Synthesis and Kinetic evaluation of an azido analogue of methylerythritol phosphate: a Novel Inhibitor of E. coli YgbP/IspD

Autor: Jean-Luc Ferrer, Philippe Chaignon, Alain Wagner, Franck Borel, Zoljargal Baatarkhuu, Myriam Seemann

Publikováno v: Scientific Reports, Vol 8, Iss 1, Pp 1-10 (2018)
Scientific Reports
Scientific Reports, 2018, 8 (1), pp.17892. ⟨10.1038/s41598-018-35586-y⟩
Scientific Reports, Nature Publishing Group, 2018, 8 (1), pp.17892. ⟨10.1038/s41598-018-35586-y⟩

As multidrug resistant pathogenic microorganisms are a serious health menace, it is crucial to continuously develop novel medicines in order to overcome the emerging resistance. The methylerythritol phosphate pathway (MEP) is an ideal target for anti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::443ca381a1e8559840927d4eecb0babf
http://link.springer.com/article/10.1038/s41598-018-35586-y

Isoprenoid Biosynthesis in Pathogenic Bacteria: Nuclear Resonance Vibrational Spectroscopy Provides Insight into the Unusual [4Fe-4S] Cluster of theE. coliLytB/IspH Protein

Autor: Isabelle Faus, Juliusz A. Wolny, S. Rackwitz, Kai Schlage, Hans-Christian Wille, Sergiy Krasutsky, C. Dale Poulter, Aleksandr I. Chumakov, Annegret Reinhard, Volker Schünemann, Philippe Chaignon, Myriam Seemann

Publikováno v: Angewandte Chemie International Edition. 54:12584-12587

The LytB/IspH protein catalyzes the last step of the methylerythritol phosphate (MEP) pathway which is used for the biosynthesis of essential terpenoids in most pathogenic bacteria. Therefore, the MEP pathway is a target for the development of new an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b94deae195901661a89a421621440725
https://doi.org/10.1002/anie.201502494

NADH oxidase activity ofBacillus subtilisnitroreductase NfrA1: Insight into its biological role

Autor: Jamal Ouazzani, Philippe Chaignon, Gilles Truan, Philippe Meyer, Sylvie Cortial, Solange Moréra, Stéphane Aymerich, Virginie Gueguen-Chaignon, Bogdan I. Iorga

Publikováno v: FEBS Letters
FEBS Letters, Wiley, 2010, 584 (18), pp.3916-22. ⟨10.1016/j.febslet.2010.08.019⟩

NfrA1 nitroreductase from the Gram-positive bacterium Bacillus subtilis is a member of the NAD(P)H/FMN oxidoreductase family. Here, we investigated the reactivity, the structure and kinetics of NfrA1, which could provide insight into the unclear biol

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc223e09d1bb1598e431bbde2a5b8c8d
https://doi.org/10.1016/j.febslet.2010.08.019

Biofilms of clinical strains ofStaphylococcusthat do not contain polysaccharide intercellular adhesin

Autor: Saïd Jabbouri, Irina Sadovskaya, Philippe Chaignon, Grigorij Kogan, Ali Chokr

Publikováno v: FEMS Microbiology Letters. 255:11-16

Staphylococcus aureus and coagulase-negative staphylococci, primarily Staphylococcus epidermidis, are recognized as a major cause of nosocomial infections associated with the use of implanted medical devices. The capacity of S. epidermidis to form bi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::690b29c6f0709f5c2dc09b609cf9eae7
https://doi.org/10.1111/j.1574-6968.2005.00043.x

Purification and identification of a Bacillus nitroreductase: Potential use in 3,5-DNBTF biosensoring system

Autor: A.P. Ventura, Philippe Lopes, Frédéric Halgand, Sylvie Cortial, Philippe Chaignon, Olivier Laprévote, Jamal Ouazzani

Publikováno v: Enzyme and Microbial Technology
Enzyme and Microbial Technology, Elsevier, 2006, 39(7), pp.1499-1506. ⟨10.1016/j.enzmictec.2006.04.023⟩

We have investigated a specific enzymatic biosensor for detecting target pollutant 3,5-dinitro-trifluoromethylbenzene (3,5-DNBTF). The predicted enzyme is a nitroreductase that catalyzes the total nitroreduction of 3,5-DNBTF to its corresponding diam

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::030040131857d17ebef752e2932b6233
https://hal.archives-ouvertes.fr/hal-00114082