View source for 9kuh


==Co-crystal structure of wild-type OYE2 with 2-(prop-1-en-2-yl)pyridine==
<StructureSection load='9kuh' size='340' side='right'caption='[[9kuh]], [[Resolution|resolution]] 3.43&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9kuh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9KUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9KUH 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]] 3.43&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1EG5:2-prop-1-en-2-ylpyridine'>A1EG5</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=9kuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9kuh OCA], [https://pdbe.org/9kuh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9kuh RCSB], [https://www.ebi.ac.uk/pdbsum/9kuh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9kuh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OYE2_YEAST OYE2_YEAST] Flavin-dependent enoate reductase that catalyzes the chemo- and stereoslective hydrogenation of electron-poor alkenes. The enzyme is reduced by NADPH, and oxygen, quinones, and alpha,beta-unsaturated aldehydes and ketones can act as electron acceptors to complete catalytic turnover. The physiological oxidant remains elusive (By similarity). Has an antioxidant activity, reducing reactive oxygen species (ROS) levels when overexpressed. Formation of OYE2-OYE3 heterodimers contribute to the induction of programmed cell death upon oxidative stress (PubMed:17897954).[UniProtKB:Q02899]<ref>PMID:17897954</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Organic nitriles are significant in pharmaceuticals, agrochemicals, cosmetics, and materials. Although numerous cyanidation methods have been developed, more eco-friendly and green protocols for manufacturing alkyl nitriles are in high demand. Here, we report a photoenzymatic enantioselective intermolecular hydrocyanoalkylation of alkenes catalyzed by flavin-dependent "ene"-reductases. The discovery of stereocomplementary enzymes that provide access to both enantiomers of the high-value nitriles further showcases the synthetic applications of this method. Radical trapping, isotopic labeling, and spectroscopic experiments have elucidated the formation of a charge transfer complex at the protein active site. The single-electron reduction of the cyanoalkyl radical precursor by flavin hydroquinone yields a cyanoalkyl radical, which then undergoes intermolecular radical addition. This active site can stereoselectively control the radical-terminating hydrogen atom transfer, enabling the synthesis of enantioenriched gamma-stereogenic nitriles. This work further expands the reactivity repertoire of biocatalytic transformations via non-natural radical mechanisms.

Enantioselective Radical Hydrocyanoalkylation of Alkenes via Photoenzymatic Catalysis.,Wu D, Sun Z, Wang S, Yang J, He J, Lei X JACS Au. 2025 Jul 11;5(7):3625-3631. doi: 10.1021/jacsau.5c00633. eCollection , 2025 Jul 28. PMID:40747066<ref>PMID:40747066</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9kuh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Wu DS]]
[[Category: Yang J]]