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© Institut Pasteur
Cristaux de cellulase, enzyme purifiée de Clostridium thermocellum permettant la digestion de la cellulose. Image colorisée.

About

We are currently developing modified nucleos(t)ides as substrate mimics to provide insight into enzyme substrate recognition, as well as libraries of functionalized heterocycles useful for the fragment based approach. Novel enzymatic routes (transglycosylation, deamination, phosphorylation) as an alternative to chemical approaches are also considered. The synthesized molecules find applications in the identification of inhibitors of essential bacterial enzymes (TMPK from Mycobacterium tuberculosis, DNPH1, an N-hydrolase involved in cell proliferation, NAD kinases from Gram-positive bacteria). In addition, the new chemical entities implement the in house chemical libraries.

Former Members

Projects

Project
Ongoing
10 Members

Inhibitors of bacterial NAD kinases

Sylvie Pochet (PI)

NAD mimics as potential antibacterial agents The NAD(P) biosynthesis pathways have attracted recent interest as a source of enzyme targets for the development of antimicrobial agents. Our own research focused on the structure-based development […]
Project
Ongoing
9 Members

Protein synthesis machinery of Trypanosomatid as a therapeutic target

Nadia Izadi-Pruneyre (PI)

Pathogenic protozoans of the trypanosomatid group still remain a major world health problem. Cycling between insect vectors and mammalian hosts, Trypanosoma cruzi is the causative agent of Chagas disease, while over 20 Leishmania species […]
Project
Completed
7 Members

Inhibitors of the 2’-deoxyribonucleotide N-hydrolase DNPH1, an enzyme involved in cellular growth and angiogenesis

Sylvie Pochet (PI)

Nucleoside analogues as potential antitumor agents. This project aims to characterize and validate the nucleotide N-hydrolase DNPH1 as a new target in oncology. Inhibition of Rcl alone or in combination with other chemotherapeutic drugs […]
Project
Ongoing
9 Members

Inhibitors of Pseudomonas aeruginosa IMPDH

Sophie Vichier-Guerre (PI)

IMPDH from Pseudomonas aeruginosa (see Inosine-5′-monophosphate dehydrogenase project) was found to be allosterically regulated by MgATP (Labesse et al., 2013). The discovery of this mode of regulation of the catalytic activity, never described before […]
Project
Completed
5 Members

Inhibitors of TMPK from Mycobacterium tuberculosis

Hélène Munier-Lehmann (PI)

TMPK from Mycobacterium tuberculosis belongs to the NMPK family, which was chosen as potential targets for the development of new antimicrobials (see “Nucleoside monophosphate kinases” project). Based on the 3D-structure of TMPK from M. […]

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Contact

Phone: 33/1 40 61 38 05 Email: sylvie.pochet@pasteur.fr Address 25-28 Rue du Docteur Roux 75015, Paris France