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首页> 外文期刊>Synlett >Whole-cell mediated Baeyer-Villiger oxidation of functionalized bicyclo[3.3.0]ketones by recombinant E-coli
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Whole-cell mediated Baeyer-Villiger oxidation of functionalized bicyclo[3.3.0]ketones by recombinant E-coli

机译:重组大肠杆菌对全细胞介导的功能化双环[3.3.0]酮的Baeyer-Villiger氧化

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摘要

Recombinant whole cells of Escherichia coli overexpressing Acinetobacter sp. NCIMB 9871 cyclohexatione monooxygenase (F.C. 1.14,13.22) have been utilized for the Baeyer-Villiger oxidation of functionalized bicyclo [3.3.0] ketones. Prochiral substrates were designed to probe the impact of polarity and spatial configuration of the functional groups on conversion and enantio-selectivity. The data give additional insight into the steric requirements of the active site of the enzyme for high optical purity. The synthetic utility of the engineered E. coli strain is demonstrated and contributions to the non-natural substrate profile available so far are provided. [References: 49]
机译:过量表达不动杆菌属的大肠杆菌重组全细胞。 NCIMB 9871环己酮单加氧酶(F.C. 1.14,13.22)已用于功能化的双环[3.3.0]酮的Baeyer-Villiger氧化。前手性底物被设计来探测官能团的极性和空间构型对转化率和对映选择性的影响。数据进一步了解了酶的活性位点对于高光学纯度的空间要求。证明了工程大肠杆菌菌株的合成效用,并提供了迄今为止可获得的对非天然底物谱的贡献。 [参考:49]

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