5yw4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure-Guided Engineering of Reductase: Efficient Attenuating Substrate Inhibition in Asymmetric Catalysis== | |
| + | <StructureSection load='5yw4' size='340' side='right'caption='[[5yw4]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5yw4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Scheffersomyces_stipitis_CBS_6054 Scheffersomyces stipitis CBS 6054]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YW4 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]] 2.047Å</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=5yw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yw4 OCA], [https://pdbe.org/5yw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yw4 RCSB], [https://www.ebi.ac.uk/pdbsum/5yw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yw4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A3LWG4_PICST A3LWG4_PICST] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Substrate inhibition of enzymes is one of the main obstacles encountered frequently in industrial biocatalysis. Haloketone reductase SsCR was seriously inhibited by substrate 2,2',4'-trichloroacetophenone. In this study, two essential loops were found that have a relationship with substrate binding by conducting X-ray crystal structure analysis. Three key residues were selected from the tips of the loops and substituted with amino acids with lower hydrophobicity to weaken the hydrophobic interactions that bridge the two loops, resulting in a remarkable reduction of substrate inhibition. Among these variants, L211H showed a significant attenuation of substrate inhibition, with a Ki of 16 mM, which was 16 times that of the native enzyme. The kinetic parameter kcat/Km of L211H was 3.1 x 10(3) s(-1) mM(-1), showing the comparable catalytic efficiency to that of the wild-type enzyme (WT). At the substrate loading of 100 mM, the space time yield of variant L211H in asymmetric reduction of the haloketone was 3-fold higher than that of the WT. | ||
| - | + | Attenuated substrate inhibition of a haloketone reductase via structure-guided loop engineering.,Shang YP, Chen Q, Li AT, Quan S, Xu JH, Yu HL J Biotechnol. 2020 Jan 20;308:141-147. doi: 10.1016/j.jbiotec.2019.12.011. Epub, 2019 Dec 19. PMID:31866427<ref>PMID:31866427</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5yw4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Scheffersomyces stipitis CBS 6054]] | ||
| + | [[Category: Chen Q]] | ||
| + | [[Category: Li AT]] | ||
| + | [[Category: Shang YP]] | ||
| + | [[Category: Xu JH]] | ||
| + | [[Category: Yu HL]] | ||
Current revision
Structure-Guided Engineering of Reductase: Efficient Attenuating Substrate Inhibition in Asymmetric Catalysis
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