View source for 9fd8


==Re-engineered peroxygenase variant of 2-deoxy-D-ribose-5-phosphate aldolase, Schiff-base complex with 4-chloro-cinnamaldehyde==
<StructureSection load='9fd8' size='340' side='right'caption='[[9fd8]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9fd8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9FD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FD8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1ICA:(~{E})-3-(4-chlorophenyl)prop-2-en-1-ol'>A1ICA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=9fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fd8 OCA], [https://pdbe.org/9fd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fd8 RCSB], [https://www.ebi.ac.uk/pdbsum/9fd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fd8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DEOC_ECOLC DEOC_ECOLC] Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The enzyme 2-deoxy-D-ribose-5-phosphate aldolase (DERA) naturally catalyzes the reversible aldol addition between acetaldehyde and D-glyceraldehyde-3-phosphate to yield 2-deoxy-D-ribose-5-phosphate. Herein we describe the redesign of DERA into a proficient non-natural peroxygenase that promotes the asymmetric epoxidation of various alpha,beta-unsaturated aldehydes. This repurposed aldolase, named DERA-EP, is able to utilize H(2)O(2) to accomplish both anti- and syn-selective epoxidations of various alpha,beta-unsaturated aldehydes to give the corresponding epoxides with moderate to high diastereoselectivity (diastereomeric ratio up to 99 : 1) and excellent enantioselectivity (enantiomeric ratio up to 99 : 1). Crystallographic analysis of DERA-EP in a substrate-free and substrate-bound state provides a structural context for the evolved activity, a clear explanation for the high enantioselectivity, and compelling evidence for catalysis via enzyme-bound iminium ion intermediates. The unprecedented anti-selectivity of DERA-EP with multiple alpha,beta-unsaturated aldehydes is complementary to the syn-selectivity of previously reported enzyme-, metal- and organo-catalysts, making DERA-EP an attractive new asset to the toolbox of epoxidation catalysts.

Engineering 2-Deoxy-D-ribose-5-phosphate Aldolase for anti- and syn-Selective Epoxidations of alpha,beta-Unsaturated Aldehydes.,Zhou H, Kunzendorf A, Xu G, Frietema HOT, Thunnissen AWH, Poelarends GJ Angew Chem Int Ed Engl. 2025 Feb 24:e202503054. doi: 10.1002/anie.202503054. PMID:39993220<ref>PMID:39993220</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9fd8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Frietema HOT]]
[[Category: Poelarends GJ]]
[[Category: Thunnissen AMWH]]
[[Category: Zhou H]]