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5l4s

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Isopiperitenone reductase from Mentha piperita in complex with NADP and beta-Cyclocitral

Structural highlights

5l4s is a 1 chain structure with sequence from Mentha x piperita. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.41Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IPIPR_MENPI Monoterpene synthase that catalyzes the specific reduction of the 1(2)-double bond of (-)-isopiperitenone to produce (+)-cis-isopulegone. Does not catalyze the reverse reaction. Unable to reduce (+)-pulegone, (+)-cis-isopulegone, (-)-menthone or the 1,2-double bond of (-)-carvone. Able to utilize NADH with 20% the efficiency of NADPH.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5l4s"

@@ Line 1: / Line 1: @@
 ==Isopiperitenone reductase from Mentha piperita in complex with NADP and beta-Cyclocitral==
-<StructureSection load='5l4s' size='340' side='right' caption='[[5l4s]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
+<StructureSection load='5l4s' size='340' side='right'caption='[[5l4s]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5l4s]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L4S FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5l4s]] 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=5L4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L4S FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6KX:BETA-CYCLOCITRAL'>6KX</scene>, <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]] 1.41&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/(-)-isopiperitenone_reductase (-)-isopiperitenone reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.82 1.3.1.82] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6KX:BETA-CYCLOCITRAL'>6KX</scene>, <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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l4s OCA], [http://pdbe.org/5l4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l4s RCSB], [http://www.ebi.ac.uk/pdbsum/5l4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l4s 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=5l4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l4s OCA], [https://pdbe.org/5l4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l4s RCSB], [https://www.ebi.ac.uk/pdbsum/5l4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l4s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/IPIPR_MENPI IPIPR_MENPI]] Monoterpene synthase that catalyzes the specific reduction of the 1(2)-double bond of (-)-isopiperitenone to produce (+)-cis-isopulegone. Does not catalyze the reverse reaction. Unable to reduce (+)-pulegone, (+)-cis-isopulegone, (-)-menthone or the 1,2-double bond of (-)-carvone. Able to utilize NADH with 20% the efficiency of NADPH.
+[https://www.uniprot.org/uniprot/IPIPR_MENPI IPIPR_MENPI] Monoterpene synthase that catalyzes the specific reduction of the 1(2)-double bond of (-)-isopiperitenone to produce (+)-cis-isopulegone. Does not catalyze the reverse reaction. Unable to reduce (+)-pulegone, (+)-cis-isopulegone, (-)-menthone or the 1,2-double bond of (-)-carvone. Able to utilize NADH with 20% the efficiency of NADPH.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Karuppiah, V]]
+[[Category: Large Structures]]
-[[Category: Leys, D]]
+[[Category: Mentha x piperita]]
-[[Category: Scrutton, N S]]
+[[Category: Karuppiah V]]
-[[Category: Toogood, H S]]
+[[Category: Leys D]]
-[[Category: Beta-cyclocitral]]
+[[Category: Scrutton NS]]
-[[Category: Isopiperitenone]]
+[[Category: Toogood HS]]
-[[Category: Oxidoreductase]]
-[[Category: Rossmann fold]]

5l4s

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Current revision

Isopiperitenone reductase from Mentha piperita in complex with NADP and beta-Cyclocitral

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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