Unusual substrate and halide versatility of phenolic halogenase PltM.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 30890712.
- Also identified by DOI 10.1038/s41467-019-09215-9 and PMC identifier 6424973.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
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.
Medical subject headings
- Bacterial Proteins
- Flavin-Adenine Dinucleotide
- Oxidoreductases