Inosine Monophosphate Dehydrogenase
Krzysztof W. Pankiewicz, Barry Goldstein
Abstract
Krzysztof W. Pankiewicz, Barry Goldstein
Abstract
Inosine 5'-monophosphate dehydrogenase (IMPDH, E.C.1.1.1.205), the NADdependent enzyme that controls de novo synthesis of purine nucleotides, catalyzes the oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5'-monophosphate (XMP), which is then converted to guanosine 5'-monophosphate (GMP) by GMP synthase (Fig.1). IMP also serves as a substrate for the biosynthesis of adenosine 5'-monophosphate (AMP). An adequate pool of purine nucleotides is essential for cell proliferation, cell signaling, and as an energy source. Consequently, inhibition of IMPDH causes a variety of biological responses, and it is not surprising that this enzyme has emerged as a major target for antiviral, antileukemic and immunosuppressive therapies.
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Inosine 5'-monophosphate dehydrogenase (IMPDH, E.C.1.1.1.205), the NADdependent enzyme that controls de novo synthesis of purine nucleotides, catalyzes the oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5'-monophosphate (XMP), which is then converted to guanosine 5'-monophosphate (GMP) by GMP synthase (Fig.1). IMP also serves as a substrate for the biosynthesis of adenosine 5'-monophosphate (AMP). An adequate pool of purine nucleotides is essential for cell proliferation, cell signaling, and as an energy source. Consequently, inhibition of IMPDH causes a variety of biological responses, and it is not surprising that this enzyme has emerged as a major target for antiviral, antileukemic and immunosuppressive therapies.
Key concepts: IMP dehydrogenase, Guanosine monophosphate, Inosine monophosphate, Inosine, Purine metabolism, Biochemistry, Nucleotide, Guanosine