Zobrazeno 1 - 10
of 76
pro vyhledávání: '"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
Publikováno v:
ACS Bio & Med Chem Au, Vol 2, Iss 1, Pp 36-52 (2021)
Externí odkaz:
https://doaj.org/article/c017083a0f1943978c81d54333b8188b
Autor:
Yuxuan Ji, Li Wei, Anqi Da, Holger Stark, Peter-Leon Hagedoorn, Simone Ciofi-Baffoni, Sally A. Cowley, Ricardo O. Louro, Smilja Todorovic, Maria Andrea Mroginski, Yvain Nicolet, Maxie M. Roessler, Nick E. Le Brun, Mario Piccioli, William S. James, Wilfred R. Hagen, Kourosh H. Ebrahimi
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Externí odkaz:
https://doaj.org/article/14e01c9c674845c487345b274dc920b1
Autor:
Tu-Quynh Nguyen, Yvain Nicolet
Publikováno v:
Life, Vol 12, Iss 11, p 1732 (2022)
Methyl transfer is essential in myriad biological pathways found across all domains of life. Unlike conventional methyltransferases that catalyze this reaction through nucleophilic substitution, many members of the radical S-adenosyl-L-methionine (SA
Externí odkaz:
https://doaj.org/article/491edeb5b64a4cf490919985520ab0be
Autor:
Mickaël V. Cherrier, Xavier Vernède, Daphna Fenel, Lydie Martin, Benoit Arragain, Emmanuelle Neumann, Juan C. Fontecilla-Camps, Guy Schoehn, Yvain Nicolet
Publikováno v:
Biomolecules, Vol 12, Iss 3, p 441 (2022)
Metalloproteins are involved in key cell processes such as photosynthesis, respiration, and oxygen transport. However, the presence of transition metals (notably iron as a component of [Fe-S] clusters) often makes these proteins sensitive to oxygen-i
Externí odkaz:
https://doaj.org/article/05ce7557a27e4bf797cb124b44be0a08
Publikováno v:
ACS Bio & Med Chem Au
ACS Bio & Med Chem Au, ACS Publications, In press, ⟨10.1021/acsbiomedchemau.1c00044⟩
ACS Bio & Med Chem Au, inPress, ⟨10.1021/acsbiomedchemau.1c00044⟩
ACS Bio & Med Chem Au, Vol 2, Iss 1, Pp 36-52 (2021)
ACS Bio & Med Chem Au, ACS Publications, In press, ⟨10.1021/acsbiomedchemau.1c00044⟩
ACS Bio & Med Chem Au, inPress, ⟨10.1021/acsbiomedchemau.1c00044⟩
ACS Bio & Med Chem Au, Vol 2, Iss 1, Pp 36-52 (2021)
International audience; This Review focuses on the structure–function relationship of radical S-adenosyl-l-methionine (SAM) enzymes involved in the assembly of metallocofactors corresponding to the active sites of [FeFe]-hydrogenase and nitrogenase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a284d21655ccbc1706072aa624f1d1a2
https://doi.org/10.1021/acsbiomedchemau.1c00044
https://doi.org/10.1021/acsbiomedchemau.1c00044
Autor:
Kourosh Honarmand Ebrahimi, Simone Ciofi-Baffoni, Peter-Leon Hagedoorn, Yvain Nicolet, Nick E. Le Brun, Wilfred R. Hagen, Fraser A. Armstrong
Publikováno v:
Nature Chemistry
Nature Chemistry, 2022, ⟨10.1038/s41557-021-00882-0⟩
Nature Chemistry, 2022, ⟨10.1038/s41557-021-00882-0⟩
International audience; A virus hijacks host cellular machineries and metabolites in order to reproduce. In response, the innate immune system activates different processes to fight back. Although many aspects of these processes have been well invest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fe8a9e54975c5decf23489f1ee8a705
https://ueaeprints.uea.ac.uk/id/eprint/84422/
https://ueaeprints.uea.ac.uk/id/eprint/84422/
Autor:
Hai Nguyen, I Dewa Made Kresna, Nils Böhringer, Jeremie Ruel, Eugenio de la Mora, Jil-Christine Kramer, Kim Lewis, Yvain Nicolet, Till F. Schäberle, Kenichi Yokoyama
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, 2022, ⟨10.1021/jacs.2c05565⟩
J Am Chem Soc
Journal of the American Chemical Society, 2022, ⟨10.1021/jacs.2c05565⟩
J Am Chem Soc
International audience; Darobactin A is a ribosomally synthesized, post-translationally modified peptide (RiPP) with potent and broad-spectrum anti-Gram-negative antibiotic activity. The structure of darobactin A is characterized by an ether and C-C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb4783972ad67702351b48036dd885ea
https://publica.fraunhofer.de/handle/publica/442259
https://publica.fraunhofer.de/handle/publica/442259
Publikováno v:
Nature Communications
Nature Communications, 2022, 13 (1), pp.2284. ⟨10.1038/s41467-022-29980-4⟩
Nature Communications, 2022, 13 (1), pp.2284. ⟨10.1038/s41467-022-29980-4⟩
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 C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::300785c8e8b59f75ab19d81a0e23c253
https://pubmed.ncbi.nlm.nih.gov/35477710
https://pubmed.ncbi.nlm.nih.gov/35477710
Publikováno v:
Chemical Science
The nitrogenase MoFe protein contains two different FeS centers, the P-cluster and the iron–molybdenum cofactor (FeMo-co). The former is a [Fe8S7] center responsible for conveying electrons to the latter, a [MoFe7S9C-(R)-homocitrate] species, where
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ed9b2c2e7987f4dbe58dbc1edc7b5961
https://pubmed.ncbi.nlm.nih.gov/34168778
https://pubmed.ncbi.nlm.nih.gov/34168778