89616-40-0Relevant articles and documents
Diastereoselective Alkene Hydroesterification Enabling the Synthesis of Chiral Fused Bicyclic Lactones
Shi, Zhanglin,Shen, Chaoren,Dong, Kaiwu
supporting information, p. 18039 - 18042 (2021/11/16)
Palladium-catalysed diastereoselective hydroesterification of alkenes assisted by the coordinative hydroxyl group in the substrate afforded a variety of chiral γ-butyrolactones bearing two stereocenters. Employing the carbonylation-lactonization products as the key intermediates, the route from the alkenes with single chiral center to chiral THF-fused bicyclic γ-lactones containing three stereocenters was developed.
Stereoselective total synthesis of (?)-galantinic acid and 1-deoxy-5-hydroxysphingolipids via prins cyclization
Rahman, Md. Ataur,Haque, Ashanul,Yadav, Jhillu Singh
, (2020/07/03)
The stereoselective total synthesis of (?)-galantinic acid 1 and 1-deoxy-5-hydroxysphingolipids 4 is described via Prins cyclization protocol followed by reductive ring opening sequence of substituted pyrenol derivative 6. The target molecules were synthesized using a common synthetic intermediate epoxide 5. Besides, we also proposed synthetic pathways to achieve other structural analogues using common intermediates.
Improving the activity and enantioselectivity of PvEH1, a Phaseolus vulgaris epoxide hydrolase, for o-methylphenyl glycidyl ether by multiple site-directed mutagenesis on the basis of rational design
Li, Chuang,Kan, Ting-Ting,Hu, Die,Wang, Ting-Ting,Su, Yong-Jun,Zhang, Chen,Cheng, Jian-Qing,Wu, Min-Chen
, (2019/08/01)
Substrate spectrum assay exhibited that PvEH1, which is an epoxide hydrolase from P. vulgaris, had the highest specific activity and enantiomeric ratio (E) for racemic o-methylphenyl glycidyl ether (rac-1) among tested aryl glycidyl ethers (1–5). To produce (R)-1 via kinetic resolution of rac-1 efficiently, the catalytic properties of PvEH1 were further improved on the basis of rational design. Firstly, the seven single-site variants of PvEH1-encoding gene (pveh1) were PCR-amplified as designed, and expressed in E. coli BL21(DE3). Among all expressed single-site mutants, PvEH1L105I and PvEH1V106I had the highest specific activities of 17.6 and 16.4 U/mg protein, respectively, while PvEH1L196D had an enhanced E value of 9.2. Secondly, to combine their respective merits, one triple-site variant, pveh1L105I/V106I/L196D, was also amplified, and expressed. The specific activity, E value, and catalytic efficiency of PvEH1L105I/V106I/L196D were 23.1 U/mg, 10.9, and 6.65 mM?1 s?1, respectively, which were 2.0-, 1.8- and 2.4-fold higher than those of wild-type PvEH1. The source of PvEH1L105I/V106I/L196D with enhanced E value for rac-1 was preliminarily analyzed by molecular docking simulation. Finally, the scale-up kinetic resolution of 100 mM rac-1 was conducted using 5 mg wet cells/mL E. coli/pveh1L105I/V106I/L196D at 25 °C for 1.5 h, producing (R)-1 with 95.0% ees, 32.1% yield and 3.52 g/L/h space-time yield.
