Unusual substrate and halide versatility of phenolic halogenase PltM

Shogo Mori, Allan H. Pang, Nishad Thamban Chandrika, Sylvie Garneau-Tsodikova () and Oleg V. Tsodikov ()
Additional contact information
Shogo Mori: University of Kentucky
Allan H. Pang: University of Kentucky
Nishad Thamban Chandrika: University of Kentucky
Sylvie Garneau-Tsodikova: University of Kentucky
Oleg V. Tsodikov: University of Kentucky

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: 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.

Date: 2019
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-019-09215-9 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-09215-9

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-019-09215-9

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().