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

Purine Metabolism Enzymes

 IMPDH    PNP    XDH    HGPRT

Purine and pyrimidine nucleotides are universal metabolites of all earth-living organisms. Building blocks of DNA, RNA and coenzymes, they are also key players of numerous cell metabolism processes: energy vehicles, precursors of lipids and sugars biosynthesis, source of methylation, mediators of cell signalling and neurotransmission. Nucleoside and nucleotide metabolism, and therefore purine metabolism enzymes are an important area of research in cell biology and in health science.
For the Drug Discovery industry, purine metabolism represents a rich source of validated or high-potential targets in Oncology, Infectiology and Immunology. The impact of drugs on nucleotides metabolism is a major concern for these therapeutic fields. NOVOCIB has developed a unique range of recombinant enzymes of purine and pyrimidine metabolism. Highly pure and active, the enzymes are provided in stable lyophilized form that does not require dry ice during transport.

IMPDH - Inosine Monophosphate Dehydrogenase (EC 1.1.1.205)

Synonyms: inosine 5'-monophosphate dehydrogenase, type 2, IMP dehydrogenase, type II, IMPDH2

Inosine Monophosphate Dehydrogenase (IMPDH) converts inosine 5’-monophosphate (IMP) to xanthosine 5’- monophosphate (XMP) using NAD+ as a cofactor. This step is crucial for guanosine biosynthesis and to feed the pool of guanine nucleotides. 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.
Recombinant Bacterial IMPDH from Staphylococcus aureus is also available either to assess the specificity of Human IMPDH inhibitors or to screen compounds that inhibit bacterial IMPDH, which is a recognized target for the development of new antibiotics.

Know more about NovoCIB's IMPDH enzymes


PNP - Purine Nucleoside Phosphorylase (EC 2.4.2.1)

PNP catalyzes the cleavage of the glycosidic bond of ribo- or deoxyribonucleosides to generate purine base and ribose- or deoxyribose-1-phosphate. The reaction is reversible for natural substrates.
A target: PNP inhibitors are investigated for chemotherapeutic applications in T-cell leukemia and T-cell-mediated autoimmune disorders, such as SLE and RA. Several PNP inhibitors have been developed to treat cancer, viral infection and auto-immune diseases.
A drug-deactivating enzyme: PNP's cleaving activity can also be responsible for the deactivation of Nucleoside Analogues. Their resistance to human PNP can be investigated in vitro to better evaluate the efficacy of the drugs.
Besides its two pharmacological properties, PNP can also be a powerful tool for drug chemistry of nucleoside analogues. Due to its reversible cleaving activity, PNP can help to considerably increase the yield of transribosylation reactions and circumvent synthesis difficulties.
Know more about NovoCIB's PNP enzyme


XDH - Xanthine Dehydrogenase (EC 1.17.1.4)

NOVOCIB's XDH is a native lyophilized enzyme extracted from bovine milk by solvent extraction and affinity purification procedures.
XDH catalyzes the formation of uric acid from hypoxanthine and xanthine, last two steps of purine catabolism.
NOVOCIB's xanthine dehydrogenase enzyme is purified under conditions that preserved the activity of the enzyme so its capacity to reduce NAD as a result of hypoxanthine/xanthine oxidation.

Know more about NovoCIB's XDH enzyme


HGPRT - Hypoxanthine-guanine phosphoribosyltransferase (EC 2.4.2.8)

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Synonyms: hypoxanthine phosphoribosyltransferase (HPRT)

NOVOCIB's human HGPRT is a recombinant protein of 25kDa cloned by RT-PCR amplification of mRNA extracted from human hepatoma cells and expressed in E.coli. The sequence of the cloned HGPRT (accession number P00492) was confirmed by DNA sequencing (100% identity).
HGPRT is a purine salvage enzyme that catalyzes the reversible transfer of the 5-phosphoribosyl group between α-D-5-phosphoribosyl-1-pyrophosphate (PRPP) and a purine base (hypoxanthine or guanine) to form a purine nucleotide IMP or GMP. The reaction is reversible but forward reaction (nucleotide formation) is heavily favoured.
Know more about NovoCIB's HGPRT enzyme


Related Links
HPRT Assay Kit
PRRP Assay Kit
Purine Metabolism Disorders
Continuous Phosphatase Assay Kit

Other enzymes and related services are continuously under development at NOVOCIB. Please, do not hesitate to visit us regularly or to contact us.