.; Hagemann, M.
Glucosylglycerate: a secondary compatible solute common to marine cyanobacteria from nitrogen-poor environments
Environ. Microbiol.
12
83-94
2010
Synechococcus sp. (B1XHT9), Prochlorococcus marinus (Q7VCL3), Prochlorococcus marinus SS120 (Q7VCL3)
brenda
Gest, P.; Kaur, D.; Pham, H.T.; van der, Woerd, M.; Hansen, E.; Brennan, P.J.; Jackson, M.; Guerin, M.E.
Preliminary crystallographic analysis of GpgS, a key glucosyltransferase involved in methylglucose lipopolysaccharide biosynthesis in Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
64
1121-1124
2008
amenda
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
J. Bacteriol.
192
1624-1633
2010
Petrotoga mobilis (A9BHI9), Petrotoga mobilis
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 DSM 9941
brenda
Pereira, P.J.B.; Empadinhas, N.; Albuquerque, L.; Sa-Moura, B.; da Costa, M.S.; Macedo-Ribeiro, S.
Mycobacterium tuberculosis glucosyl-3-phosphoglycerate synthase: structure of a key enzyme in Methylglucose lipopolysaccharide biosynthesis
PLOS One
3
e3748
2008
Mycobacterium tuberculosis
brenda
Kaur, D.; Pham, H.; Larrouy-Maumus, G.; Riviere, M.; Vissa, V.; Guerin, M.E.; Puzo, G.; Brennan, P.J.; Jackson, M.
Initiation of methylglucose lipopolysaccharide biosynthesis in mycobacteria
PLoS One
4(5)
e5447
2009
amenda
Urresti, S.; Albesa-Jove, D.; Schaeffer, F.; Pham, H.T.; Kaur, D.; Gest, P.; van der Woerd, M.J.; Carreras-Gonzalez, A.; Lopez-Fernandez, S.; Alzari, P.M.; Brennan, P.J.; Jackson, M.; Guerin, M.E.
Mechanistic insights into the retaining glucosyl-3-phosphoglycerate synthase from mycobacteria
J. Biol. Chem.
287
24649-24661
2012
amenda
Cunha, S.; dAvo, A.F.; Mingote, A.; Lamosa, P.; da Costa, M.S.; Costa, J.
Mannosylglucosylglycerate biosynthesis in the deep-branching phylum Planctomycetes: characterization of the uncommon enzymes from Rhodopirellula baltica
Sci. Rep.
3
2378
2013
Rhodopirellula baltica (Q7UXY8), Rhodopirellula baltica, Rhodopirellula baltica DSM 10527 (Q7UXY8)
brenda
Albesa-Jove, D.; Mendoza, F.; Rodrigo-Unzueta, A.; Gomollon-Bel, F.; Cifuente, J.O.; Urresti, S.; Comino, N.; Gomez, H.; Romero-Garcia, J.; Lluch, J.M.; Sancho-Vaello, E.; Biarnes, X.; Planas, A.; Merino, P.; Masgrau, L.; Guerin, M.E.
A native ternary complex trapped in a crystal reveals the catalytic mechanism of a retaining glycosyltransferase
Angew. Chem. Int. Ed. Engl.
54
9898-9902
2015
Mycobacterium tuberculosis (P9WMW9), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WMW9)
brenda
Kumar, G.; Guan, S.; Frantom, P.A.
Biochemical characterization of the retaining glycosyltransferase glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis
Arch. Biochem. Biophys.
564
120-127
2014
Mycobacterium tuberculosis (P9WMW9), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WMW9)
brenda
Alarico, S.; Nunes-Costa, D.; Silva, A.; Costa, M.; Macedo-Ribeiro, S.; Empadinhas, N.
A genuine mycobacterial thermophile Mycobacterium hassiacum growth, survival and GpgS stability at near-pasteurization temperatures
Microbiology
166
474-483
2020
Mycolicibacterium hassiacum (K5B7Z4), Mycolicibacterium hassiacum, Mycolicibacterium hassiacum DSM 44199 (K5B7Z4)
brenda
Albesa-Jove, D.; Romero-Garcia, J.; Sancho-Vaello, E.; Contreras, F.X.; Rodrigo-Unzueta, A.; Comino, N.; Carreras-Gonzalez, A.; Arrasate, P.; Urresti, S.; Biarnes, X.; Planas, A.; Guerin, M.E.
Structural snapshots and loop dynamics along the catalytic cycle of glycosyltransferase GpgS
Structure
25
1034-1044
2017
Mycobacterium tuberculosis (P9WMW9), Mycobacterium tuberculosis ATCC 25618 (P9WMW9)
brenda