Evolution of C4 Phosphoenolpyruvate Carboxylase： Enhanced Feedback Inhibitor Tolerance Is Determined by a Single Residue

作     者：Judith Katharina Paulus, Christian Niehus Georg Groth 

作者机构：Cluster of Excellence on Plant Sciences (CEPLAS) Institute of Biochemical Plant Physiology Heinrich Heine University Düsseldorf Germany 

出 版 物：《Molecular Plant》 (分子植物（英文版）)

年 卷 期：2013年第6卷第6期

页      面：1996-1999页

核心收录：

学科分类：0710[理学-生物学] 0832[工学-食品科学与工程（可授工学、农学学位）] 08[工学] 09[农学] 0901[农学-作物学] 083203[工学-农产品加工及贮藏工程] 

基　　金：supported by a grant from Deutsche Forschungsgemeinschaft through graduate program IRTG 1525 iGRAD-Plant 

主　　题：Phosphoenolpyruvate carboxylase (PEPC) Inhibitor 

摘      要：Dear Editor, Phosphoenolpyruvate carboxylase （PEPC） is the essential enzyme for initial carbon fixation in C4 photosynthesis. The C4-PEPC evolved from a non-photosynthetic C3 ancestor by subtle sequence changes resulting in distinctly different kinetic and regulatory characteristics （Svensson et al., 1997）. Malate and aspartate, which are formed from the carboxyla- tion product of PEPC, serve as feedback inhibitors of the PEPC （Wedding et al., 1990）. Higher malate or aspartate concen- trations during C4 photosynthesis require a reduced sensitiv- ity towards the feedback inhibitors of the C4-PEPC （Jacobs et al., 2008）.