TY - JOUR
T1 - Unusual substrate and halide versatility of phenolic halogenase PltM
AU - Mori, Shogo
AU - Pang, Allan H.
AU - Thamban Chandrika, Nishad
AU - Garneau-Tsodikova, Sylvie
AU - Tsodikov, Oleg V.
N1 - Funding Information:
This work was supported by a NSF CAREER Award MCB-1149427 (to S.G.-T.), a grant as part of the National Center for Advancing Translational Sciences (UL1TR000117) (to S.G.-T. and O.V.T.), and by startup funds from the College of Pharmacy at the University of Kentucky (to S.G.-T. and O.V.T.). S.M. is a recipient of a 2018 long-term visit fellowship from the Yamada Science Foundation, Japan. The authors thank Dr. James J. La Clair and Prof. Michael D. Burkart from UCSD for valuable discussion and suggestions on optimization of PltM reaction conditions for halogenation. The authors are grateful to the staff of sector SER-CAT of Advanced Photon Source of the Argonne National Laboratory for support during the remote data collection.
Publisher Copyright:
© 2019, The Author(s).
PY - 2019/12/1
Y1 - 2019/12/1
N2 - Controlled halogenation of chemically versatile substrates is difficult to achieve. Here we describe a unique flavin-dependent halogenase, PltM, which is capable of utilizing a wide range of halides for installation on a diverse array of phenolic compounds, including FDA-approved drugs and natural products, such as terbutaline, fenoterol, resveratrol, and catechin. Crystal structures of PltM in complex with phloroglucinol and FAD in different states yield insight into substrate recognition and the FAD recycling mechanism of this halogenase.
AB - Controlled halogenation of chemically versatile substrates is difficult to achieve. Here we describe a unique flavin-dependent halogenase, PltM, which is capable of utilizing a wide range of halides for installation on a diverse array of phenolic compounds, including FDA-approved drugs and natural products, such as terbutaline, fenoterol, resveratrol, and catechin. Crystal structures of PltM in complex with phloroglucinol and FAD in different states yield insight into substrate recognition and the FAD recycling mechanism of this halogenase.
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U2 - 10.1038/s41467-019-09215-9
DO - 10.1038/s41467-019-09215-9
M3 - Article
C2 - 30890712
AN - SCOPUS:85063291405
SN - 2041-1723
VL - 10
JO - Nature communications
JF - Nature communications
IS - 1
M1 - 1255
ER -