View source for 7ywv


==Eugenol oxidase from rhodococcus jostii: mutant S81H, D151E, A423M, H434Y, S394V, Q425S, I445D, S518P==
<StructureSection load='7ywv' size='340' side='right'caption='[[7ywv]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ywv]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_jostii_RHA1 Rhodococcus jostii RHA1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YWV 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EOL:2-METHOXY-4-(PROP-2-EN-1-YL)PHENOL'>EOL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=7ywv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ywv OCA], [https://pdbe.org/7ywv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ywv RCSB], [https://www.ebi.ac.uk/pdbsum/7ywv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ywv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q0SBK1_RHOJR Q0SBK1_RHOJR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Various 4-alkylphenols can be easily obtained through reductive catalytic fractionation of lignocellulosic biomass. Selective dehydrogenation of 4-n-propylguaiacol results in the formation of isoeugenol, a valuable flavor and fragrance molecule and versatile precursor compound. Here we present the engineering of a bacterial eugenol oxidase to catalyze this reaction. Five mutations, identified from computational predictions, are first introduced to render the enzyme more thermostable. Other mutations are then added and analyzed to enhance chemoselectivity and activity. Structural insight demonstrates that the slow catalytic activity of an otherwise promising enzyme variant is due the formation of a slowly-decaying covalent substrate-flavin cofactor adduct that can be remedied by targeted residue changes. The final engineered variant comprises eight mutations, is thermostable, displays good activity and acts as a highly chemoselective 4-n-propylguaiacol oxidase. We lastly use our engineered biocatalyst in an illustrative preparative reaction at gram-scale. Our findings show that a natural enzyme can be redesigned into a tailored biocatalyst capable of valorizing lignin-based monophenols.

Structure- and computational-aided engineering of an oxidase to produce isoeugenol from a lignin-derived compound.,Guo Y, Alvigini L, Trajkovic M, Alonso-Cotchico L, Monza E, Savino S, Maric I, Mattevi A, Fraaije MW Nat Commun. 2022 Nov 23;13(1):7195. doi: 10.1038/s41467-022-34912-3. PMID:36418310<ref>PMID:36418310</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ywv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodococcus jostii RHA1]]
[[Category: Alvigini L]]
[[Category: Mattevi A]]