Structural basis for selectivity in flavin-dependent monooxygenase-catalyzed oxidative dearomatization.

ABSTRACT: Biocatalytic reactions embody many features of ideal chemical transformations, including the potential for impeccable selectivity, high catalytic efficiency, mild reaction conditions and the use of environmentally benign reagents. These advantages have created a demand for biocatalysts that expand the portfolio of complexity-generating reactions available to synthetic chemists. However, the tradeoff that often exists between the substrate scope of a biocatalyst and its selectivity limits the application of enzymes in synthesis. We recently demonstrated that a flavin-dependent monooxygenase, TropB, maintains high levels of site- and stereoselectivity across a range of structurally diverse substrates. Herein, we disclose the structural basis for substrate binding in TropB, which performs a s

SUBMITTER: Benitez AR 

PROVIDER: S-EPMC6658140 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature