title: Inhibition by hydroxymalonate of malate dependent biosynthesis of progesterone in the mitochondrial fraction of human term placenta.
abstract: It has been shown that the conversion of cholesterol to progesterone by human term placental mitochondria incubated in the presence of malate or fumarate was inhibited by hydroxymalonate--an inhibitor of malic enzyme. No inhibition was observed when mitochondria were incubated in the presence of citrate or isocitrate. The degree of inhibition by hydroxymalonate of partly purified NAD(P)-linked malic enzyme activity was identical to that of both malate dependent pyruvate and progesterone formation by intact mitochondria. These data strongly support a previous suggestion that malic enzyme plays an important role in the malate dependent progesterone biosynthesis by human placental mitochondria.
mesh_terms: D002784:Cholesterol / Q000378:metabolism; D005260:Female; D006801:Humans; D008291:Malate Dehydrogenase / Q000037:antagonists & inhibitors; D008293:Malates / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D010920:Placenta / Q000378:metabolism*; D011374:Progesterone / Q000096:biosynthesis*; D013646:Tartronates / Q000494:pharmacology
chemical_list: D008293:Malates; D013646:Tartronates; D009243:NAD; C032973:tartronic acid; D011374:Progesterone; D009249:NADP; C030298:malic acid; D002784:Cholesterol; D008291:Malate Dehydrogenase