L-tyrosine-bound ThiH structure reveals C–C bond break differences within radical SAM aromatic amino acid lyases

Autor: Patricia Amara, Claire Saragaglia, Jean-Marie Mouesca, Lydie Martin, Yvain Nicolet

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)

ThiH is a radical SAM L-tyrosine lyase involved in the biosynthesis of the thiazole ring of vitamin B1. Here, the authors report the crystal structure of ThiH in complex with its L-tyrosine substrate, revealing an unexpected protonation state and tun

Externí odkaz: https://doaj.org/article/7de329fe16964e7aa1a98eeb2de5da9e

Radical S -Adenosyl- l -methionine Tryptophan Lyase (NosL): How the Protein Controls the Carboxyl Radical •CO 2 – Migration

Autor: Maxime Bella, Yvain Nicolet, Lydie Martin, Jean-Marie Mouesca, Patricia Amara, Claire Saragaglia, Serge Gambarelli

Publikováno v: Journal of the American Chemical Society
Journal of the American Chemical Society, American Chemical Society, 2018, 140 (48), pp.16661-16668. ⟨10.1021/jacs.8b09142⟩
Journal of the American Chemical Society, 2018, 140 (48), pp.16661-16668. ⟨10.1021/jacs.8b09142⟩

International audience; The radical S-adenosyl-l-methionine tryptophan lyase uses radical-based chemistry to convert l-tryptophan into 3-methyl-2-indolic acid, a fragment in the biosynthesis of the thiopeptide antibiotic nosiheptide. This complex rea

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8372c1ceeeedecfd0768a8be9788bca5
https://hal.archives-ouvertes.fr/hal-02008403

L-tyrosine-bound ThiH structure reveals C–C bond break differences within radical SAM aromatic amino acid lyases.

Autor: Amara, Patricia, Saragaglia, Claire, Mouesca, Jean-Marie, Martin, Lydie, Nicolet, Yvain

Publikováno v: Nature Communications; 4/27/2022, Vol. 13 Issue 1, p1-11, 11p