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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Binding Sites
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Crystallography, X-Ray
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Flavin-Adenine Dinucleotide / chemistry
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Flavin-Adenine Dinucleotide / metabolism*
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Flavins / chemistry
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Halogenation
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Models, Molecular
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Mutagenesis
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Oxidoreductases / genetics
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Oxidoreductases / metabolism*
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Phloroglucinol / chemistry
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Phloroglucinol / metabolism
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Substrate Specificity
Substances
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Bacterial Proteins
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Flavins
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Flavin-Adenine Dinucleotide
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Phloroglucinol
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Oxidoreductases