A coupled chlorinase-fluorinase system with high efficiency of trans-halogenation and a shared substrate tolerance
September 15-19, 2019
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.
Please click Additional Files below to see the full abstract.
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