Activation and inactivation of phosphoenolpyruvate carboxykinase by ferrous ions.
Phosphoenolpyruvate carboxykinase from rat liver cytosol is activated by Fe2+ ions in either direction of catalysis. Preincubation of the purified enzyme with Fe2+ ions causes a time-dependent irreversible loss of activity; this is not seen with unpurified enzyme. Purified enzyme can be protected from inactivation by Fe2+ ions by partially purified protein fractions from liver (ferroactivator fractions). The possible role of ferroactivator and Fe2+ ions in regulating phosphoenolpyruvate carboxykinase is discussed.
D000818:Animals; D002413:Cations, Divalent / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D005296:Ferrous Compounds / Q000494:pharmacology*; D007501:Iron / Q000494:pharmacology*; D008099:Liver / Q000201:enzymology*; D010710:Phosphates / Q000494:pharmacology; D010729:Phosphoenolpyruvate Carboxykinase (GTP) / Q000037:antagonists & inhibitors / Q000378:metabolism*; D051381:Rats
D002413:Cations, Divalent; D005296:Ferrous Compounds; D010710:Phosphates; D007501:Iron; D010729:Phosphoenolpyruvate Carboxykinase (GTP)