Unknown

Dataset Information

0

Unusual substrate and halide versatility of phenolic halogenase PltM.


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.

SUBMITTER: Mori S 

PROVIDER: S-EPMC6424973 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Unusual substrate and halide versatility of phenolic halogenase PltM.

Mori Shogo S   Pang Allan H AH   Thamban Chandrika Nishad N   Garneau-Tsodikova Sylvie S   Tsodikov Oleg V OV  

Nature communications 20190319 1


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 t  ...[more]

Similar Datasets

| S-EPMC5627516 | biostudies-literature
| S-EPMC7754283 | biostudies-literature
| S-EPMC4456221 | biostudies-literature
| S-EPMC6218459 | biostudies-literature
| S-EPMC3375752 | biostudies-literature
| S-EPMC2764930 | biostudies-literature
| S-EPMC8498867 | biostudies-literature
| S-EPMC6411290 | biostudies-literature
| S-EPMC5091363 | biostudies-literature
2022-01-01 | GSE168700 | GEO