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7emg
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7emg is ON HOLD Authors: Zheng, Y.C., Wang, T., Bai, Y.P. Description: Carbonyl Reductase Variant 4 (R123C/L209P/F183Y/V61K) from Serratia marcesce...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Carbonyl Reductase Variant 4 (R123C/L209P/F183Y/V61K) from Serratia marcescens complexed with NADP+== | |
| + | <StructureSection load='7emg' size='340' side='right'caption='[[7emg]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7emg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EMG 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]] 2.449Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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=7emg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7emg OCA], [https://pdbe.org/7emg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7emg RCSB], [https://www.ebi.ac.uk/pdbsum/7emg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7emg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0G8B235_SERMA A0A0G8B235_SERMA] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.[ARBA:ARBA00002607][RuleBase:RU366074] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A carbonyl reductase variant, SmCRM5, from Serratia marcescens was obtained through structure-guided directed evolution. The variant showed improved specific activity (U mg(-1)) towards most of the 16 tested substrates and gave high stereoselectivities of up to 99% in the asymmetric synthesis of 13 gamma-/delta-lactones. In particular, SmCRM5 showed a 13.8-fold higher specific activity towards the model substrate, i.e., 5-oxodecanoic acid, and gave (R)-delta-decalactone in 99% ee with a space-time yield (STY) of 301 g L(-1) d(-1). The preparative synthesis of six delta-lactones in high yields and with high enantiopurities showed the feasibility of the biocatalytic synthesis of these high-value-added chemicals, providing a cost-effective and green alternative to noble-metal catalysis. | ||
| - | + | Stereoselective synthesis of chiral delta-lactones via an engineered carbonyl reductase.,Wang T, Zhang XY, Zheng YC, Bai YP Chem Commun (Camb). 2021 Sep 24. doi: 10.1039/d1cc04542c. PMID:34559867<ref>PMID:34559867</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Bai | + | <div class="pdbe-citations 7emg" style="background-color:#fffaf0;"></div> |
| - | [[Category: Wang | + | == References == |
| - | [[Category: Zheng | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Serratia marcescens]] | ||
| + | [[Category: Bai YP]] | ||
| + | [[Category: Wang T]] | ||
| + | [[Category: Zheng YC]] | ||
Current revision
Carbonyl Reductase Variant 4 (R123C/L209P/F183Y/V61K) from Serratia marcescens complexed with NADP+
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