The crystal structure of FeS quinolinate synthase unravels an enzymatic dehydration mechanism that uses tyrosine and a hydrolase-type triad. Mickael V Cherrier, Alice Chan, Claudine Darnault, Debora Reichmann, Patricia Amara, Sandrine Ollagnier de Choudens, Juan-Carlos Fontecilla-Camps
To cite this version:
Mickael V Cherrier, Alice Chan, Claudine Darnault, Debora Reichmann, Patricia Amara, et al.. The crystal structure of FeS quinolinate synthase unravels an enzymatic dehydration mechanism that uses tyrosine and a hydrolase-type triad.. Journal of the American Chemical Society, American Chemical Society, 2014, 136 (14), pp.5253-5256. 10.1021/ja501431b. hal-01054288
HAL Id: hal-01054288 https://hal.archives-ouvertes.fr/hal-01054288 Submitted on 6 Aug 2014
HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. The crystal structure of Fe4S4quinolinate synthase unravels an enzymatic dehydration mechanism that uses tyrosine and a hydrolase-type triad. Mickaël V. Cherrier, , Alice Chan,§ Claudine Darnault, Debora Reichmann, § Patricia Amara, Sandrine Ollagnier de Choudens*,§ and Juan C. Fontecilla-Camps*,