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Information on EC 2.4.1.359 - glucosylglycerol phosphorylase (configuration-retaining)
for references in articles please use BRENDA:EC2.4.1.359
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.359 glucosylglycerol phosphorylase (configuration-retaining)
IUBMB Comments
The enzyme, characterized from the halotolerant bacterium Marinobacter adhaerens, is likely responsible for degradation of the compatible solute 2-O-α-D-glucopyranosyl-glycerol when the environmental salt concentration decreases. cf. EC 2.4.1.332, 1,2-α-glucosylglycerol phosphorylase.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 2.4.1.359
- starch
-
1-phosphate
- phosphoglucomutase
-
1,6-bisphosphate
- glucose-1-phosphate
-
2.7.5.1
-
hardy-weinberg
- li+
-
bloodstains
-
diptera
-
plastidial
-
codominant
- phosphomannomutase
-
allozymes
-
glc-1-p
- alpha-d-glucose
Reaction Schemes
showSynonyms
glucosylglycerol phosphorylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-O-alpha-D-glucopyranosylglycerol:phosphate alpha-D-glucosyltransferase
-
2-O-alpha-D-glucosylglycerol phosphorylase (retaining)
GGoP
glucosylglycerol phosphorylase
GtfA
MaGGoP
2-O-alpha-D-glucosylglycerol phosphorylase (retaining)
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-O-alpha-D-glucopyranosyl-glycerol + phosphate = alpha-D-glucose 1-phosphate + glycerol
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-
-
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SYSTEMATIC NAME
IUBMB Comments
2-O-alpha-D-glucopyranosyl-glycerol:phosphate alpha-D-glucosyltransferase (configuration-retaining)
The enzyme, characterized from the halotolerant bacterium Marinobacter adhaerens, is likely responsible for degradation of the compatible solute 2-O-alpha-D-glucopyranosyl-glycerol when the environmental salt concentration decreases. cf. EC 2.4.1.332, 1,2-alpha-glucosylglycerol phosphorylase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
alpha-D-glucopyranose 1-phosphate + D-glycerate
Substrates: degradation in vitro is a successive process of phosphorolysis and hydrolysis
Products: -
Products: -
?
alpha-D-glucose 1-phosphate + 1,2-propanediol
2-O-(alpha-D-glucopyranosyl)propanediol + phosphate
2-O-(alpha-D-glucopyranosyl)glycerol + phosphate
alpha-D-glucose 1-phosphate + glycerol
Substrates: -
Products: -
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r
2-O-(alpha-D-glucopyranosyl)glycerol + phosphate
alpha-D-glucose 1-phosphate + glycerol
Substrates: -
Products: -
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r
2-O-(alpha-D-glucopyranosyl)glycerol + phosphate
alpha-D-glucose 1-phosphate + glycerol
Substrates: -
Products: -
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r
alpha-D-glucose 1-phosphate + 1,2-propanediol
2-O-(alpha-D-glucopyranosyl)propanediol + phosphate
Substrates: -
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r
alpha-D-glucose 1-phosphate + 1,2-propanediol
2-O-(alpha-D-glucopyranosyl)propanediol + phosphate
Substrates: -
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r
alpha-D-glucose 1-phosphate + 1,2-propanediol
2-O-(alpha-D-glucopyranosyl)propanediol + phosphate
Substrates: -
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r
alpha-D-glucose 1-phosphate + glycerol
2-O-(alpha-D-glucopyranosyl)glycerol + phosphate
Substrates: -
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r
alpha-D-glucose 1-phosphate + glycerol
2-O-(alpha-D-glucopyranosyl)glycerol + phosphate
Substrates: -
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r
alpha-D-glucose 1-phosphate + glycerol
2-O-(alpha-D-glucopyranosyl)glycerol + phosphate
Substrates: -
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r
additional information
?
-
Substrates: no transglucosylation activity with fructose, fructose 6-phosphate or glycerate as acceptors
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?
additional information
?
-
Substrates: the enzyme catalyses the reversible phosphorolysis of 2-O-alpha-D-glucosylglycerol with retention of the anomeric configuration. Homology modelling, docking and mutagenesis are performed to pinpoint particular acceptor site residues (Tyr194, Ala333, Gln336) involved in the binding of glycerol. In the phosphorolytic direction, the enzyme is active on glucosylglycerol but not on sucrose or glucosylglycerate. A variety of other acceptors are surveyed as well, but significant activity can only be observed using 1,2-propanediol. No transglucosylation activity is detected when fructose, fructose 6-phosphate, or glycerate are supplied as acceptor
Products: -
Products: -
?
additional information
?
