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 |
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| Přispěvatelé: | Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Conception d’Architectures Moléculaires et Processus Electroniques (CAMPE ), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), ANR-16-CE29-0019,CARBONARA,Contrôle de la coupure de liaisons carbone-carbone par les enzymes à radical SAM(2016), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017) |
| Rok vydání: | 2021 |
| Předmět: |
S-Adenosylmethionine
Multidisciplinary [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Tryptophan MESH: S-Adenosylmethionine General Physics and Astronomy Lyases General Chemistry MESH: Catalysis MESH: Lyases General Biochemistry Genetics and Molecular Biology Catalysis MESH: Tyrosine Tyrosine MESH: Tryptophan |
| Zdroj: | Nature Communications Nature Communications, 2022, 13 (1), pp.2284. ⟨10.1038/s41467-022-29980-4⟩ |
| ISSN: | 2041-1723 |
| Popis: | 2-iminoacetate synthase ThiH is a radical S-adenosyl-L-methionine (SAM) L-tyrosine lyase and catalyzes the L-tyrosine Cα–Cβ bond break to produce dehydroglycine and p-cresol while the radical SAM L-tryptophan lyase NosL cleaves the L-tryptophan Cα–C bond to produce 3-methylindole-2-carboxylic acid. It has been difficult to understand the features that condition one C–C bond break over the other one because the two enzymes display significant primary structure similarities and presumably similar substrate-binding modes. Here, we report the crystal structure of L-tyrosine bound ThiH from Thermosinus carboxydivorans revealing an unusual protonation state of L-tyrosine upon binding. Structural comparison of ThiH with NosL and computational studies of the respective reactions they catalyze show that substrate activation is eased by tunneling effect and that subtle structural changes between the two enzymes affect, in particular, the hydrogen-atom abstraction by the 5´-deoxyadenosyl radical species, driving the difference in reaction specificity. |
| Databáze: | OpenAIRE |
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