The Fourth Molybdenum Containing Enzyme mARC: Cloning and Involvement in the Activation ofN-Hydroxylated Prodrugs
Journal of Medicinal Chemistry2008Vol. 51(24), pp. 8173–8177
Citations Over TimeTop 10% of 2008 papers
Sanja Gruenewald, Bettina Wahl, Florian Bittner, Helen Hungeling, Stephanie Kanzow, Joscha Kotthaus, Ulrike Schwering, Ralf R. Mendel, Bernd Clement
Abstract
The recently discovered mammalian molybdoprotein mARC1 is capable of reducing N-hydroxylated compounds. Upon reconstitution with cytochrome b(5) and b(5) reductase, benzamidoxime, pentamidine, and diminazene amidoximes, N-hydroxymelagatran, guanoxabenz, and N-hydroxydebrisoquine are efficiently reduced. These substances are amidoxime/N-hydroxyguanidine prodrugs, leading to improved bioavailability compared to the active amidines/guanidines. Thus, the recombinant enzyme allows prediction about in vivo reduction of N-hydroxylated prodrugs. Furthermore, the prodrug principle is not dependent on cytochrome P450 enzymes.
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