ArticleChemical communications (Cambridge, England)2018
A coupled chlorinase-fluorinase system with a high efficiency of trans-halogenation and a shared substrate tolerance.
Article in Chemical communications (Cambridge, England), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- A Nonconventional Archaeal Fluorinase Identified by In Silico Mining for Enhanced Fluorine Biocatalysis.ACS catalysis · 2022Article
- Oligomerization engineering of the fluorinase enzyme leads to an active trimer that supports synthesis of fluorometabolites in vitro.Microbial biotechnology · 2022Article
- Enzymatic synthesis of fluorinated compounds.Applied microbiology and biotechnology · 2021Review
- Whole-cell catalysis by surface display of fluorinase on Escherichia coli using N-terminal domain of ice nucleation protein.Microbial cell factories · 2021Article
- Halogenating Enzymes for Active Agent Synthesis: First Steps Are Done and Many Have to Follow.Molecules (Basel, Switzerland) · 2019Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Enzymatic trans-halogenation enables radiolabeling under mild and aqueous conditions, but rapid reactions are desired. We developed a coupled chlorinase-fluorinase system for rapid trans-halogenation. Notably, the chlorinase shares a substrate tolerance with the fluorinase, enabling these two enzymes to cooperatively produce 5'-fluorodeoxy-2-ethynyladenosine (5'-FDEA) in up to 91.6% yield in 1 h.
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Registered trials
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