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Inhibition and Localization of Human and Rat Dihydroorotate Dehydrogenase

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Purine and Pyrimidine Metabolism in Man X

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 486))

Conclusion

Inhibitors of mammalian DHODH display a variety of inhibition mechanisms and often show a significant species specific efficacy (Table 1). Increasing information about the topochemistry and protein structure of DHODH suggests that the inner-membrane and membrane-associated N-terminal domains of the enzyme, which also distinguish mammalian DHODH from their prokaryotic counterparts14, play a major role in the binding, specificity and efficacy of DHODH inhibitors.

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References

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Knecht, W., Loffler, M. (2002). Inhibition and Localization of Human and Rat Dihydroorotate Dehydrogenase. In: Zoref-Shani, E., Sperling, O. (eds) Purine and Pyrimidine Metabolism in Man X. Advances in Experimental Medicine and Biology, vol 486. Springer, Boston, MA. https://doi.org/10.1007/0-306-46843-3_52

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  • DOI: https://doi.org/10.1007/0-306-46843-3_52

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-0-306-46515-4

  • Online ISBN: 978-0-306-46843-8

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