Enzymes
UniProtKB help_outline | 1 proteins |
Enzyme class help_outline |
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Reaction participants Show >> << Hide
- Name help_outline 2-O-(α-D-glucopyranosyl)glycerol Identifier CHEBI:82766 Charge 0 Formula C9H18O8 InChIKeyhelp_outline AQTKXCPRNZDOJU-ZEBDFXRSSA-N SMILEShelp_outline OCC(CO)O[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 992 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline α-D-glucose 1-phosphate Identifier CHEBI:58601 (Beilstein: 3560164) help_outline Charge -2 Formula C6H11O9P InChIKeyhelp_outline HXXFSFRBOHSIMQ-VFUOTHLCSA-L SMILEShelp_outline OC[C@H]1O[C@H](OP([O-])([O-])=O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 41 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline glycerol Identifier CHEBI:17754 (Beilstein: 635685; CAS: 56-81-5) help_outline Charge 0 Formula C3H8O3 InChIKeyhelp_outline PEDCQBHIVMGVHV-UHFFFAOYSA-N SMILEShelp_outline OCC(O)CO 2D coordinates Mol file for the small molecule Search links Involved in 74 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:56416 | RHEA:56417 | RHEA:56418 | RHEA:56419 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Exploring the sequence diversity in glycoside hydrolase family 13_18 reveals a novel glucosylglycerol phosphorylase.
Franceus J., Decuyper L., D'hooghe M., Desmet T.
In the carbohydrate-active enzyme database, GH13_18 is a family of retaining glycoside phosphorylases that act on α-glucosides. In this work, we explored the functional diversity of this family by comparing distinctive sequence motifs in different branches of its phylogenetic tree. A glycoside pho ... >> More
In the carbohydrate-active enzyme database, GH13_18 is a family of retaining glycoside phosphorylases that act on α-glucosides. In this work, we explored the functional diversity of this family by comparing distinctive sequence motifs in different branches of its phylogenetic tree. A glycoside phosphorylase from Marinobacter adhaerens HP15 that was predicted to have a novel function was expressed and characterised. The enzyme was found to catalyse the reversible phosphorolysis of 2-O-α-D-glucosylglycerol with retention of the anomeric configuration, a specificity that has never been described before. Homology modelling, docking and mutagenesis were performed to pinpoint particular acceptor site residues (Tyr194, Ala333, Gln336) involved in the binding of glycerol. The new enzyme specificity provides additional insights into bacterial metabolic routes, being the first report of a phosphorolytic route for glucosylglycerol in a glucosylglycerol-producing organism. Furthermore, 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. Family GH13_18 has clearly proven to be more diverse than was initially assumed, and the analysis of specificity-determining sequence motifs has shown to be a straightforward and fruitful tool for enzyme discovery. << Less
Appl. Microbiol. Biotechnol. 102:3183-3191(2018) [PubMed] [EuropePMC]