Chemoenzymatic enantioconvergent hydrolysis of p-nitrostyrene oxide into (R)-p-nitrophenyl glycol by a newly cloned epoxide hydrolase VrEH2 from Vigna radiata

2015 ◽  
Vol 58 ◽  
pp. 16-20 ◽  
Author(s):  
Yan-Wen Wu ◽  
Xu-Dong Kong ◽  
Qing-Qing Zhu ◽  
Li-Qiang Fan ◽  
Jian-He Xu
Keyword(s):  
Vigna Radiata ◽  
Epoxide Hydrolase ◽  
Enantioconvergent Hydrolysis ◽  
Hydrolysis Of

scholarly journals Substantially improving the enantioconvergence of PvEH1, a Phaseolus vulgaris epoxide hydrolase, towards m-chlorostyrene oxide by laboratory evolution

2019 ◽  
Vol 18 (1) ◽  
Author(s):  
Xun-Cheng Zong ◽  
Chuang Li ◽  
Yao-Hui Xu ◽  
Die Hu ◽  
Bo-Chun Hu ◽  
...  
Keyword(s):  
Phaseolus Vulgaris ◽  
Epoxide Hydrolase ◽  
Substrate Binding ◽  
Binding Pocket ◽  
Saturation Mutagenesis ◽  
Substrate Binding Pocket ◽  
Laboratory Evolution ◽  
E Coli ◽  
Enantioconvergent Hydrolysis ◽  
Hydrolysis Of

Abstract Background Epoxide hydrolase can regioselectively catalyze the oxirane ring-opening hydrolysis of rac-epoxides producing the corresponding chiral diols. In our laboratory, a gene named pveh1 encoding an EH from Phaseolus vulgaris was cloned. Although the directed modification of PvEH1 was carried out, the mutant PvEH1Y3 showed a limited degree of enantioconvergence towards racemic (rac-) m-chlorostyrene oxide (mCSO). Results PvEH1 and PvEH1Y3 were combinatively subjected to laboratory evolution to further enhance the enantioconvergence of PvEH1Y3 towards rac-mCSO. Firstly, the substrate-binding pocket of PvEH1 was identified using a CAVER 3.0 software, and divided into three zones. After all residues in zones 1 and 3 were subjected to leucine scanning, two E. coli transformants, E. coli/pveh1Y149L and /pveh1P184L, were selected, by which rac-mCSO was transformed into (R)-m-chlorophenyl-1,2-ethanediol (mCPED) having 55.1% and 27.2% eep. Secondly, two saturation mutagenesis libraries, E. coli/pveh1Y149X and /pveh1P184X (X: any one of 20 residues) were created at sites Y149 and P184 of PvEH1. Among all transformants, both E. coli/pveh1Y149L (65.8% αS and 55.1% eep) and /pveh1P184W (66.6% αS and 59.8% eep) possessed the highest enantioconvergences. Finally, the combinatorial mutagenesis was conducted by replacements of both Y149L and P184W in PvEH1Y3, constructing E. coli/pveh1Y3Z2, whose αS reached 97.5%, higher than that (75.3%) of E. coli/pveh1Y3. In addition, the enantioconvergent hydrolysis of 20 mM rac-mCSO was performed by E. coli/pveh1Y3Z2, giving (R)-mCPED with 95.2% eep and 97.2% yield. Conclusions In summary, the enantioconvergence of PvEH1Y3Z2 was successfully improved by laboratory evolution, which was based on the study of substrate-binding pocket by leucine scanning. Our present work introduced an effective strategy for the directed modification of enantioconvergence of PvEH1.

Previously published / Prédémment paruAsymmetric total synthesis of (+)-exo-brevicomin based on enantioconvergent biocatalytic hydrolysis of an alkene-functionalized 2,3-disubstituted epoxide

2002 ◽  
Vol 80 (6) ◽  
Author(s):  
Sandra F Mayer ◽  
Harald Mang ◽  
Andreas Steinreiber ◽  
Robert Saf ◽  
Kurt Faber
Keyword(s):  
Total Synthesis ◽  
Asymmetric Synthesis ◽  
Bark Beetle ◽  
Epoxide Hydrolase ◽  
Side Chains ◽  
Beetle Species ◽  
Epoxide Hydrolases ◽  
Pheromone System ◽  
Enantioconvergent Hydrolysis ◽  
Hydrolysis Of

A short total asymmetric synthesis of (+)-exo- and (–)-endo-brevicomin ((+)-exo-3 and (–)-endo-3), which are components of the attracting pheromone system of several bark-beetle species belonging to the genera Dendroctonus and Dryocoetes, was accomplished via a chemoenzymatic protocol. The key step consisted of biocatalytic hydrolysis by bacterial epoxide hydrolases of cis-configured 2,3-disubstituted oxiranes bearing olefinic side chains. This reaction proceeded in an enantioconvergent fashion, by affording a single enantiomeric vic-diol from the rac-epoxide in up to 92% ee and 83% isolated yield.Key words: bacterial epoxide hydrolase, 2,3-disubstituted oxirane, enantioconvergent hydrolysis, (+)-exo-brevicomin, (–)-endo-brevicomin.

Asymmetric total synthesis of (+)-exo-brevicomin based on enantioconvergent biocatalytic hydrolysis of an alkene-functionalized 2,3-disubstituted epoxide

2002 ◽  
Vol 80 (4) ◽  
pp. 362-369 ◽  
Author(s):  
Sandra F Mayer ◽  
Harald Mang ◽  
Andreas Steinreiber ◽  
Robert Saf ◽  
Kurt Faber
Keyword(s):  
Total Synthesis ◽  
Asymmetric Synthesis ◽  
Bark Beetle ◽  
Epoxide Hydrolase ◽  
Beetle Species ◽  
Asymmetric Total Synthesis ◽  
Epoxide Hydrolases ◽  
Pheromone System ◽  
Enantioconvergent Hydrolysis ◽  
Hydrolysis Of

A short total asymmetric synthesis of (+)-exo- and (–)-endo-brevicomin ((+)-exo-3 and (–)-endo-3), which are components of the attracting pheromone system of several bark-beetle species belonging to the genera Dendroctonus and Dryocoetes, was accomplished via a chemoenzymatic protocol. The key step consisted of biocatalytic hydrolysis by bacterial epoxide hydrolases of cis-configured 2,3-disubstituted oxiranes bearing olefinic side chains. This reaction proceeded in an enantioconvergent fashion, by affording a single enantiomeric vic-diol from the rac-epoxide in up to 92% ee and 83% isolated yield.Key words: bacterial epoxide hydrolase, 2,3-disubstituted oxirane, enantioconvergent hydrolysis, (+)-exo-brevicomin, (–)-endo-brevicomin.

scholarly journals Conformational diversity and enantioconvergence in potato epoxide hydrolase 1

2016 ◽  
Vol 14 (24) ◽  
pp. 5639-5651 ◽  
Author(s):  
P. Bauer ◽  
Å. Janfalk Carlsson ◽  
B. A. Amrein ◽  
D. Dobritzsch ◽  
M. Widersten ◽  
...  
Keyword(s):  
Epoxide Hydrolase ◽  
Styrene Oxide ◽  
Computational Studies ◽  
Conformational Diversity ◽  
Enantioconvergent Hydrolysis ◽  
Hydrolysis Of

Computational studies highlight the importance of conformational diversity in the enantioconvergent hydrolysis of styrene oxide by potato epoxide hydrolase 1.

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