Thioether bond formation by SPASM domain radical SAM enzymes: Cα H-atom abstraction in subtilosin A biosynthesis

AlbA is a radical SAM enzyme catalyzing the formation of three unusual thioether bonds in the antibiotic subtilosin A. We demonstrate here that AlbA catalyzes direct Cα H-atom abstraction and likely contains three essential [4Fe-4S] centers. This leads us to propose novel mechanistic perspectives fo...

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Veröffentlicht in:	Chemical communications (Cambridge, England) England), 2016-01, Vol.52 (37), p.6249-6252
Hauptverfasser:	Benjdia, Alhosna, Guillot, Alain, Lefranc, Benjamin, Vaudry, Hubert, Leprince, Jérôme, Berteau, Olivier
Format:	Artikel
Sprache:	eng
Schlagworte:	Anti-Bacterial Agents Bacterial Proteins Bacteriocins Biocatalysis Cell Behavior Cellular Biology Chemical Sciences Free Radicals Life Sciences Medicinal Chemistry Models, Molecular Neurobiology Neurons and Cognition Peptides, Cyclic Pharmaceutical sciences Pharmacology Sulfides
Online-Zugang:	Volltext
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Beschreibung
Zusammenfassung:	AlbA is a radical SAM enzyme catalyzing the formation of three unusual thioether bonds in the antibiotic subtilosin A. We demonstrate here that AlbA catalyzes direct Cα H-atom abstraction and likely contains three essential [4Fe-4S] centers. This leads us to propose novel mechanistic perspectives for thioether bond catalysis by radical SAM enzymes.
ISSN:	1359-7345 1364-548X
DOI:	10.1039/c6cc01317a