Inactivation of maize leaf phosphoenolpyruvate carboxylase by the binding to chloroplast membranes |
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Authors: | Wu M X Wedding R T |
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Institution: | Department of Biochemistry, University of California, Riverside, California 92521. |
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Abstract: | Phosphoenolpyruvate carboxylase (PEPC) purified from maize (Zea mays L.) leaves associates with maize leaf chloroplast membrane in vitro. The binding of PEPC to the membrane results in enzyme inactivation. A protein isolated from a maize leaf chloroplast membrane preparation inactivated PEPC. Treatment with membrane preparation or with partially purified inactivating protein accelerates PEPC inactivation at low temperature (4°C). Interaction of PEPC with chloroplast membrane or inactivating protein may inactivate the enzyme by influencing dissociation of the enzyme active tetramer. |
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