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| | <StructureSection load='4ufp' size='340' side='right'caption='[[4ufp]], [[Resolution|resolution]] 2.95Å' scene=''> | | <StructureSection load='4ufp' size='340' side='right'caption='[[4ufp]], [[Resolution|resolution]] 2.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ufp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Potato Potato]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UFP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UFP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ufp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UFP FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ufn|4ufn]], [[4ufo|4ufo]]</td></tr> | + | </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=4ufp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ufp OCA], [https://pdbe.org/4ufp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ufp RCSB], [https://www.ebi.ac.uk/pdbsum/4ufp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ufp ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 and 3.3.2.10 3.3.2.9 and 3.3.2.10] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ufp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ufp OCA], [http://pdbe.org/4ufp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ufp RCSB], [http://www.ebi.ac.uk/pdbsum/4ufp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ufp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q41415_SOLTU Q41415_SOLTU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Epoxide hydrolase|Epoxide hydrolase]] | + | *[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hydrolase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Potato]] | + | [[Category: Solanum tuberosum]] |
| - | [[Category: Bauer, P]] | + | [[Category: Bauer P]] |
| - | [[Category: Carlsson, A J]] | + | [[Category: Carlsson AJ]] |
| - | [[Category: Dobritzsch, D]] | + | [[Category: Dobritzsch D]] |
| - | [[Category: Kamerlin, S C.L]] | + | [[Category: Kamerlin SCL]] |
| - | [[Category: Nilsson, M]] | + | [[Category: Nilsson M]] |
| - | [[Category: Widersten, M]] | + | [[Category: Widersten M]] |
| - | [[Category: Alpha/beta-hydrolase]]
| + | |
| - | [[Category: Asymmetric synthese]]
| + | |
| - | [[Category: Directed evolution]]
| + | |
| - | [[Category: Epoxide hydrolysis]]
| + | |
| Structural highlights
Function
Q41415_SOLTU
Publication Abstract from PubMed
Engineered enzyme variants of potato epoxide hydrolase (StEH1) display varying degrees of enrichment of (2R)-3-phenylpropane-1,2-diol from racemic benzyloxirane. Curiously, the observed increase in the enantiomeric excess of the (R)-diol is not only due to changes in enantioselectivity for the preferred epoxide enantiomer, but also to changes in the regioselectivity of the epoxide ring opening of (S)-benzyloxirane. To probe the structural origin of these differences in substrate selectivities and catalytic regiopreferences, we have solved the crystal structures for the in-vitro evolved StEH1 variants. We have additionally used these structures as a starting point for docking the epoxide enantiomers into the respective active sites. Interestingly, despite the simplicity of our docking calculations, the apparent preferred binding modes obtained from the docking appears to rationalize the experimentally determined regioselectivities. These calculations could also identify an active site residue (F33) as a putatively important interaction partner, a role that could explain the high degree of conservation of this residue during evolution. Overall, our combined experimental, structural and computational studies of this system provide snapshots into the evolution of enantioconvergence in StEH1 catalyzed epoxide hydrolysis.
Laboratory Evolved Enzymes Provide Snapshots of the Development of Enantioconvergence in Enzyme-Catalyzed Epoxide Hydrolysis.,Janfalk Carlsson A, Bauer P, Dobritzsch D, Nilsson M, Kamerlin SC, Widersten M Chembiochem. 2016 Jul 7. doi: 10.1002/cbic.201600330. PMID:27383542[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Janfalk Carlsson A, Bauer P, Dobritzsch D, Nilsson M, Kamerlin SC, Widersten M. Laboratory Evolved Enzymes Provide Snapshots of the Development of Enantioconvergence in Enzyme-Catalyzed Epoxide Hydrolysis. Chembiochem. 2016 Jul 7. doi: 10.1002/cbic.201600330. PMID:27383542 doi:http://dx.doi.org/10.1002/cbic.201600330
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