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- W2269862912 abstract "Abstract A novel ( R )‐imine reductase ( Pl RIR) from Paenibacillus lactis was heterologously overexpressed in Escherichia coli , purified and characterized. The purified Pl RIR exhibited relatively high catalytic efficiency ( k cat / K m =1.58 s −1 m m −1 ) towards 2,3,3‐trimethylindolenine. A panel of 3 H ‐indoles and 3 H ‐indole iodides were reduced by Pl RIR to yield the corresponding products with good‐to‐excellent enantioselectivity (66–98 % ee ). In addition, Pl RIR also possesses good activities toward other types of imines such as pyrroline, tetrahydropyridine, and dihydroisoquinoline, indicating a reasonably broad substrate acceptance. In a 100 mg scale preparative reaction, 100 m m 2,3,3‐trimethylindolenine was converted efficiently to afford ( R )‐2,3,3‐trimethylindoline with 96 % ee and 81 % yield." @default.
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- W2269862912 date "2016-01-26" @default.
- W2269862912 modified "2023-10-17" @default.
- W2269862912 title "A Novel (<i>R</i>)-Imine Reductase from<i>Paenibacillus lactis</i>for Asymmetric Reduction of 3 <i>H</i>-Indoles" @default.
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- W2269862912 doi "https://doi.org/10.1002/cctc.201501170" @default.
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