-
Substrates: no transglucosylation activity with fructose, fructose 6-phosphate or glycerate as acceptors
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyses the reversible phosphorolysis of 2-O-alpha-D-glucosylglycerol with retention of the anomeric configuration. Homology modelling, docking and mutagenesis are performed to pinpoint particular acceptor site residues (Tyr194, Ala333, Gln336) involved in the binding of glycerol. In the phosphorolytic direction, the enzyme is active on glucosylglycerol but not on sucrose or glucosylglycerate. A variety of other acceptors are surveyed as well, but significant activity can only be observed using 1,2-propanediol. No transglucosylation activity is detected when fructose, fructose 6-phosphate, or glycerate are supplied as acceptor
Products: -
Products: -
?
additional information
?
-
Substrates: no transglucosylation activity with fructose, fructose 6-phosphate or glycerate as acceptors
Products: -
Products: -
?
additional information
?
-
-
Substrates: no transglucosylation activity with fructose, fructose 6-phosphate or glycerate as acceptors
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyses the reversible phosphorolysis of 2-O-alpha-D-glucosylglycerol with retention of the anomeric configuration. Homology modelling, docking and mutagenesis are performed to pinpoint particular acceptor site residues (Tyr194, Ala333, Gln336) involved in the binding of glycerol. In the phosphorolytic direction, the enzyme is active on glucosylglycerol but not on sucrose or glucosylglycerate. A variety of other acceptors are surveyed as well, but significant activity can only be observed using 1,2-propanediol. No transglucosylation activity is detected when fructose, fructose 6-phosphate, or glycerate are supplied as acceptor
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyses the reversible phosphorolysis of 2-O-alpha-D-glucosylglycerol with retention of the anomeric configuration. Homology modelling, docking and mutagenesis are performed to pinpoint particular acceptor site residues (Tyr194, Ala333, Gln336) involved in the binding of glycerol. In the phosphorolytic direction, the enzyme is active on glucosylglycerol but not on sucrose or glucosylglycerate. A variety of other acceptors are surveyed as well, but significant activity can only be observed using 1,2-propanediol. No transglucosylation activity is detected when fructose, fructose 6-phosphate, or glycerate are supplied as acceptor
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: sucrose, cellobiose, trehalose, melibiose, maltose, lactose, and kojibiose
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-O-(alpha-D-glucopyranosyl)glycerol + phosphate
alpha-D-glucose 1-phosphate + glycerol
Substrates: -
Products: -
Products: -
r
2-O-(alpha-D-glucopyranosyl)glycerol + phosphate
alpha-D-glucose 1-phosphate + glycerol
Substrates: -
Products: -
Products: -
r
2-O-(alpha-D-glucopyranosyl)glycerol + phosphate
alpha-D-glucose 1-phosphate + glycerol
Substrates: -
Products: -
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r
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
slight activation up to 0.2 M, about 60% inhibition at 0.8 M, almost complete inhibition at 1.2 M
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
3.9
2-O-(alpha-D-glucopyranosyl)glycerol
recombinant enzyme, pH 6.5, 37°C
10
2-O-(alpha-D-glucopyranosyl)glycerol
recombinant enzyme, pH 6.5, 37°C
2.5
alpha-D-glucose 1-phosphate
recombinant enzyme, pH 6.5, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14
2-O-(alpha-D-glucopyranosyl)glycerol
recombinant enzyme, pH 6.5, 37°C
3 - 6
alpha-D-glucose 1-phosphate
recombinant enzyme, pH 6.5, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
2-O-(alpha-D-glucopyranosyl)glycerol
recombinant enzyme, pH 6.5, 37°C
3.6
2-O-(alpha-D-glucopyranosyl)glycerol
recombinant enzyme, pH 6.5, 37°C
14.4
alpha-D-glucose 1-phosphate
recombinant enzyme, pH 6.5, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12.7
purified recombinant enzyme, pH 6.5, 37°C, phosphorolytic activity
17
substrate 2-O-(alpha-D-glucopyranosyl)glycerol, pH 6.5, 37°C
33
45.2
purified recombinant enzyme, pH 6.5, 37°C, synthetic activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7.5
over 20% of maximal activity within this range, profile overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
