Department of Biochemistry, University of California, Riverside, California 92521.
Plant Physiol. 1992 Sep;100(1):382-7. doi: 10.1104/pp.100.1.382.
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 degrees C). Interaction of PEPC with chloroplast membrane or inactivating protein may inactivate the enzyme by influencing dissociation of the enzyme active tetramer.
磷酸烯醇式丙酮酸羧化酶（PEPC）从玉米（Zea mays L.）叶片中纯化出来，在体外与玉米叶片叶绿体膜结合。PEPC 与膜的结合导致酶失活。从玉米叶绿体膜制剂中分离出一种蛋白质，可使 PEPC 失活。用膜制剂或部分纯化的失活蛋白处理可在低温（4°C）下加速 PEPC 的失活。PEPC 与叶绿体膜或失活蛋白的相互作用可能通过影响酶活性四聚体的解离而使酶失活。
