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Long-term regulation of pyruvate dehydrogenase complex. Evidence that kinase-activator protein (KAP) is free pyruvate
1Department of Biochemistry and Genetics, Medical School, University of Newcastle upon Tyne, U.K.
The Biochemical Journal
|May 1, 1991
Abstract:
The kinase-activator protein (KAP) of pyruvate dehydrogenase complex (PDC) has been purified approx. 2250-fold from high-speed supernatants of mitochondrial extracts from the liver of 48 h-starved rats. Purified KAP demonstrates kinase activity towards both the E1 component of PDC and towards a synthetic peptide corresponding to the major phosphorylation site on E1. Furthermore, the activities of KAP and PDC kinase co-fractionate through several stages of purification and have the same apparent mass. We conclude that KAP is not a distinct protein, but is kinase which has dissociated from the complex.