6ix4

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 6ix4 is a 2 chain structure with sequence from Aspergillus usamii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.511Å Ligands: , , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function T2B4K5_ASPUS 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Epoxide hydrolase 3D structures

spinqualitylabelsall models 6ix4, resolution 1.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image