Changes in catalytic activity and association state of pyruvate carboxylase which are dependent on enzyme concentration

Paul Attwood, M.A. Geeves

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The specific activity of chicken liver pyruvate carboxylase has been shown to decrease with decreasing enzyme concentration, even at 100 muM, which is close to the estimated physiological concentration. The kinetics of the loss of enzyme specific activity following dilution were biphasic. Incubation of dilution-inactivated enzyme with ATP, acetyl CoA, Mg2+ + ATP or, to a lesser degree, with Mg2+ alone resulted in a high degree of reactivation, while no reactivation occurred in the presence of pyruvate. The association state of the enzyme before, during, and after dilution inactivation has been assessed by gel filtration chromatography. These studies indicate that on dilution, there is dissociation of the catalytically active tetrameric enzyme species into inactive dimers. Reactivation of the enzyme resulted in reassociation of enzymic dimers into tetramers. The enzyme was shown to form high molecular weight aggregates at high enzyme concentrations. (C) 2002 Elsevier Science (USA). All rights reserved.
Original languageEnglish
Pages (from-to)63-72
JournalArchives of Biochemistry and Biophysics
Volume401
DOIs
Publication statusPublished - 2002

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