The ATP-dependent reductive carboxylation of 2-oxoglutarate using cytosol from rat liver

An enzyme system (isocitrate synthase) catalysing the conversion of 2-oxoglutarate to isocitrate has been detected in and partially purified from rat liver. The activity of this enzyme system is dependent on the presence of Mg 2+, ATP, HCO 3 − and NADPH. The major proportion of the isocitrate syntha...

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Veröffentlicht in:	Biochemical and biophysical research communications 1976-08, Vol.71 (3), p.712-718
Hauptverfasser:	Keech, D.Bruce, Mattoo, Autar K., Carabott, Mary J.J., Wallace, John C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - pharmacology Animals Cytosol - drug effects Cytosol - enzymology Enzyme Activation - drug effects Isocitrate Dehydrogenase - isolation & purification Isocitrate Dehydrogenase - metabolism Liver - enzymology Magnesium - pharmacology Multienzyme Complexes - metabolism NAD Rats
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Beschreibung
Zusammenfassung:	An enzyme system (isocitrate synthase) catalysing the conversion of 2-oxoglutarate to isocitrate has been detected in and partially purified from rat liver. The activity of this enzyme system is dependent on the presence of Mg 2+, ATP, HCO 3 − and NADPH. The major proportion of the isocitrate synthase was found in the cytosol and its level of activity was related to the nutritional state of the animal, undergoing changes parallel to those observed in the rate of lipogenesis. During purification, the activity of the isocitrate synthase system increased relative to that of isocitrate dehydrogenase (NADP +).
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(76)90889-5