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Information on EC 2.4.1.266 - glucosyl-3-phosphoglycerate synthase
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2.4.1.266 glucosyl-3-phosphoglycerate synthaseIUBMB Comments
The enzyme is involved in biosynthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate via the two-step pathway in which glucosyl-3-phosphoglycerate synthase catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-glucopyranosyl)-D-glycerate by EC 3.1.3.85 glucosyl-3-phosphoglycerate phosphatase. The activity is dependent on divalent cations (Mn2+, Co2+, or Mg2+). The enzyme from Persephonella marina shows moderate flexibility on the sugar donor concerning the nucleotide moiety (UDP-glucose, ADP-glucose, GDP-glucose) but is strictly specific for glucose. The enzyme is also strictly specific for 3-phospho-D-glycerate as acceptor . The enzyme from Methanococcoides burtonii is strictly specific for GDP-glucose and 3-phospho-D-glycerate . This enzyme catalyses the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria [4,5].
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Word Map
- 2.4.1.266
- mycobacteria
- tuberculosis
-
glucosylglycerate
- glycosyltransferase
- lipopolysaccharide
-
methylglucose
- gg
- d-3-phosphoglycerate
- gdp-mannose
- planctomycetes
- udp
-
phylum
- burtonii
-
methylmannose
- marina
-
deep-branching
- smegmatis
-
mannosyl-3-phosphoglycerate
-
methanococcoides
- mobilis
-
petrotoga
- gdp-glucose
-
glucosylation
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
glucosyl-3-phosphoglycerate synthase, msmeg_5084, gpgs protein, rv1208 protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glucosyl-3-phosphoglycerate synthase
glucosylphosphoglycerate synthase
GpgS
GpgS protein
RB1005
additional information
additional information
-
the enzyme belongs to the retaining family 81 glycosyltransferases
additional information
-
the enzyme belongs to the retaining family 81 glycosyltransferases
-
additional information
-
the enzyme belongs to the retaining family 81 glycosyltransferases
additional information
the enzyme belongs to the retaining family 81 glycosyltransferases
additional information
the enzyme belongs to the retaining family 81 glycosyltransferases
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
-
-
-
NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
reaction model wherein the catalytic site is essentially preformed, with a few conformational changes of lateral chain residues as the protein proceeds along the catalytic cycle
-
-
NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
front-side substrate-assisted SNi-type reaction
NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
ordered kinetic mechanism with 3-phosphoglycerate binding first, followed by UDP-glucose
NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
front-side substrate-assisted SNi-type reaction
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-
NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
ordered kinetic mechanism with 3-phosphoglycerate binding first, followed by UDP-glucose
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
NDP-glucose:3-phospho-D-glycerate 2-alpha-D-glucosyltransferase
The enzyme is involved in biosynthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate via the two-step pathway in which glucosyl-3-phosphoglycerate synthase catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-glucopyranosyl)-D-glycerate by EC 3.1.3.85 glucosyl-3-phosphoglycerate phosphatase. The activity is dependent on divalent cations (Mn2+, Co2+, or Mg2+). The enzyme from Persephonella marina shows moderate flexibility on the sugar donor concerning the nucleotide moiety (UDP-glucose, ADP-glucose, GDP-glucose) but is strictly specific for glucose. The enzyme is also strictly specific for 3-phospho-D-glycerate as acceptor [1]. The enzyme from Methanococcoides burtonii is strictly specific for GDP-glucose and 3-phospho-D-glycerate [2]. This enzyme catalyses the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria [4,5].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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)
-
-
?
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
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-
-
?
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
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-
-
?
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
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-
?
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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)
-
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?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
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involved in biosynthesis of methylated polysaccharides
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UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
involved in biosynthesis of methylated polysaccharides
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UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
involved in biosynthesis of methylated polysaccharides
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additional information
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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
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additional information
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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
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additional information
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key enzyme of glucosylglycerate synthesis
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additional information
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key enzyme of glucosylglycerate synthesis
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additional information
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key enzyme of glucosylglycerate synthesis
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Ni2+
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
additional information
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
Mg2+
strictly dependent on divalent cations in the following order of efficiency: Mn2+, Co2+, Mg2+
Mg2+
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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+
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
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
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
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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
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K+, Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+, do not stimulate GpgS activity at any concentration
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
UMP
competitive with UDP-glucose, uncompetitive with 3-phospho-D-glycerate
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Starvation
A genuine mycobacterial thermophile: Mycobacterium hassiacum growth, survival and GpgS stability at near-pasteurization temperatures.
Tuberculosis
A genuine mycobacterial thermophile: Mycobacterium hassiacum growth, survival and GpgS stability at near-pasteurization temperatures.
Tuberculosis
A Native Ternary Complex Trapped in a Crystal Reveals the Catalytic Mechanism of a Retaining Glycosyltransferase.
Tuberculosis
Biochemical characterization of the retaining glycosyltransferase glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis.
Tuberculosis
Mycobacterium tuberculosis glucosyl-3-phosphoglycerate synthase: structure of a key enzyme in methylglucose lipopolysaccharide biosynthesis.
Tuberculosis
Mycobacterium tuberculosis Rv2419c, the missing glucosyl-3-phosphoglycerate phosphatase for the second step in methylglucose lipopolysaccharide biosynthesis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics, recombinant enzyme
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additional information
additional information
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kinetics, recombinant enzyme
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additional information
additional information
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GpgSs exhibits Michaelis-Menten kinetics at 37°C
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additional information
additional information
GpgSs exhibits Michaelis-Menten kinetics at 37°C
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additional information
additional information
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GpgSs exhibits Michaelis-Menten kinetics at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM