View source for 5l53


==Menthone neomenthol reductase from Mentha piperita in complex with NADP==
<StructureSection load='5l53' size='340' side='right'caption='[[5l53]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5l53]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mentha_x_piperita Mentha x piperita]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L53 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]] 2.24&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=5l53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l53 OCA], [https://pdbe.org/5l53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l53 RCSB], [https://www.ebi.ac.uk/pdbsum/5l53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l53 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q06ZW2_MENPI Q06ZW2_MENPI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Three enzymes of the Mentha essential oil biosynthetic pathway are highly homologous, namely the ketoreductases (-)-menthone:(-)-menthol reductase and (-)-menthone:(+)-neomenthol reductase, and the "ene" reductase isopiperitenone reductase. We identified a rare catalytic residue substitution in the last two, and performed comparative crystal structure analyses and residue-swapping mutagenesis to investigate whether this determines the reaction outcome. The result was a complete loss of native activity and a switch between ene reduction and ketoreduction. This suggests the importance of a catalytic glutamate vs. tyrosine residue in determining the outcome of the reduction of alpha,beta-unsaturated alkenes, due to the substrate occupying different binding conformations, and possibly also to the relative acidities of the two residues. This simple switch in mechanism by a single amino acid substitution could potentially generate a large number of de novo ene reductases.

Pinpointing a Mechanistic Switch Between Ketoreduction and "Ene" Reduction in Short-Chain Dehydrogenases/Reductases.,Lygidakis A, Karuppiah V, Hoeven R, Ni Cheallaigh A, Leys D, Gardiner JM, Toogood HS, Scrutton NS Angew Chem Int Ed Engl. 2016 Aug 8;55(33):9596-600. doi: 10.1002/anie.201603785. , Epub 2016 Jul 13. PMID:27411040<ref>PMID:27411040</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5l53" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mentha x piperita]]
[[Category: Karuppiah V]]
[[Category: Leys D]]
[[Category: Scrutton NS]]
[[Category: Toogood HS]]