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.
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| http://dx.doi.org/10.1038/s41467-019-09215-9 | DOI Listing |
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Publisher Correction: Unusual substrate and halide versatility of phenolic halogenase PltM.
Nat Commun
April 2019
Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY, 40536-0596, USA.
The original version of this Article contained an error in Fig. 1, in which the labels 'NADP' and 'NADPH + H' were incorrectly given as 'NADPH' and 'NADPH + H', respectively. This has been corrected in both the PDF and HTML versions of the Article.
View Article and Find Full Text PDFUnusual substrate and halide versatility of phenolic halogenase PltM.
Nat Commun
March 2019
Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY, 40536-0596, USA.
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.
View Article and Find Full Text PDFA novel halogenase gene from the pentachloropseudilin producer Actinoplanes sp. ATCC 33002 and detection of in vitro halogenase activity.
FEMS Microbiol Lett
August 2004
Institut für Biochemie, Technische Universität Dresden, D-01062 Dresden, Germany.
A novel halogenase gene (halB) was isolated from a cosmid library of the pentachloropseudilin producer Actinoplanes sp. ATCC 33002. The halogenase has high identity (55%) to the flavin-dependent monodechloroaminopyrrolnitrin-3 halogenase from pyrrolnitrin biosynthesis and to the halogenases PltM and PltA (35% and 28%, respectively) involved in pyoluteorin biosynthesis.
View Article and Find Full Text PDFCharacterization of the pyoluteorin biosynthetic gene cluster of Pseudomonas fluorescens Pf-5.
J Bacteriol
April 1999
Agricultural Research Service, U.S. Department of Agriculture, Corvallis, Oregon 97330, USA.
Ten genes (plt) required for the biosynthesis of pyoluteorin, an antifungal compound composed of a bichlorinated pyrrole linked to a resorcinol moiety, were identified within a 24-kb genomic region of Pseudomonas fluorescens Pf-5. The deduced amino acid sequences of eight plt genes were similar to the amino acid sequences of genes with known biosynthetic functions, including type I polyketide synthases (pltB, pltC), an acyl coenzyme A (acyl-CoA) dehydrogenase (pltE), an acyl-CoA synthetase (pltF), a thioesterase (pltG), and three halogenases (pltA, pltD, and pltM). Insertions of the transposon Tn5 or Tn3-nice or a kanamycin resistance gene in each of these genes abolished pyoluteorin production by Pf-5.
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