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Research article - Peer-reviewed, 2009

Mechanistic Investigations of Anaerobic Sulfatase-Maturating Enzyme: Direct C-beta H-Atom Abstraction Catalyzed by a Radical AdoMet Enzyme

Benjdia, Alhosna; Leprince, Jerome; Sandstrom, Corine; Vaudry, Hubert; Berteau, Olivier


Sulfatases are unique in requiring an essential post-translational modification of a critical active-site cysteinyt or seryl residue to 3-oxoalanine usually called C alpha-formylglycine (FGly). This post-translational modification is catalyzed anaerobically by anaerobic Sulfatase Maturating Enzyme (anSME), a member of the radical AdoMet superfamily. Using a new labeled substrate, we demonstrate that anSME uses a 5'-deoxyadenosyl radical to catalyze direct H-atom abstraction from the substrate. We thus established that anSMEs are the first radical AdoMet enzymes catalyzing a post-translational modification involving C, H-atom abstraction from an active site cysteinyl or seryl residue. This mechanistic study allowed us to decipher the first steps of the mechanism of this new radical AdoMet enzyme family.

Published in

Journal of the American Chemical Society
2009, volume: 131, number: 24, pages: 8348-8349

Authors' information

Benjdia, Alhosna
Leprince, Jerome
Swedish University of Agricultural Sciences, Department of Chemistry
Vaudry, Hubert
Berteau, Olivier

UKÄ Subject classification

Organic Chemistry
Biochemistry and Molecular Biology

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