期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 131, 期 24, 页码 8348-+出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja901571p
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资金
- Region Ile-de-France
- Agence Nationale de la Recherche [ANR-08-BLAN-0224-02]
- Agence Nationale de la Recherche (ANR) [ANR-08-BLAN-0224] Funding Source: Agence Nationale de la Recherche (ANR)
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.
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