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| | <StructureSection load='7bwb' size='340' side='right'caption='[[7bwb]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='7bwb' size='340' side='right'caption='[[7bwb]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7bwb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bommo Bommo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BWB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7BWB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7bwb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BWB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BWB FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BmSuc1, Suc1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7091 BOMMO])</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]] 1.8Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-fructofuranosidase Beta-fructofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.26 3.2.1.26] </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=7bwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bwb OCA], [https://pdbe.org/7bwb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bwb RCSB], [https://www.ebi.ac.uk/pdbsum/7bwb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bwb 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=7bwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bwb OCA], [http://pdbe.org/7bwb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7bwb RCSB], [http://www.ebi.ac.uk/pdbsum/7bwb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7bwb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A6F8Z6Y2_BOMMO A0A6F8Z6Y2_BOMMO] |
| | <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: Beta-fructofuranosidase]] | + | [[Category: Bombyx mori]] |
| - | [[Category: Bommo]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Miyazaki, T]] | + | [[Category: Miyazaki T]] |
| - | [[Category: Oba, N]] | + | [[Category: Oba N]] |
| - | [[Category: Beta-propeller]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Horizontal gene transfer]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Sucrose]]
| + | |
| Structural highlights
Function
A0A6F8Z6Y2_BOMMO
Publication Abstract from PubMed
Sucrose-hydrolyzing enzymes are largely divided into beta-fructofuranosidase and sucrose alpha-glucosidase. The domestic silkworm Bombyx mori possesses both enzymes, BmSUC1 and BmSUH, belonging to the glycoside hydrolase family 32 (GH32) and GH13, respectively. BmSUC1 was presumed to be acquired by horizontal gene transfer from bacteria based on phylogenetic analysis and related to tolerance to sugar-mimic alkaloids contained in mulberry latex. Here we investigated the substrate specificity of recombinant BmSUC1 that can hydrolyze not only sucrose but also fructooligosaccharides and fructans, and revealed that the enzyme was competitively inhibited by 1,4-dideoxy-1,4-imino-D-arabinitol, one of the alkaloids. Moreover, the crystal structures of BmSUC1 in apo form and complex with sucrose were determined, and the active site pocket was shallow and suitable for shorter substrates but was related to more relaxed substrate specificity than the strict sucrose alpha-glucosidase BmSUH. Considering together with the distribution of BmSUC1-orthologous genes in many lepidopterans, our results suggest that BmSUC1 contributes to the digestion of fructooligosaccharides and fructans derived from feed plants.
Structural insight into the substrate specificity of Bombyx mori beta-fructofuranosidase belonging to the glycoside hydrolase family 32.,Miyazaki T, Oba N, Park EY Insect Biochem Mol Biol. 2020 Oct 24;127:103494. doi: 10.1016/j.ibmb.2020.103494. PMID:33132139[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miyazaki T, Oba N, Park EY. Structural insight into the substrate specificity of Bombyx mori beta-fructofuranosidase belonging to the glycoside hydrolase family 32. Insect Biochem Mol Biol. 2020 Oct 24;127:103494. doi: 10.1016/j.ibmb.2020.103494. PMID:33132139 doi:http://dx.doi.org/10.1016/j.ibmb.2020.103494
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