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

Abstract : Sulfatases are unique in requiring an essential post-translational modification of a critical active-site cysteinyl 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(beta) 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.
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https://hal-normandie-univ.archives-ouvertes.fr/hal-01960686
Contributor : Jérôme Leprince <>
Submitted on : Wednesday, December 19, 2018 - 3:11:08 PM
Last modification on : Tuesday, September 8, 2020 - 5:34:01 PM

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Alhosna Benjdia, Corine Sandstrom, Hubert Vaudry, Olivier Berteau, Jérôme Leprince, et al.. Mechanistic Investigations of Anaerobic Sulfatase-Maturating Enzyme: Direct C β H-Atom Abstraction Catalyzed by a Radical AdoMet Enzyme. Journal of the American Chemical Society, American Chemical Society, 2009, 131 (24), pp.8348-8349. ⟨10.1021/ja901571p⟩. ⟨hal-01960686⟩

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