Title
A coupled chlorinase-fluorinase system with high efficiency of trans-halogenation and a shared substrate tolerance
Conference Dates
September 15-19, 2019
Abstract
Enzymatic trans-halogenation enables radiolabeling under mild and aqueous conditions, but rapid reactions are desired. We discovered two new S-adenosyl-L-methionine (SAM)-dependent chlorinases from soil bacteria and developed a coupled chlorinase-fluorinase system for highly improved trans-halogenation reactions. The chlorinase was for the first time demonstrated to tolerate the modification at the C-2 position of the adenine ring and act cooperatively with the fluorinase to accelerate the trans-halogenation of 5’-chlorodeoxy-2-ethynyladenosine (5’-ClDEA) to 5’-fluorodeoxy-2-ethynyladenosine (5’-FDEA). The acetylene group will enable the linkage with an azide tethered peptide via a “click” reaction. The coupled chlorinase-fluorinase system offers the prospect of developing rapid radiolabeling protocols under mild and aqueous conditions.
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Recommended Citation
Huihua Sun, Huimin Zhao, and Ee Lui Ang, "A coupled chlorinase-fluorinase system with high efficiency of trans-halogenation and a shared substrate tolerance" in "Enzyme Engineering XXV", Huimin Zhao, University of Illinois at Urbana-Champaign, USA John Wong, Pfizer, USA Eds, ECI Symposium Series, (2019). https://dc.engconfintl.org/enzyme_xxv/66