Effect of ligands on Drosophila phosphorylase a as monitored by its enzymic inactivation |
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| Authors: | V Dombrádi P Friedrich G Bot |
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| Institution: | 1. Institute of Medical Chemistry, University School of Medicine, H-4026 Debrecen, Bem Place 18/B, Hungary;2. Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H-1502, Budapest, P.O. Box 7, Hungary;1. College of Life Science, Northwest A&F University, Yangling, Shaanxi 712100, China;2. College of Natural Resources and Environment, Northwest A&F University, Yangling, Shaanxi 712100, China;3. College of Mechanical and Electronic Engineering, Northwest A&F University, Yangling, Shaanxi 712100, China;4. Northwest Research Center of Rural Renewable Energy, Exploitation and Utilization of Ministry of Agriculture, Northwest A&F University, Yangling, Shaanxi 712100, China;5. PowerChina Northwest Engineering Corporation Limited, Xi’an, Shaanxi 710065, China;1. National Center for Soybean Biotechnology and Division of Plant Sciences, University of Missouri, Columbia, MO 65211, USA;2. School of Human and Life Sciences, Canterbury Christ Church University, Canterbury, CT1 1QU, United Kingdom;1. Physiology of Plant Metabolism, Institute for Biosciences, University of Rostock, Albert-Einstein-Str. 3, 18059 Rostock, Germany;2. Plant Evolutionary Cell Biology, Faculty of Biology, Ludwig-Maximilians-Universität München, 82152 Planegg-Martinsried, Germany;3. Institute of Biology/Plant Physiology, Humboldt-Universität zu Berlin, Philippstr. 13, 10115 Berlin, Germany;4. Plant Cell and Molecular Biology, Institute of Biology, Humboldt-Universität zu Berlin, Philippstr. 13, 10115 Berlin, Germany;5. Molecular Biotechnology and Systems Biology, TU Kaiserslautern, Kaiserslautern, Germany;6. Plant Molecular Biology (Botany), Faculty of Biology, Ludwig-Maximilians-Universität München, 82152 Planegg-Martinsried, Germany;1. The First Affiliated Hospital of Xi''an Jiaotong University, 277 Yanta West Road, Xi''an, Shaanxi, 710061, China;2. Schepens Eye Research Institute/Massachusetts Eye and Ear, Harvard University School of Medicine, 20 Staniford Street, Boston, MA, 02114, USA;3. The Second Xiangya Hospital of Central South University, 139 Middle Renmin Road, Changsha, Hunan, 410011, China;1. University of Rostock, Institute for Biosciences, Physiology of Plant Metabolism, Albert-Einstein-Strasse 3, 18059 Rostock, Germany;2. Humboldt-Universität zu Berlin, Institute of Biology, Physiology of Plant Cell Organelles, Philippstrasse 13, 10115 Berlin, Germany;3. Ludwig-Maximilians-Universität München, Faculty of Biology, Plant Evolutionary Cell Biology, 82152 Planegg-Martinsried, Germany |
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| Abstract: | The dephosphorylation of Drosophila phosphorylase a with the catalytic subunit of fruit-fly protein phosphatase-1 was inhibited by AMP, IMP, ADP, ATP, glucose-6-P, glucose-1-P and UDPG. Glucose, caffeine and glycogen did not influence the reaction. The inhibitory effect of AMP was reduced by glucose and caffeine. The above ligands acted through the modification of phosphorylase a conformation. This conclusion was drawn from the ligands' effect on the dephosphorylation of phosphohistone by Drosophila phosphatase-1 and on the tryptic digestion of fruit-fly phosphorylase a. |
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