6ix4: Difference between revisions
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<StructureSection load='6ix4' size='340' side='right'caption='[[6ix4]], [[Resolution|resolution]] 1.51Å' scene=''> | <StructureSection load='6ix4' size='340' side='right'caption='[[6ix4]], [[Resolution|resolution]] 1.51Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ix4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IX4 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6ix4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_usamii Aspergillus usamii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IX4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6ix4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ix4 OCA], [https://pdbe.org/6ix4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ix4 RCSB], [https://www.ebi.ac.uk/pdbsum/6ix4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ix4 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/T2B4K5_ASPUS T2B4K5_ASPUS] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Only a few known epoxide hydrolases (EHs) displayed activity towards o-nitrostyrene oxide (4a), presumably owing to the large steric hindrance caused by o-nitro substituent. Therefore, excavating EHs with high activity and enantio- and/or regio-selectivity towards racemic (rac-) 4a is essential but challenging. Here, AuEH2 from Aspergillus usamii was expressed in E. coli BL21(DE3). E. coli/Aueh2, an E. coli transformant expressing AuEH2, possessed EH activities of 16.2-184 U/g wet cell towards rac-styrene oxide (1a) and its derivatives (2a-13a), and the largest enantiomeric ratio of 96 towards rac-4a. The regioselectivity coefficients, beta(R) and beta(S), of AuEH2 were determined to be 99.2% and 98.9%, suggesting that it regiopreferentially attacks the C(beta) in the oxirane rings of (R)- and (S)-4a. Then, the nearly perfect kinetic resolution of 20 mM rac-4a in pure water was carried out using 20 mg/mL wet cells of E. coli/Aueh2 at 25 degrees C for 50 min, retaining (S)-4a with over 99% ee(s) and 48.9% yield(s), while producing (R)-o-nitrophenyl-1,2-ethanediol (4b) with 95.3% ee(p) and 49.8% yield(p). To elucidate the molecular mechanism of AuEH2 with high enantiopreference for (R)-4a, its crystal structure was solved by X-ray diffraction and the molecular docking of AuEH2 with (R)- or (S)-4a was simulated. | |||
Nearly perfect kinetic resolution of racemic o-nitrostyrene oxide by AuEH2, a microsomal epoxide hydrolase from Aspergillus usamii, with high enantio- and regio-selectivity.,Hu D, Hu BC, Wen Z, Zhang D, Liu YY, Zang J, Wu MC Int J Biol Macromol. 2021 Feb 1;169:1-7. doi: 10.1016/j.ijbiomac.2020.12.074. , Epub 2020 Dec 13. PMID:33316339<ref>PMID:33316339</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ix4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aspergillus usamii]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hou XD]] | |||
[[Category: Hou | [[Category: Hu BC]] | ||
[[Category: Hu | [[Category: Hu D]] | ||
[[Category: Hu | [[Category: Rao YJ]] | ||
[[Category: Rao | [[Category: Wu L]] | ||
[[Category: Wu | [[Category: Wu MC]] | ||
[[Category: Wu | |||
Revision as of 13:19, 24 November 2022
Structure of an epoxide hydrolase from Aspergillus usamii E001 (AuEH2) at 1.51 Angstroms resolutionStructure of an epoxide hydrolase from Aspergillus usamii E001 (AuEH2) at 1.51 Angstroms resolution
Structural highlights
FunctionPublication Abstract from PubMedOnly a few known epoxide hydrolases (EHs) displayed activity towards o-nitrostyrene oxide (4a), presumably owing to the large steric hindrance caused by o-nitro substituent. Therefore, excavating EHs with high activity and enantio- and/or regio-selectivity towards racemic (rac-) 4a is essential but challenging. Here, AuEH2 from Aspergillus usamii was expressed in E. coli BL21(DE3). E. coli/Aueh2, an E. coli transformant expressing AuEH2, possessed EH activities of 16.2-184 U/g wet cell towards rac-styrene oxide (1a) and its derivatives (2a-13a), and the largest enantiomeric ratio of 96 towards rac-4a. The regioselectivity coefficients, beta(R) and beta(S), of AuEH2 were determined to be 99.2% and 98.9%, suggesting that it regiopreferentially attacks the C(beta) in the oxirane rings of (R)- and (S)-4a. Then, the nearly perfect kinetic resolution of 20 mM rac-4a in pure water was carried out using 20 mg/mL wet cells of E. coli/Aueh2 at 25 degrees C for 50 min, retaining (S)-4a with over 99% ee(s) and 48.9% yield(s), while producing (R)-o-nitrophenyl-1,2-ethanediol (4b) with 95.3% ee(p) and 49.8% yield(p). To elucidate the molecular mechanism of AuEH2 with high enantiopreference for (R)-4a, its crystal structure was solved by X-ray diffraction and the molecular docking of AuEH2 with (R)- or (S)-4a was simulated. Nearly perfect kinetic resolution of racemic o-nitrostyrene oxide by AuEH2, a microsomal epoxide hydrolase from Aspergillus usamii, with high enantio- and regio-selectivity.,Hu D, Hu BC, Wen Z, Zhang D, Liu YY, Zang J, Wu MC Int J Biol Macromol. 2021 Feb 1;169:1-7. doi: 10.1016/j.ijbiomac.2020.12.074. , Epub 2020 Dec 13. PMID:33316339[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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