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Information on EC 2.4.1.266 - glucosyl-3-phosphoglycerate synthase and Organism(s) Petrotoga mobilis and UniProt Accession A9BHI9

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.266 glucosyl-3-phosphoglycerate synthase
IUBMB 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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Petrotoga mobilis
UNIPROT: A9BHI9
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The taxonomic range for the selected organisms is: Petrotoga mobilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
glucosyl-3-phosphoglycerate synthase, msmeg_5084, gpgs protein, rv1208 protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -
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].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
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
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-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
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
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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+
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+
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+
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
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-phospho-D-glycerate
progressively inhibitory above 5 mM
ADP
strong inhibitor
EDTA
0.1 mM, completely inhibits the enzyme activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 0.7
3-phospho-D-glycerate
0.9 - 1
UDP-glucose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
pH 6.0: about 80% of maximal activity, pH 8.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 75
60°C: about 85% of maximal activity, 75°C: about 60% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37100
2 * 37100, calculated from sequence
80000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 37100, calculated from sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
half-life: 6 min, addition of Co2+ had a negligible stabilizing effect, addition of both substrates increased the half-life of the enzyme to about 16 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team