View source for 7xg5


==Crystal structure of an (R)-selective omega-transaminase mutant from Aspergillus terreus with PLP==
<StructureSection load='7xg5' size='340' side='right'caption='[[7xg5]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7xg5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_terreus_NIH2624 Aspergillus terreus NIH2624]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XG5 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]] 1.76&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=7xg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xg5 OCA], [https://pdbe.org/7xg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xg5 RCSB], [https://www.ebi.ac.uk/pdbsum/7xg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xg5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q0C8G1_ASPTN Q0C8G1_ASPTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fast screening of enzyme variants is crucial for tailoring biocatalysts for the asymmetric synthesis of non-natural chiral chemicals, such as amines. However, most existing screening methods either are limited by the throughput or require specialized equipment. Herein, we report a simple, high-throughput, low-equipment dependent, and generally applicable growth selection system for engineering amine-forming or converting enzymes and apply it to improve biocatalysts belonging to three different enzyme classes. This results in (i) an amine transaminase variant with 110-fold increased specific activity for the asymmetric synthesis of the chiral amine intermediate of Linagliptin; (ii) a 270-fold improved monoamine oxidase to prepare the chiral amine intermediate of Cinacalcet by deracemization; and (iii) an ammonia lyase variant with a 26-fold increased activity in the asymmetric synthesis of a non-natural amino acid. Our growth selection system is adaptable to different enzyme classes, varying levels of enzyme activities, and thus a flexible tool for various stages of an engineering campaign.

A growth selection system for the directed evolution of amine-forming or converting enzymes.,Wu S, Xiang C, Zhou Y, Khan MSH, Liu W, Feiler CG, Wei R, Weber G, Hohne M, Bornscheuer UT Nat Commun. 2022 Dec 3;13(1):7458. doi: 10.1038/s41467-022-35228-y. PMID:36460668<ref>PMID:36460668</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7xg5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus terreus NIH2624]]
[[Category: Large Structures]]
[[Category: Bornscheuer UT]]
[[Category: Liu WD]]
[[Category: Weber G]]
[[Category: Wei R]]
[[Category: Wu SK]]
[[Category: Xiang C]]