7emg: Difference between revisions
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==Carbonyl Reductase Variant 4 (R123C/L209P/F183Y/V61K) from Serratia marcescens complexed with NADP+== | ==Carbonyl Reductase Variant 4 (R123C/L209P/F183Y/V61K) from Serratia marcescens complexed with NADP+== | ||
<StructureSection load='7emg' size='340' side='right'caption='[[7emg]]' scene=''> | <StructureSection load='7emg' size='340' side='right'caption='[[7emg]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>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> | <table><tr><td colspan='2'>[[7emg]] is a 2 chain structure. 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='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> | </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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </span></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> | </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> | |||
</div> | |||
<div class="pdbe-citations 7emg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bai | [[Category: Bai, Y P]] | ||
[[Category: Wang T]] | [[Category: Wang, T]] | ||
[[Category: Zheng | [[Category: Zheng, Y C]] | ||
[[Category: Carbonyl reductase]] | |||
[[Category: Nadp+ complex]] | |||
[[Category: Oxidoreductase]] | |||
Revision as of 10:54, 16 February 2022
Carbonyl Reductase Variant 4 (R123C/L209P/F183Y/V61K) from Serratia marcescens complexed with NADP+
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