125803-26-1Relevant articles and documents
Biocatalytic Potential of the Epoxide Hydrolase from Agrobacterium radiobacter AD1 and a Mutant with Enhanced Enantioselectivity
Lutje Spelberg, Jeffrey H.,Rink, Rick,Archelas, Alain,Furstoss, Roland,Janssen, Dick B.
, p. 980 - 985 (2002)
Optically pure epoxides are useful synthons for a variety of biologically active compounds. The epoxide hydrolase obtained from Agrobacterium radiobacter AD1 hydrolyses racemic aryl epoxides with moderate and aliphatic epoxides with low enantioselectivity
Self-assembled nanoreactors as highly active catalysts in the hydrolytic kinetic resolution (HKR) of epoxides in water
Rossbach, Benjamin M.,Leopold, Kerstin,Weberskirch, Ralf
, p. 1309 - 1312 (2006)
CoIII(salen) complexes have been immobilized on amphiphilic block copolymers, which self-assemble in water to give micellar aggregates with a hydrophobic Co(salen) core and a water-soluble shell (see picture). These aggregates were used to catalyze the hydrolytic kinetic resolution (HKR) of racemic aromatic epoxides over four consecutive cycles and gave the epoxides in up to 99 % ee. H2salen = N,N′-bis(salicylidene)ethylenediamine. (Chemical Equation Presented).
Highly selective anti-Prelog synthesis of optically active aryl alcohols by recombinant Escherichia coli expressing stereospecific alcohol dehydrogenase
Li, Ming,Nie, Yao,Mu, Xiao Qing,Zhang, Rongzhen,Xu, Yan
, p. 429 - 433 (2016)
Biocatalytic asymmetric synthesis has been widely used for preparation of optically active chiral alcohols as the important intermediates and precursors of active pharmaceutical ingredients. However, the available whole-cell system involving anti-Prelog specific alcohol dehydrogenase is yet limited. A recombinant Escherichia coli system expressing anti-Prelog stereospecific alcohol dehydrogenase from Candida parapsilosis was established as a whole-cell system for catalyzing asymmetric reduction of aryl ketones to anti-Prelog configured alcohols. Using 2-hydroxyacetophenone as the substrate, reaction factors including pH, cell status, and substrate concentration had obvious impacts on the outcome of whole-cell biocatalysis, and xylose was found to be an available auxiliary substrate for intracellular cofactor regeneration, by which (S)-1-phenyl-1,2-ethanediol was achieved with an optical purity of 97%e.e. and yield of 89% under the substrate concentration of 5?g/L. Additionally, the feasibility of the recombinant cells toward different aryl ketones was investigated, and most of the corresponding chiral alcohol products were obtained with an optical purity over 95%e.e. Therefore, the whole-cell system involving recombinant stereospecific alcohol dehydrogenase was constructed as an efficient biocatalyst for highly enantioselective anti-Prelog synthesis of optically active aryl alcohols and would be promising in the pharmaceutical industry.
Manipulating regioselectivity of an epoxide hydrolase for single enzymatic synthesis of (: R)-1,2-diols from racemic epoxides
Hu, Die,Zong, Xun-Cheng,Xue, Feng,Li, Chuang,Hu, Bo-Chun,Wu, Min-Chen
, p. 2799 - 2802 (2020)
Both the activity and regioselectivity of Phaseolus vulgaris epoxide hydrolase were remarkably improved via reshaping two substrate tunnels based on rational design. The elegant one-step enantioconvergent hydrolysis of seven rac-epoxides was achieved by single mutants, allowing green and efficient access to valuable (R)-1,2 diols with high eep (90.1-98.3%) and yields.
