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| | <StructureSection load='5man' size='340' side='right'caption='[[5man]], [[Resolution|resolution]] 2.04Å' scene=''> | | <StructureSection load='5man' size='340' side='right'caption='[[5man]], [[Resolution|resolution]] 2.04Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5man]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/As_1.2190 As 1.2190]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MAN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MAN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5man]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_adolescentis Bifidobacterium adolescentis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MAN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sucP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1680 AS 1.2190])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900052:alpha-nigerose'>PRD_900052</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.7 2.4.1.7] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5man OCA], [https://pdbe.org/5man PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5man RCSB], [https://www.ebi.ac.uk/pdbsum/5man PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5man ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5man OCA], [http://pdbe.org/5man PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5man RCSB], [http://www.ebi.ac.uk/pdbsum/5man PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5man ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SUCP_BIFAA SUCP_BIFAA] Catalyzes the reversible phosphorolysis of sucrose into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose (PubMed:14740189, PubMed:20691225). Is involved in sucrose degradation. Also displays transglucosylation activity in vitro, by transferring the glucosyl moiety of Glc1P to a broad range of monomeric sugars, such as D- and L-arabinose, D- and L-arabitol, and xylitol (PubMed:14740189).<ref>PMID:14740189</ref> <ref>PMID:20691225</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: As 1 2190]] | + | [[Category: Bifidobacterium adolescentis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Transferase]]
| + | [[Category: Grimm C]] |
| - | [[Category: Grimm, C]] | + | [[Category: Kraus M]] |
| - | [[Category: Kraus, M]] | + | |
| - | [[Category: Enzyme design]]
| + | |
| - | [[Category: Resveratrol]]
| + | |
| - | [[Category: Sucrose phosphorylase]]
| + | |
| Structural highlights
Function
SUCP_BIFAA Catalyzes the reversible phosphorolysis of sucrose into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose (PubMed:14740189, PubMed:20691225). Is involved in sucrose degradation. Also displays transglucosylation activity in vitro, by transferring the glucosyl moiety of Glc1P to a broad range of monomeric sugars, such as D- and L-arabinose, D- and L-arabitol, and xylitol (PubMed:14740189).[1] [2]
Publication Abstract from PubMed
Here we present a point mutation-triggered domain shift which switches the acceptor preference of a sucrose phosphorylase from phosphate to a variety of large polyphenolic compounds including resveratrol and quercetin, enabling their efficient glucosylation. The variant possesses a high affinity for aromatic substrates due to newly introduced pi-pi- and hydrophobic interactions in the altered active site. The domain shift brings about a substantially enlarged and multifunctional active site for polyphenol glucosylation and rare disaccharide production. The crystal structure of the variant with its product resveratrol-3-alpha-d-glucoside allows the prediction of the substrate scope and regioselectivity of the aromatic compounds' glucosylation sites.
Switching enzyme specificity from phosphate to resveratrol glucosylation.,Kraus M, Grimm C, Seibel J Chem Commun (Camb). 2017 Nov 9;53(90):12181-12184. doi: 10.1039/c7cc05993k. PMID:29057405[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van den Broek LA, van Boxtel EL, Kievit RP, Verhoef R, Beldman G, Voragen AG. Physico-chemical and transglucosylation properties of recombinant sucrose phosphorylase from Bifidobacterium adolescentis DSM20083. Appl Microbiol Biotechnol. 2004 Aug;65(2):219-27. Epub 2004 Jan 22. PMID:14740189 doi:http://dx.doi.org/10.1007/s00253-003-1534-x
- ↑ Cerdobbel A, Desmet T, De Winter K, Maertens J, Soetaert W. Increasing the thermostability of sucrose phosphorylase by multipoint covalent immobilization. J Biotechnol. 2010 Oct 1;150(1):125-30. doi: 10.1016/j.jbiotec.2010.07.029. Epub , 2010 Aug 4. PMID:20691225 doi:http://dx.doi.org/10.1016/j.jbiotec.2010.07.029
- ↑ Kraus M, Grimm C, Seibel J. Switching enzyme specificity from phosphate to resveratrol glucosylation. Chem Commun (Camb). 2017 Nov 9;53(90):12181-12184. doi: 10.1039/c7cc05993k. PMID:29057405 doi:http://dx.doi.org/10.1039/c7cc05993k
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