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==The Crystal Structure of the S154Y Mutant Carbonyl Reductase from Leifsonia xyli Explains Enhanced Activity for 3,5-Bis(trifluoromethyl)acetophenone Reduction==
<StructureSection load='6xnb' size='340' side='right'caption='[[6xnb]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xnb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leifsonia_xyli Leifsonia xyli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XNB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XNB 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]] 1.16&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6xnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xnb OCA], [https://pdbe.org/6xnb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xnb RCSB], [https://www.ebi.ac.uk/pdbsum/6xnb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xnb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/T2FLN4_9MICO T2FLN4_9MICO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Carbonyl reductase from Leifsonia xyli (LXCAR, UniProtKB - T2FLN4) can stereoselectively catalyze the reduction of 3,5-bis(trifluoromethyl)acetophenone (BTAP) to its corresponding alcohol, (R)-[3,5-bis(trifluoromethyl)phenyl]ethanol ((R)-BTPE), which is a valuable chiral intermediate for the synthesis of antiemetic drugs, Aprepitant and Fosaprepitant. Moreover, this protein was found to have a broad spectrum of substrate specificity and can asymmetrically catalyze the reduction of a variety of ketones and keto esters. Even though molecular modelling of this protein was done by Wang et al. (2014), a crystal structure has not yet obtained. In this study, a single mutant, S154Y, which was shown to have higher catalytic activity toward BTAP than that of the wild type, was overexpressed in Escherichia coli BL21 (DE3), purified, and crystallized. The crystal structure of LXCAR-S154Y explains how the mutant enzyme can work with BTAP more efficiently than wild type carbonyl reductase. Furthermore, the structure explains why LXCAR-S154Y can use either NADH or NADPH efficiently as a cofactor, as well as elucidates a proton relay system present in the enzyme.

The crystal structure of the S154Y mutant carbonyl reductase from Leifsonia xyli explains enhanced activity for 3,5-bis(trifluoromethyl)acetophenone reduction.,Li J, Dinh T, Phillips R Arch Biochem Biophys. 2022 Mar 2;720:109158. doi: 10.1016/j.abb.2022.109158. PMID:35247363<ref>PMID:35247363</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6xnb" style="background-color:#fffaf0;"></div>

==See Also==
*[[Carbonyl reductase 3D structures|Carbonyl reductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Leifsonia xyli]]
[[Category: Dinh T]]
[[Category: Phillips R]]