Microbiological transformations. Part 45: A green chemistry preparative scale synthesis of enantiopure building blocks of Eliprodil: Elaboration of a high substrate concentration epoxide hydrolase-catalyzed hydrolytic kinetic resolution process
Manoj,Archelas,Baratti,Furstoss
, p. 695 - 701 (2001)
The enantioselective hydrolysis of racemic para-chlorostyrene oxide 2 following a typical 'green chemistry' procedure based on the use of two different Epoxide Hydrolases is described. This allows the preparation of both enantiomers of 2 in very high enantiomeric purity. Furthermore, using a 'one-pot' sequential bi-enzymatic strategy enabling to overcome the 50% yield limitation intrinsic to any resolution process, rac-2 could be transformed into nearly enantiopure (R)-3 with an overall yield as high as 93%. The methodology developed was based on the use of a biphasic reactor at high substrate concentration, which is highly desirable for any potential industrial process. The obtained chirons are valuable building blocks for the synthesis of various biologically active targets, like (R)-Eliprodil.
Asymmetric dihydroxylation of aryl olefins by sequential enantioselective epoxidation and regioselective hydrolysis with tandem biocatalysts
Xu, Yi,Jia, Xin,Panke, Sven,Li, Zhi
, p. 1481 - 1483 (2009)
Chiral aryl vicinal diols were obtained in high ee and yield by asymmetric dihydroxylation of aryl olefins with tandem biocatalysts: one contains an enantioselective styrene monooxygenase, and the other contains a regioselective epoxide hydrolase.
Highly regio- and enantio-selective hydrolysis of two racemic epoxides by GmEH3, a novel epoxide hydrolase from Glycine max
Zhang, Chen,Li, Chuang,Zhu, Xiu-xiu,Liu, You-yi,Zhao, Jun,Wu, Min-chen
, p. 2795 - 2803 (2020/09/01)
A novel epoxide hydrolase from Glycine max, designated GmEH3, was excavated based on the computer-aided analysis. Then, gmeh3, a GmEH3-encoding gene, was cloned and successfully expressed in E. coli Rosetta(DE3). Among the ten investigated rac-epoxides, GmEH3 possessed the highest and best complementary regioselectivities (regioselectivity coefficients, αS = 93.7% and βR = 97.2%) in the asymmetric hydrolysis of rac-m-chlorostyrene oxide (5a), and the highest enantioselectivity (enantiomeric ratio, E = 55.6) towards rac-phenyl glycidyl ether (7a). The catalytic efficiency (kcatS/KmS = 2.50 mM?1 s?1) of purified GmEH3 for (S)-5a was slightly higher than that (kcatR/KmR = 1.52 mM?1 s?1) for (R)-5a, whereas the kcat/Km (5.16 mM?1 s?1) for (S)-7a was much higher than that (0.09 mM?1 s?1) for (R)-7a. Using 200 mg/mL wet cells of E. coli/gmeh3 as the biocatalyst, the scale-up enantioconvergent hydrolysis of 150 mM rac-5a at 25 °C for 1.5 h afforded (R)-5b with 90.2% eep and 95.4% yieldp, while the kinetic resolution of 500 mM rac-7a for 2.5 h retained (R)-7a with over 99% ees and 43.2% yields. Furthermore, the sources of high regiocomplementarity of GmEH3 for (S)- and (R)-5a as well as high enantioselectivity towards rac-7a were analyzed via molecular docking (MD) simulation.
Chiral Ion-Pair Organocatalyst-Promoted Efficient Enantio-selective Reduction of α-Hydroxy Ketones
Zhang, Yiliang,He, Li,Shi, Lei
, p. 1926 - 1931 (2018/03/27)
The enantioselective reduction of α-hydroxy ketones with catecholborane has been developed employing 5 mol% of an 1,1′-bi-2-naphthol (BINOL)-derived ion-pair organocatalyst. This methodology provides a straightforward access to the corresponding aromatic 1,2-diols in high yields (up to 90%) with excellent enantioselectivities (up to 97%). Furthermore, the α-amino ketones also could be reduced with moderate ee values under mild reaction condition. (Figure presented.).
