Structural highlights
Publication Abstract from PubMed
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.
Unusual substrate and halide versatility of phenolic halogenase PltM.,Mori S, Pang AH, Thamban Chandrika N, Garneau-Tsodikova S, Tsodikov OV Nat Commun. 2019 Mar 19;10(1):1255. doi: 10.1038/s41467-019-09215-9. PMID:30890712[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mori S, Pang AH, Thamban Chandrika N, Garneau-Tsodikova S, Tsodikov OV. Unusual substrate and halide versatility of phenolic halogenase PltM. Nat Commun. 2019 Mar 19;10(1):1255. doi: 10.1038/s41467-019-09215-9. PMID:30890712 doi:http://dx.doi.org/10.1038/s41467-019-09215-9
