Fumarate reductase in the control of heme biosynthesis.
A drug-induced stimulation of heme biosynthesis in mouse liver was accompanied by altered fumarate metabolism. In liver homogenate, fumarate 1,4-C(14) was incorporated, via succinate and succinyl coenzyme A, into heme at an accelerated rate. This pathway of fumarate utilization was inhibited by acetoacetate but not by beta-hydroxybutyrate. Fumarate reduction to succinate required reduced nicotinamide adenine dinucleotide. The enzyme fumarate reductase is suggested as a link between terminal oxidation and cellular control of the heme biosynthetic pathway.
D000090:Acetoacetates / Q000494:pharmacology; D000818:Animals; D001669:Biochemical Phenomena; D001671:Biochemistry; D002247:Carbon Isotopes; D003065:Coenzyme A; D005650:Fumarates / Q000378:metabolism*; D006418:Heme / Q000096:biosynthesis*; D006885:Hydroxybutyrates / Q000494:pharmacology; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology*; D051379:Mice; D009243:NAD; D010088:Oxidoreductases; D011874:Radiometry; D013347:Subcellular Fractions; D013386:Succinates / Q000096:biosynthesis
D000090:Acetoacetates; D002247:Carbon Isotopes; D005650:Fumarates; D006885:Hydroxybutyrates; D013386:Succinates; D009243:NAD; D006418:Heme; D010088:Oxidoreductases; D003065:Coenzyme A