heterologous expression of GGP in cyanobacterium Synechocystis sp. PCC 6803 significantly reduces the salt-induced glucosylglycerol accumulation
additional information
evolution
the enzyme belongs to the glycoside hydrolase GH13_18 family, simplified phylogenetic tree
evolution
-
the enzyme belongs to the glycoside hydrolase GH13_18 family, simplified phylogenetic tree
-
evolution
-
the enzyme belongs to the glycoside hydrolase GH13_18 family, simplified phylogenetic tree
-
metabolism
the enzyme specificity provides additional insights into bacterial metabolic routes, describing a phosphorolytic route for glucosylglycerol in a glucosylglycerol-producing organism
metabolism
-
the enzyme specificity provides additional insights into bacterial metabolic routes, describing a phosphorolytic route for glucosylglycerol in a glucosylglycerol-producing organism
-
metabolism
-
the enzyme specificity provides additional insights into bacterial metabolic routes, describing a phosphorolytic route for glucosylglycerol in a glucosylglycerol-producing organism
-
additional information
homology structure modeling using the crystal structure from the Bifidobacterium adolescentis sucrose phosphorylase (PDB IDs 1R7A, 2GDU, 2GDV) as template, docking study and enzyme-substrate interactions analysis, overview. Tyr194 and Gln336 each seemingly form a hydrogen bond with a hydroxyl group of glycerol, while Ala333 is situated at a suitable location for hydrophobic interaction with atom C1'
additional information
-
homology structure modeling using the crystal structure from the Bifidobacterium adolescentis sucrose phosphorylase (PDB IDs 1R7A, 2GDU, 2GDV) as template, docking study and enzyme-substrate interactions analysis, overview. Tyr194 and Gln336 each seemingly form a hydrogen bond with a hydroxyl group of glycerol, while Ala333 is situated at a suitable location for hydrophobic interaction with atom C1'
-
additional information
-
homology structure modeling using the crystal structure from the Bifidobacterium adolescentis sucrose phosphorylase (PDB IDs 1R7A, 2GDU, 2GDV) as template, docking study and enzyme-substrate interactions analysis, overview. Tyr194 and Gln336 each seemingly form a hydrogen bond with a hydroxyl group of glycerol, while Ala333 is situated at a suitable location for hydrophobic interaction with atom C1'
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GGOP_MARAH
Marinobacter adhaerens (strain DSM 23420 / HP15)
480
0
54825
Swiss-Prot
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure. Residues Tyr194 and Gln336 each form a hydrogen bond with a hydroxyl group of glycerol, while Ala333 is situated at a suitable location for hydrophobic interaction with atom C1
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q336A
Q336A
Q336A
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ecombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gtfA, sequence comparisons and phylogenetic tree, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
glucosylglycerol phosphorylase might be an attractive biocatalyst for the production of the osmolyte glucosylglycerol, which is currently produced on industrial scale by exploiting a side activity of the closely related sucrose phosphorylase
synthesis
-
glucosylglycerol phosphorylase might be an attractive biocatalyst for the production of the osmolyte glucosylglycerol, which is currently produced on industrial scale by exploiting a side activity of the closely related sucrose phosphorylase
-
synthesis
-
glucosylglycerol phosphorylase might be an attractive biocatalyst for the production of the osmolyte glucosylglycerol, which is currently produced on industrial scale by exploiting a side activity of the closely related sucrose phosphorylase
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Franceus, J.; Decuyper, L.; Dhooghe, M.; Desmet, T.
Exploring the sequence diversity in glycoside hydrolase family 13_18 reveals a novel glucosylglycerol phosphorylase
Appl. Microbiol. Biotechnol.
102
3183-3191
2018
Marinobacter adhaerens (E4PMA5), Marinobacter adhaerens DSM 23420 (E4PMA5), Marinobacter adhaerens HP15 (E4PMA5), Marinobacter adhaerens HP15
brenda
Cheng, L.; Zhang, Z.; Zhu, D.; Luo, Q.; Lu, X.
Glucosylglycerol phosphorylase, a potential novel pathway of microbial glucosylglycerol catabolism
Appl. Microbiol. Biotechnol.
108
214
2024
Marinobacter salinexigens (A0A5B0VBK8)
brenda
EXTERNAL LINKS (specific for EC-Number 2.4.1.359)
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