Rat liver protoporphyrinogen IX oxidase: site of synthesis and factor influencing its activity.
Rat liver protoporphyrinogen IX oxidase is not formed in mitochondria in contrast to the claims made for the yeast enzyme (Poulson and Polglase, FEBS Lett. (1974) 40, 258). Inhibition of mitochondrial protein synthesis in regenerating rat livers by thiamphenicol led, instead, to a slight increase in protoporphyrinogen oxidase activity. Protoporphyrinogen IX oxidase was not induced in rat liver by triiodothyronine, an inducer of mitochondrial protein synthesis, or by AIA, an inducer of heme synthesis. Significant increases in activity were observed to be associated with rapidly growing cells, such as regenerating livers and rat ascites hepatoma cells.
D000502:Allylisopropylacetamide / Q000494:pharmacology; D000818:Animals; D003576:Electron Transport Complex IV / Q000378:metabolism; D004790:Enzyme Induction; D008099:Liver / Q000201:enzymology*; D008115:Liver Regeneration; D008930:Mitochondria, Liver / Q000201:enzymology; D010088:Oxidoreductases / Q000096:biosynthesis*; D044925:Oxidoreductases Acting on CH-CH Group Donors; D050768:Protoporphyrinogen Oxidase; D051381:Rats; D013839:Thiamphenicol / Q000494:pharmacology; D014284:Triiodothyronine / Q000494:pharmacology
D014284:Triiodothyronine; D000502:Allylisopropylacetamide; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; D050768:Protoporphyrinogen Oxidase; D003576:Electron Transport Complex IV; D013839:Thiamphenicol