Early studies of purified rat liver enzyme by Forman and Kennedy suggested the presence of flavin mononucleotide and iron-sulfur complexes as cofactors. More recent work by Bader, Beuneu, and their colleagues with recombinant human protein expressed in insect cells has confirmed the presence of flavin mononucleotide, at a stoichiometry of one molecule per molecule of apoenzyme but suggests that iron-sulfur complexes, if indeed they are involved in the oxidation and electron transport process, are not an integral part of the dihydroorotate dehydrogenase holoenzyme.
Beuneu, C, Auger, R, Löffler, M, Lepoivre, M, Guissani, A, Lemaire, G
Knecht, W, Fries, M, Bader, B, Löffler, M
Forman, JH, Kennedy, J
Jones, ME
Kornberg, A, Lieberman, I
dihydroorotate dehydrogenase activity of DHODH:FMN [mitochondrial inner membrane]
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