Survey of pyruvate,phosphate dikinase activity of plants in relation to the C3, C4 and CAM mechanisms of CO2 assimilation |
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| Affiliation: | 1. Laboratory of Plant, Soil and Environment Interactions (LR21ES01, Department of Biology, Faculty of sciences of Tunis, University of Tunis El Manar (UTM), University Campus of Tunis El-Manar, 2092 Tunis, Tunisia;2. Chemical Engineering Department (DEQ), School of Industrial Engineering of Barcelona (ETSEIB), Universitat Politècnica de Catalunya (UPC), Av, Diagonal 647, 08028 Barcelona, Spain;3. Laboratory of Extremophile Plants, Centre of Biotechnology of Borj Cedria (CBBC), B.P. 901, 2050 Hammam-Lif, Tunisia;4. Research Unit “Nutrition et Métabolisme Azotés et Protéines de Stress” (UR/ES-13-29), Biology Department, Faculty of Sciences of Tunis (FST), University of Tunis El-Manar (UTM), University Campus of Tunis El-Manar, 2092 Tunis, Tunisia;5. Integrated and Urban Plant Pathology Laboratory, University of Liège, Gembloux Agro-Bio Tech, 2 passage des Déportés 5030 Gembloux, Belgium;1. Key Laboratory of Geographic Information Science (Ministry of Education), School of Geographical Sciences, East China Normal University, 500 Dongchuan Road, Shanghai 200241, China;2. State Key Laboratory of Estuarine and Coastal Research, East China Normal University, 3663 North Zhongshan Road, Shanghai 200062, China;1. Department of Botany, Bacha Khan University Charsadda KP, Pakistan;2. Department of Botany, Islamia College Peshawar, Pakistan;3. Key Laboratory of Resource Biology and Biotechnology in Western China, Ministry of Education, College of Life Sciences, Northwest University, Xi''an 710069, China;4. College of Life science, Northwest University, Xi''an 710069, China;5. Institute of Grassland Science, Key Laboratory of Vegetation Ecology, Northeast Normal University, Changchun, Jilin, China |
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| Abstract: | The pyruvate, phosphate dikinase activity (PPD, EC 2.7.9.1) associated with crude extracts of leaf tissue of some C3 and C4 plants was determined by phosphoenolpyruvate plus PPi-dependent phosphorylation of AMP. The PPD activity of all C4 plants examined was > 15 nmol/mg protein/min. Several factors contributed to the underestimation of PPD activity in crude extracts of at least some species. Significant PPD activity (> 0.15 nmol/mg protein/min) was not detected in the majority of C3 species but several C3 species and the two CAM species studied exhibited activity in the range 0.4–4 nmol/mg protein/min while the C3 species Avena sativa showed activity up to 8 nmol/mg protein/min. The oat leaf enzyme was partially purified; it exhibited properties similar to those of partially purified PPD from maize. Leaf extracts of the orchids Cymbidium canaliculatum and C. madidum contained high levels of PPD activity similar to the majority of C4 plants. PPD activity has also been shown in other previously unstudied species. |
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