Higher plant NADP+-dependent isocitrate dehydrogenases,ammonium assimilation and NADPH production |
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| Affiliation: | 1. Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Nanhai Road 7, Qingdao 266071, China;2. College of Earth Sciences, University of Chinese Academy of Science, Beijing 100049, China;3. Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao 266071, China;4. Department of Biology Science, Fujian Agriculture and Forestry University, Fuzhou 35002, China;5. School of Biology & Basic Medical Sciences, Soochow University, Suzhou 215000, China;1. Department of Biology, Memorial University of Newfoundland, St. John''s, NL, A1B 3X9, Canada;2. Umeå Plant Science Centre, Department of Plant Physiology, University of Umeå, SE-901 87 Umeå, Sweden;1. Plant Proteomics, Max-Planck Institute for Plant Breeding Research, Carl-von-Linné Weg 10, 50829 Köln, Germany;2. Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany |
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| Abstract: | ![]()
The assimilation of ammonium into glutamate is mainly achieved by the GS/GOGAT pathway and requires carbon skeletons in the form of 2-oxoglutarate. To date, the exact enzymatic origin of this organic acid for plant ammonium assimilation is unknown. NADP+-dependent isocitrate dehydrogenases can carry out this function and the recent efforts concentrated on evaluating the involvement of different isoforms, distinguished by their subcellular localisation, are analysed. Furthermore, a possible role for these enzymes in the production of NADPH for redox-regulated cell metabolism, such as the recycling of glutathione required in response to oxidative stress will be discussed. |
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