Anaerobic Sulfatase-Maturating Enzymes: Radical SAM Enzymes Able To Catalyze in Vitro Sulfatase Post-translational Modification - Normandie Université Accéder directement au contenu
Article Dans Une Revue Journal of the American Chemical Society Année : 2007

Anaerobic Sulfatase-Maturating Enzymes: Radical SAM Enzymes Able To Catalyze in Vitro Sulfatase Post-translational Modification

Anaerobic sulfatase-maturating enzymes: radical SAM enzymes able to catalyze in vitro sulfatase post-translational modification.

Résumé

Sulfatases are widespread enzymes, found from prokaryotes to eukaryotes and involved in many biochemical processes. To be active, all known sulfatases undergo a unique post-translational modification leading to the conversion of a critical active-site residue, i.e., a serine or a cysteine, into a C alpha-formylglycine (FGly). Two different systems are involved in sulfatase maturation. One, named FGE, is an oxygen-dependent oxygenase and has been fully characterized. The other one, a member of the so-called "radical SAM" super-family, has been only preliminary investigated. This latter system allows the maturation of sulfatases in strictly anaerobic conditions and has thus been named anSME (anaerobic Sulfatase Maturating Enzyme). Our results provide the first experimental evidence that anSME are iron-sulfur enzymes able to perform the reductive cleavage of SAM and thus belong to the radical SAM super-family. Furthermore, they demonstrate that anSME are able to efficiently oxidize cysteine into FGly in an oxygen-independent manner.

Dates et versions

hal-01960680 , version 1 (19-12-2018)

Identifiants

Citer

Alhosna Benjdia, Jérôme Leprince, Alain Guillot, Hubert Vaudry, Sylvie Rabot, et al.. Anaerobic Sulfatase-Maturating Enzymes: Radical SAM Enzymes Able To Catalyze in Vitro Sulfatase Post-translational Modification. Journal of the American Chemical Society, 2007, 129 (12), pp.3462-3463. ⟨10.1021/ja067175e⟩. ⟨hal-01960680⟩
30 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More