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Unusual substrate and halide versatility of phenolic halogenase PltM.
- Source :
-
Nature communications [Nat Commun] 2019 Mar 19; Vol. 10 (1), pp. 1255. Date of Electronic Publication: 2019 Mar 19. - Publication Year :
- 2019
-
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.
- Subjects :
- Bacterial Proteins chemistry
Bacterial Proteins genetics
Binding Sites
Crystallography, X-Ray
Flavin-Adenine Dinucleotide chemistry
Flavins chemistry
Halogenation
Models, Molecular
Mutagenesis
Oxidoreductases genetics
Phloroglucinol chemistry
Phloroglucinol metabolism
Substrate Specificity
Bacterial Proteins metabolism
Flavin-Adenine Dinucleotide metabolism
Oxidoreductases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2041-1723
- Volume :
- 10
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Nature communications
- Publication Type :
- Academic Journal
- Accession number :
- 30890712
- Full Text :
- https://doi.org/10.1038/s41467-019-09215-9