(E.C.1.1.1.205) * Pricing updated September 10th, 2011. Prices are subject to change without notice. Shipping charges are not included. ** One unit of IMPDH converts 1.0 µmole of IMP and NAD to XMP and NADH per minute at pH 8 at 37°C. Specific Activity: ≥ 0.3 U/mg protein. For other size, please contact us Click to order or to get further information |
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Synonyms: inosine 5'-monophosphate dehydrogenase, IMP dehydrogenase
NOVOCIB's bacterial IMPDH is a recombinant protein of ca. 53kDa cloned by PCR amplification of guaB gene of Staphylococcus aureus and expressed in E. coli.
Today, antibiotic resistance is one of the world’s most important public health problems. There is an urgent need for new antibiotic compounds acting on new targets. One attractive strategy for developing new antibiotics consists in inhibiting bacterial IMPDH, an enzyme involved in the de novo synthesis of purine nucleotides, and therefore, necessary for bacterial cell growth and division.
Mammalian and bacterial IMPDHs are known to have significantly different kinetic properties and inhibitor sensitivities(1,2). The experiments done with previously cloned human IMPDH2 and bacterial IMPDH of Staphylococcus aureus, are illustrated below. In agreement with published data, mycophenolic acid (MPA) inhibits human IMPDH type II >20-times more efficiently than bacterial IMPDH with IC50 values of 100nM and 2.6µM, respectively (A). In contrast, mizoribine monophosphate displays the opposite selectivity (B). It is a more potent inhibitor of bacterial IMPDH with respective IC50 values of 12nM and 185nM for bacterial and human enzymes.
Bacterial recombinant IMPDH and human recombinant IMPDH, Type 2, enzymes are useful tools for selection of species-specific IMPDH inhibitors. Both enzymes are available at NOVOCIB.
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Today, antibiotic resistance is one of the world’s most important public health problems. There is an urgent need for new antibiotic compounds acting on new targets. One attractive strategy for developing new antibiotics consists in inhibiting bacterial IMPDH, an enzyme involved in the de novo synthesis of purine nucleotides, and therefore, necessary for bacterial cell growth and division.
Mammalian and bacterial IMPDHs are known to have significantly different kinetic properties and inhibitor sensitivities(1,2). The experiments done with previously cloned human IMPDH2 and bacterial IMPDH of Staphylococcus aureus, are illustrated below. In agreement with published data, mycophenolic acid (MPA) inhibits human IMPDH type II >20-times more efficiently than bacterial IMPDH with IC50 values of 100nM and 2.6µM, respectively (A). In contrast, mizoribine monophosphate displays the opposite selectivity (B). It is a more potent inhibitor of bacterial IMPDH with respective IC50 values of 12nM and 185nM for bacterial and human enzymes.
Bacterial recombinant IMPDH and human recombinant IMPDH, Type 2, enzymes are useful tools for selection of species-specific IMPDH inhibitors. Both enzymes are available at NOVOCIB.
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IMPDH inhibition: Effect of MPA (A) and mizoribine monophosphate (B) on human recombinant IMPDH II (red curve) and bacterial recombinant IMPDH of Staphylococcus aureus (blue curve). Enzymatic assays are performed in duplicate at 37°C in 0.1M KH2PO4 buffer pH 8.0 in the presence of 1mM DTT, 200µM NAD, 200µM IMP, 60nM Human IMPDH, Type 2 or 95nM IMPDH S.aureus. Reaction is followed in an iEMS Reader MF (Labsystems) microtiter plate reader at 340nm.
Monophosphorylated mizoribine is produced enzymatically by phosphorylation of mizoribine (MP Biochemicals) using NOVOCIB's adenosine kinase (AK). |
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| Unit Definition: One unit of IMPDH converts 1.0 µmole of IMP and NAD to XMP and NADH per minute at pH 8 at 37°C. Specific Activity: ≥ 0.3 unit/mg protein. Purity: controlled by 12%AA SDS-PAGE. | |
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Download this document "NovoCIB's Bacterial Recombinant IMPDH"
See also our brochure "NovoCIB IMPDH Products & Services"
| Related Links | |
| • Purine Metabolism Enzymes
• Human Recombinant IMPDH • IMPDH Screening Assay Kit |
• Nucleoside Kinase Assay Kits
• HPRT Assay • PRPP Assay |




