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Journal articles
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.
https://hal-normandie-univ.archives-ouvertes.fr/hal-01960686
Contributor : Jérôme Leprince Connect in order to contact the contributor
Submitted on : Wednesday, December 19, 2018 - 3:11:08 PM
Last modification on : Wednesday, January 26, 2022 - 2:00:29 PM
Contributor : Jérôme Leprince Connect in order to contact the contributor
Submitted on : Wednesday, December 19, 2018 - 3:11:08 PM
Last modification on : Wednesday, January 26, 2022 - 2:00:29 PM
