Thioether bond formation by SPASM domain radical SAM enzymes: C α H-atom abstraction in subtilosin A biosynthesis

Alhosna Benjdia (1) , Alain Guillot (1) , Benjamin Lefranc (2, 3) , Hubert Vaudry (3, 2) , Jérôme Leprince (4, 3) , Olivier Berteau (1)

1 MICALIS - MICrobiologie de l'ALImentation au Service de la Santé
2 DC2N - Différenciation et communication neuronale et neuroendocrine
3 IRIB - Institute for Research and Innovation in Biomedicine
4 DC2N - Différenciation et communication neuronale et neuroendocrine

AlbA is a radical SAM enzyme catalyzing the formation of three unusual thioether bonds in the antibiotic subtilosin A. We demonstrate here that AlbA catalyzes direct Cα H-atom abstraction and likely contains three essential [4Fe-4S] centers. This leads us to propose novel mechanistic perspectives for thioether bond catalysis by radical SAM enzymes.

Keywords: Reveals; Prokaryotes; Posttranslational modification; Sulfatase-maturating enzymes

Keywords: Bacillus-subtilis; Substrate

Domains: Chemical Sciences; Medicinal Chemistry; Life Sciences [q-bio]; Cellular Biology; Cell Behavior [q-bio.CB]; Life Sciences [q-bio]; Neurons and Cognition [q-bio.NC]; Neurobiology; Life Sciences [q-bio]; Pharmaceutical sciences; Pharmacology

Alhosna Benjdia, Alain Guillot, Benjamin Lefranc, Hubert Vaudry, Jérôme Leprince, et al.. Thioether bond formation by SPASM domain radical SAM enzymes: C α H-atom abstraction in subtilosin A biosynthesis. Chemical Communications, 2016, 52 (37), pp.6249-6252. ⟨10.1039/c6cc01317a⟩. ⟨hal-01960692⟩