Dr Larissa Balakireva, CEO & Founder of NovoCIB, was awarded with the Trophy of
"Femmes en Or 2011, Femme de l'Innovation"
in September 2011
IMPDH Enzymes

Inosine Monophosphate Dehydrogenase (IMPDH) (EC catalyzes the conversion of inosine 5’-monophosphate (IMP) to xanthosine 5’- monophosphate (XMP), which is a crucial step for guanosine biosynthesis and for the pool of guanine nucleotides.

In Human, IMPDH is a validated target for several therapeutic applications (cancer, immunological disorders...). Several IMPDH inhibitors, including blockbusters (e.g. CellCept®), have shown their clinical efficacy. Besides nucleoside (or NAD) analogues, new chemical entities (NCEs) have been identified as efficient IMPDH inhibitors and are currently investigated.

Mammalian and bacterial IMPDHs are known to have significantly different kinetic properties and inhibitor sensitivities(1, 2).
NOVOCIB provides two recombinant IMPDH enzymes: Human IMPDH, Type II, and Staphylococcus aureus IMPDH. These two enzymes are useful tools for the selection of species-specific IMPDH inhibitors.

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... or download our brochure "NovoCIB's IMPDH Products & Services" 


References (with links to PubMed)
1. L. Hedstrom and L. Gan (2006): IMP dehydrogenase: structural schizophrenia and an unusual base Curr. Opin. Chem. Biol. 10(5), 520-525
2. R. Zhang et al. (1999): Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase Biochemistry 13;38(15), 4691-700

Related Links
Purine Metabolism Enzymes
IMPDH Inhibition: Whole Cell Assay
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