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| | <StructureSection load='5l53' size='340' side='right'caption='[[5l53]], [[Resolution|resolution]] 2.24Å' scene=''> | | <StructureSection load='5l53' size='340' side='right'caption='[[5l53]], [[Resolution|resolution]] 2.24Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5l53]] is a 1 chain structure. 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 [http://proteopedia.org/fgij/fg.htm?mol=5L53 FirstGlance]. <br> | + | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.24Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/(+)-neomenthol_dehydrogenase (+)-neomenthol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.208 1.1.1.208] </span></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'>[http://proteopedia.org/fgij/fg.htm?mol=5l53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l53 OCA], [http://pdbe.org/5l53 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l53 RCSB], [http://www.ebi.ac.uk/pdbsum/5l53 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l53 ProSAT]</span></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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q06ZW2_MENPI Q06ZW2_MENPI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Karuppiah, V]] | + | [[Category: Mentha x piperita]] |
| - | [[Category: Leys, D]] | + | [[Category: Karuppiah V]] |
| - | [[Category: Scrutton, N S]] | + | [[Category: Leys D]] |
| - | [[Category: Toogood, H S]] | + | [[Category: Scrutton NS]] |
| - | [[Category: Isomenthone]] | + | [[Category: Toogood HS]] |
| - | [[Category: Menthone]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
Q06ZW2_MENPI
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lygidakis A, Karuppiah V, Hoeven R, Ni Cheallaigh A, Leys D, Gardiner JM, Toogood HS, Scrutton NS. Pinpointing a Mechanistic Switch Between Ketoreduction and "Ene" Reduction in Short-Chain Dehydrogenases/Reductases. Angew Chem Int Ed Engl. 2016 Aug 8;55(33):9596-600. doi: 10.1002/anie.201603785. , Epub 2016 Jul 13. PMID:27411040 doi:http://dx.doi.org/10.1002/anie.201603785
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