7wnw: Difference between revisions
New page: '''Unreleased structure''' The entry 7wnw is ON HOLD Authors: Jun, Z., Rongchang, C., Shu-shan, G. Description: Crystal structure of Imine Reductase Mutant(M5) from Actinoalloteichus h... |
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==Crystal structure of Imine Reductase Mutant(M5) from Actinoalloteichus hymeniacidonis in complex with NADPH== | |||
<StructureSection load='7wnw' size='340' side='right'caption='[[7wnw]], [[Resolution|resolution]] 2.13Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7wnw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinoalloteichus_hymeniacidonis Actinoalloteichus hymeniacidonis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WNW 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]] 2.13Å</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=7wnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wnw OCA], [https://pdbe.org/7wnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wnw RCSB], [https://www.ebi.ac.uk/pdbsum/7wnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wnw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1D8BXU6_9PSEU A0A1D8BXU6_9PSEU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Although imine reductases (IREDs) are emerging as attractive reductive aminases (RedAms), their substrate scope is still narrow, and rational engineering is rare. Focusing on hydrogen bond reorganization and cavity expansion, a concise strategy combining rational cavity design, combinatorial active-site saturation test (CAST), and thermostability engineering was designed, that transformed the weakly active IR-G36 into a variant M5 with superior performance for the synthesis of (R)-3-benzylamino-1-Boc-piperidine, with a 4193-fold improvement in catalytic efficiency, a 16.2 improvement in Tm, and a significant increase in the e.e. value from 78% (R) to >99% (R). M5 exhibits broad substrate scope for the synthesis of diverse azacycloalkylamines, and the reaction was demonstrated on a hectogram-scale under industrially relevant conditions. Our study provides a compelling example of the preparation of versatile and efficient IREDs, with exciting opportunities in medicinal and process chemistry as well as synthetic biology. | |||
Tuning an Imine Reductase for the Asymmetric Synthesis of Azacycloalkylamines by Concise Structure-Guided Engineering.,Zhang J, Liao D, Chen R, Zhu F, Ma Y, Gao L, Qu G, Cui C, Sun Z, Lei X, Gao S Angew Chem Int Ed Engl. 2022 Mar 23. doi: 10.1002/anie.202201908. PMID:35322515<ref>PMID:35322515</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7wnw" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Actinoalloteichus hymeniacidonis]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen R]] | |||
[[Category: Gao S]] | |||
[[Category: Zhand J]] | |||