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The role of oligomerization in regulation of maize phosphoenolpyruvate carboxylase activity. Influence of Mg-PEP and malate on the oligomeric equilibrium of PEP carboxylase



The role of oligomerization in regulation of maize phosphoenolpyruvate carboxylase activity. Influence of Mg-PEP and malate on the oligomeric equilibrium of PEP carboxylase



Biochemical and Biophysical Research Communications 168(2): 778-785



PEP carboxylase was purified to a final specific activity of 33 units/mg from leaves of 3-week-old maize plants. Size exclusion HPLC showed a single peak of PEP carboxylase migrating as a tetramer. Dynamic laser-light scattering spectroscopy showed that PEP carboxylase existed predominantly as a tetramer when incubated with 5 mM Mg-PEP but converted to a dimeric state when the substrate was replaced by 5 mM malate (a PEP carboxylase inhibitor).

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Accession: 002258523

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PMID: 2334435



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