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.
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.
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
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
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
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
the enzyme specificity provides additional insights into bacterial metabolic routes, describing a phosphorolytic route for glucosylglycerol in a glucosylglycerol-producing organism
the enzyme specificity provides additional insights into bacterial metabolic routes, describing a phosphorolytic route for glucosylglycerol in a glucosylglycerol-producing organism
the enzyme specificity provides additional insights into bacterial metabolic routes, describing a phosphorolytic route for glucosylglycerol in a glucosylglycerol-producing organism
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'
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'
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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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
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
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
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