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

Benjamin Lefranc 1 Hubert Vaudry Jérôme Leprince 2, 1 Olivier Berteau 3 Alhosna Benjdia 3 Alain Guillot 3
1 DC2N - Différenciation et communication neuronale et neuroendocrine
2 DC2N - Différenciation et communication neuronale et neuroendocrine
3 MICALIS - MICrobiologie de l'ALImentation au Service de la Santé
Abstract : 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 : sulfatase-maturating enzymes prokaryotes posttranslational modification reveals
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https://hal-normandie-univ.archives-ouvertes.fr/hal-01960692
Contributor : Jérôme Leprince Connect in order to contact the contributor
Submitted on : Wednesday, December 19, 2018 - 3:13:03 PM
Last modification on : Friday, March 11, 2022 - 2:41:05 PM

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COMUE-NORMANDIE | INRA | AGROPARISTECH | UNIROUEN | DC2N | UNIV-PARIS-SACLAY | INRAE | GS-BIOSPHERA | GS-HEALTH-DRUG-SCIENCES | MICALIS | NORDIC

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

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