5ldg: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5ldg is ~~ON HOLD~~

==Isopiperitenone reductase from Mentha piperita in complex with Isopiperitenone and NADP==

== Structural highlights ==

<table><tr><td colspan='2'>[[5ldg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LDG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LDG FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IT9:(-)-ISOPIPERITENONE'>IT9</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></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='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=5ldg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ldg OCA], [http://pdbe.org/5ldg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ldg RCSB], [http://www.ebi.ac.uk/pdbsum/5ldg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ldg 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.

== 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.

~~Authors~~:

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Karuppiah, V]]

[[Category: Leys, D]]

[[Category: Scrutton, N S]]

[[Category: Toogood, H S]]

[[Category: Isopiperitenone]]

[[Category: Isopulegone]]

[[Category: Oxidoreductase]]

[[Category: Rossmann fold]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5ldg is ON HOLD
+==Isopiperitenone reductase from Mentha piperita in complex with Isopiperitenone and NADP==
+<StructureSection load='5ldg' size='340' side='right' caption='[[5ldg]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ldg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LDG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LDG FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IT9:(-)-ISOPIPERITENONE'>IT9</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></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='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=5ldg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ldg OCA], [http://pdbe.org/5ldg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ldg RCSB], [http://www.ebi.ac.uk/pdbsum/5ldg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ldg 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.
+<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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5ldg" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Karuppiah, V]]
+[[Category: Leys, D]]
+[[Category: Scrutton, N S]]
+[[Category: Toogood, H S]]
+[[Category: Isopiperitenone]]
+[[Category: Isopulegone]]
+[[Category: Oxidoreductase]]
+[[Category: Rossmann fold]]