氢胺化
合理设计
区域选择性
化学
烷基
生物催化
裂解酶
组合化学
芳基
催化作用
氨
酶
生物化学
有机化学
纳米技术
材料科学
反应机理
作者
Syed T. Ahmed,Fabio Parmeggiani,Nicholas J. Weise,Sabine L. Flitsch,Nicholas J. Turner
出处
期刊:ACS Catalysis
[American Chemical Society]
日期:2018-03-07
卷期号:8 (4): 3129-3132
被引量:46
标识
DOI:10.1021/acscatal.8b00496
摘要
Engineered variants of phenylalanine ammonia lyase from Planctomyces brasiliensis were developed through rational design efforts focusing on the aryl binding pocket of the active site, guided by structural and phylogenetic inference. Inherent problems traditionally associated with the biocatalytic hydroamination of acrylic acids, such as low conversion and poor regioselectivity with alkyl and methoxy derivatives, could be overcome. The PbPAL variants described here represent a valuable addition to the biocatalytic toolbox, allowing previously inaccessible amino acid building blocks to be obtained regio- and enantioselectively on preparative scale.
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