Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Carine Vergne"'
Autor:
Eddy Elisée, Laurine Ducrot, Raphaël Méheust, Karine Bastard, Aurélie Fossey-Jouenne, Gideon Grogan, Eric Pelletier, Jean-Louis Petit, Mark Stam, Véronique de Berardinis, Anne Zaparucha, David Vallenet, Carine Vergne-Vaxelaire
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract Native amine dehydrogenases offer sustainable access to chiral amines, so the search for scaffolds capable of converting more diverse carbonyl compounds is required to reach the full potential of this alternative to conventional synthetic re
Externí odkaz:
https://doaj.org/article/19dd54a88db747b3aaeff48cb3524f74
Autor:
Nikolas Capra, Chloé Lelièvre, Océane Touré, Aurélie Fossey-Jouenne, Carine Vergne-Vaxelaire, Dick B. Janssen, Andy-Mark W. H. Thunnissen, Anne Zaparucha
Publikováno v:
Frontiers in Catalysis, Vol 4 (2024)
The CoA ligase from Metallosphaera sedula (MsACL) can be used for the chemoenzymatic synthesis of amides from carboxylic acids. In this CoA-independent conversion, the enzyme catalyzes the adenylation of a carboxylic acid with the help of ATP, follow
Externí odkaz:
https://doaj.org/article/e79be1107d974a38a3146cf5d3218eee
Autor:
Aurélie Fossey-Jouenne, Laurine Ducrot, Ewald P. J. Jongkind, Eddy Elisée, Anne Zaparucha, Gideon Grogan, Caroline E. Paul, Carine Vergne-Vaxelaire
Publikováno v:
Frontiers in Catalysis, Vol 3 (2023)
Native amine dehydrogenases (nat-AmDHs) catalyze the (S)-stereoselective reductive amination of various ketones and aldehydes in the presence of high concentrations of ammonia. Based on the structure of CfusAmDH from Cystobacter fuscus complexed with
Externí odkaz:
https://doaj.org/article/c32f5be7224942469cfcd8089113a86c
Autor:
Thomas Bessonnet, Aline Mariage, Jean-Louis Petit, Virginie Pellouin, Adrien Debard, Anne Zaparucha, Carine Vergne-Vaxelaire, Véronique de Berardinis
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 9 (2021)
Despite the success of some nitrilases in industrial applications, there is a constant demand to broaden the catalog of these hydrolases, especially robust ones with high operational stability. By using the criteria of thermoresistance to screen a co
Externí odkaz:
https://doaj.org/article/0a695ba44560498984da5b74a6a4e77f
Autor:
Jérémy Domergue, Diane Erdmann, Aurélie Fossey-Jouenne, Jean-Louis Petit, Adrien Debard, Véronique de Berardinis, Carine Vergne-Vaxelaire, Anne Zaparucha
Publikováno v:
AMB Express, Vol 9, Iss 1, Pp 1-11 (2019)
Abstract Flavin-dependent halogenases (FHals) catalyse the halogenation of electron-rich substrates, mainly aromatics. Halogenated compounds have many applications, as pharmaceutical, agrochemicals or as starting materials for the synthesis of comple
Externí odkaz:
https://doaj.org/article/6456068c0d5a413fa45760cd3270acca
Autor:
Alain Perret, Christophe Lechaplais, Sabine Tricot, Nadia Perchat, Carine Vergne, Christine Pellé, Karine Bastard, Annett Kreimeyer, David Vallenet, Anne Zaparucha, Jean Weissenbach, Marcel Salanoubat
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e22918 (2011)
BackgroundBacteria are key components in all ecosystems. However, our knowledge of bacterial metabolism is based solely on the study of cultivated organisms which represent just a tiny fraction of microbial diversity. To access new enzymatic reaction
Externí odkaz:
https://doaj.org/article/f697af082c04491d853e25a9ad2db1d8
Autor:
Laurine Ducrot, Megan Bennett, Gwenaëlle André‐Leroux, Eddy Elisée, Sacha Marynberg, Aurélie Fossey‐Jouenne, Anne Zaparucha, Gideon Grogan, Carine Vergne‐Vaxelaire
Publikováno v:
ChemCatChem. 14
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f9cbb0fdd329349899793a955daa3d65
https://doi.org/10.1002/cctc.202201257
https://doi.org/10.1002/cctc.202201257
Autor:
Laurine Ducrot, Megan Bennett, Gwenaëlle André‐Leroux, Eddy Elisée, Sacha Marynberg, Aurélie Fossey‐Jouenne, Anne Zaparucha, Gideon Grogan, Carine Vergne‐Vaxelaire
Publikováno v:
ChemCatChem
ChemCatChem, 2022, 2022, pp.e202200880. ⟨10.1002/cctc.202200880⟩
ChemCatChem, 2022, 2022, pp.e202200880. ⟨10.1002/cctc.202200880⟩
International audience; Native Amine Dehydrogenases (nat-AmDHs) are NAD(P)H-enzymes performing reductive amination, mainly active towards small aliphatic aldehydes and cyclic ketones, due to active site volumes limited by the presence of several bulk
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a89f08329eeff2420e990ee5604baee9
https://doi.org/10.1002/cctc.202200880
https://doi.org/10.1002/cctc.202200880
Autor:
Carine Vergne-Vaxelaire, Chloé M. Lelièvre, Jean-Louis Petit, Anne Zaparucha, Mélanie Balandras
Publikováno v:
ChemCatChem
ChemCatChem, 2019, 12 (4), pp.1184-1189. ⟨10.1002/cctc.201901870⟩
ChemCatChem, 2019, 12 (4), pp.1184-1189. ⟨10.1002/cctc.201901870⟩
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::701327742039ab710f7f9e47bb551fbc
https://doi.org/10.1002/cctc.201901870
https://doi.org/10.1002/cctc.201901870
Publikováno v:
Chembiochem : a European journal of chemical biology. 23(10)
Native amine dehydrogenases (nat-AmDHs) have recently emerged as a potentially valuable new reservoir of enzymes for the sustainable and selective synthesis of chiral amines, catalyzing the NAD(P)H-dependent ammoniation of carbonyl compounds with hig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2600eae2e32384dd8c0376ba920e8dc3
https://pubmed.ncbi.nlm.nih.gov/35349204
https://pubmed.ncbi.nlm.nih.gov/35349204