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Light/dark modulation of phosphoenolpyruvate carboxylase in C3 and C 4 species
1Department of Botany, Washington State University, 99164-4238, Pullman, WA, USA.
Abstract:
In this report, the effects of light on the activity and allosteric properties of phosphoenolpyruvate (PEP) carboxylase were examined in newly matured leaves of several C3 and C4 species. Illumination of previously darkened leaves increased the enzyme activity 1.1 to 1.3 fold in C3 species and 1.4 to 2.3 fold in C4 species, when assayed under suboptimal conditions (pH 7) without allosteric effectors. The sensitivities of PEP carboxylase to the allosteric effectors malate and glucose-6-phosphate were markedly different between C3 and C4 species. In the presence of 5 mM malate, the activity of the enzyme extracted from illuminated leaves was 3 to 10 fold higher than that from darkened leaves in C4 species due to reduced malate inhibition of the enzyme from illuminated leaves, whereas it increased only slightly in C3 species. The Ki(malate) for the enzyme increased about 3 fold by illumination in C4 species, but increased only slightly in C3 species. Also, the addition of the positive effector glucose-6-phosphate provided much greater protection against malate inhibition of the enzyme from C4 species than C3 species. Feeding nitrate to excised leaves of nitrogen deficient plants enhanced the degree of light activation of PEP carboxylase in the C4 species maize, but had little or no effect in the C3 species wheat. These results suggest that post-translational modification by light affects the activity and allosteric properties of PEP carboxylase to a much greater extend in C4 than in C3 species.
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