Information on EC 2.4.1.268 - glucosylglycerate synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.268
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RECOMMENDED NAME
GeneOntology No.
glucosylglycerate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ADP-glucose + D-glycerate = 2-O-(alpha-D-glucopyranosyl)-D-glycerate + ADP
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glucosylglycerate biosynthesis II
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mannosylglucosylglycerate biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
ADP-glucose:D-glycerate 2-alpha-D-glucosyltransferase
Persephonella marina possesses two enzymic systems for the synthesis of glucosylglycerate. The first one is a single-step pathway in which glucosylglycerate synthase catalyses the synthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate in one-step from ADP-glucose and D-glycerate. The second system is a two-step pathway in which EC 2.4.1.266 (glucosyl-3-phosphoglycerate synthase) catalyses the conversion of NDP-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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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 + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + ADP
show the reaction diagram
ADP-glucose + glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + ADP
show the reaction diagram
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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-(alpha-D-glucosyl)-D-glycerate in one-step from 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-(alpha-D-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase (GpgP)
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?
GDP-glucose + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + GDP
show the reaction diagram
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?
UDP-glucose + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + UDP
show the reaction diagram
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?
additional information
?
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activity is not observed with: ADP-glucose, UDP-galactose, GDP-fucose, GDP-mannose or ADP-ribose. D-Glycerate is the only glucosylacceptor. No activity with mannose-6-phosphate, glucose-1-phosphate, glucose-6-phosphate, trehalose-6-phosphate, and fructose-6-phosphate or with the three-carbon compounds D-3-phosphoglycerate, D-2-phosphoglycerate, D-glycerate, L-glycerate, glycerol, and glycerol-3-phosphate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP-glucose + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + ADP
show the reaction diagram
A9BEU2
the enzyme is involved in the nonphosphorylating pathway for synthesis of the solute mannosylglucosylglycerate. In Petrotoga mobilis two alternative pathways for the synthesis of the solute mannosylglucosylglycerate are proposed. The first one is 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 during stress adaptation
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ADP-glucose + glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + ADP
show the reaction diagram
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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-(alpha-D-glucosyl)-D-glycerate in one-step from 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-(alpha-D-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase (GpgP)
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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20 mM, strongly stimulates glucosylglycerate synthase activity
Mg2+
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20 mM, strongly stimulates glucosylglycerate synthase activity
Mn2+
20 mM, stimulation. No stimulation by Mg2+, Ni2+, Co2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Zn2+
strong inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 9.3
ADP-glucose
0.9 - 3.4
D-glycerate
7.1
GDP-glucose
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pH 6.5, 70C
6.8
UDP-glucose
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pH 6.5, 70C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.4 - 67.3
D-glycerate
521
0.12
D-lactate
Rhodothermus marinus
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pH 7.8, 25C, cosubstrate: GDP-mannose
600
5 - 7.9
GDP-glucose
1105
12.6 - 68.2
GDP-mannose
366
0.22
glycolic acid
Rhodothermus marinus
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pH 7.8, 25C, cosubstrate: GDP-mannose
4251
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27.4
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pH 6.5, 70C, substrate: GDP-glucose
47
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pH 6.5, 70C, substrate: UDP-glucose
284.3
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pH 6.5, 70C, substrate: ADP-glucose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9
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pH 4.5: about 50% of maximal activity, pH 9.0: about 35% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 95
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70C: about 65% of maximal activity, 95C: about 85% of maximal activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
170000
gel filtration
210000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
half-life: 3.1 h, recombinant enzyme
70
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1 week, no loss of activity
85
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half-life: 74 h
100
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half-life: 8 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli