Enzymes
| UniProtKB help_outline | 261 proteins |
| Enzyme class help_outline |
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- Name help_outline sucrose 6F-phosphate Identifier CHEBI:57723 (Beilstein: 3918937) help_outline Charge -2 Formula C12H21O14P InChIKeyhelp_outline PJTTXANTBQDXME-UGDNZRGBSA-L SMILEShelp_outline OC[C@H]1O[C@H](O[C@]2(CO)O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@@H]2O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 4 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 1,002 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline β-D-fructose 6-phosphate Identifier CHEBI:57634 (Beilstein: 6422468) help_outline Charge -2 Formula C6H11O9P InChIKeyhelp_outline BGWGXPAPYGQALX-ARQDHWQXSA-L SMILEShelp_outline OC[C@@]1(O)O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 18 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 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
Cross-references
| RHEA:38863 | RHEA:38864 | RHEA:38865 | RHEA:38866 | |
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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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The quest for a thermostable sucrose phosphorylase reveals sucrose 6'-phosphate phosphorylase as a novel specificity.
Verhaeghe T., Aerts D., Diricks M., Soetaert W., Desmet T.
Sucrose phosphorylase is a promising biocatalyst for the glycosylation of a wide range of compounds, but its industrial application has been hampered by the low thermostability of known representatives. Hence, in this study, the putative sucrose phosphorylase from the thermophile Thermoanaerobacte ... >> More
Sucrose phosphorylase is a promising biocatalyst for the glycosylation of a wide range of compounds, but its industrial application has been hampered by the low thermostability of known representatives. Hence, in this study, the putative sucrose phosphorylase from the thermophile Thermoanaerobacterium thermosaccharolyticum was recombinantly expressed and fully characterised. The enzyme showed significant activity on sucrose (optimum at 55 °C), and with a melting temperature of 79 °C and a half-life of 60 h at the industrially relevant temperature of 60 °C, it is far more stable than known sucrose phosphorylases. Substrate screening and detailed kinetic characterisation revealed however a preference for sucrose 6'-phosphate over sucrose. The enzyme can thus be considered as a sucrose 6'-phosphate phosphorylase, a specificity not yet reported to date. Homology modelling and mutagenesis pointed out particular residues (Arg134 and His344) accounting for the difference in specificity. Moreover, phylogenetic and sequence analysis suggest that glycoside hydrolase 13 subfamily 18 might harbour even more specificities. In addition, the second gene residing in the same operon as sucrose 6'-phosphate phosphorylase was identified as well, and found to be a phosphofructokinase. The concerted action of both these enzymes implies a new pathway for the breakdown of sucrose, in which the reaction products end up at different stages of the glycolysis. << Less
Appl. Microbiol. Biotechnol. 98:7027-7037(2014) [PubMed] [EuropePMC]