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Updated: Apr 11, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Characterization of Two Multisite Halogenases and Exploration of Substrate Promiscuity
Shu-Ya Peng1,2, Jun-Bin He2, Qiu-Yue Nie2
1State Key Laboratory of Bioreactor Engineering, School of Biotechnology, East China University of Science and Technology, Shanghai 200237, China.
None:
Halogenases offer valuable opportunities in synthetic chemistry and biocatalysis. Here, we identify two novel flavin-dependent phenolic multisite halogenases, FasVamrb99 and IdmB26, from distinct biosynthetic pathways that exhibit divergent polyhalogenation of naphthacemycin B2. Substrate screening revealed that both enzymes display robust polyhalogenation activity, enabling halogenation not only at ortho positions adjacent to nonphenolic hydroxyl groups but also across a range of drug molecules. These features highlight their versatility and potential as biocatalysts for synthetic applications.
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