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Purine and Pyrimidine Metabolism in Man VIII pp 155–160Cite as

Inosine 5’-Monophosphate Dehydrogenase as a Chemotherapeutic Target

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 370))

Abstract

Inosine 5’-monophosphate, EC 1.1.1.205 (IMPDH) catalyzes the conversion of IMP to XMP utilizing NAD as a proton acceptor. Its role in catalyzing the rate determining step in the biosynthesis of GTP1 gives IMPDH a position of central importance in cellular activity because of the myriad activities of GTP in biosynthesis and cellular regulation. The activity of IMPDH is much higher in proliferating tissues, both normal and malignant 2, 3 suggesting that the salvage of guanine by hypoxanthine-guanine phosphoribosyltransferase is probably inadequate to satisfy the requirements of dividing cells for guanine nucleotides.

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Author information

Authors and Affiliations

  1. Cancer Research Department, Zeneca Pharmaceuticals, Alderley Park, Macclesfield, SK104TG, England

    Trevor J. Franklin & Philip Hedge

  2. Department of Cell and Structural Biology, University of Manchester, Oxford Rd., Manchester, M13 9PT, England

    Gwynneth Edwards

Authors
  1. Trevor J. Franklin
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  2. Gwynneth Edwards
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  3. Philip Hedge
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Editor information

Editors and Affiliations

  1. Indiana University School of Medicine, Indianapolis, Indiana, USA

    Amrik Sahota

  2. Indiana University, Bloomington, Indiana, USA

    Milton W. Taylor

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Franklin, T.J., Edwards, G., Hedge, P. (1995). Inosine 5’-Monophosphate Dehydrogenase as a Chemotherapeutic Target. In: Sahota, A., Taylor, M.W. (eds) Purine and Pyrimidine Metabolism in Man VIII. Advances in Experimental Medicine and Biology, vol 370. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2584-4_35

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  • DOI: https://doi.org/10.1007/978-1-4615-2584-4_35

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-6105-3

  • Online ISBN: 978-1-4615-2584-4

  • eBook Packages: Springer Book Archive

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