Kinetic properties of glycogen synthase from skeletal muscle after phosphorylation by glycogen synthase kinase 4 |
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| Authors: | D F Brown M Hegazy E M Reimann |
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| Affiliation: | 1. Hamilton College, Clinton, NY 13323 USA;2. Department of Biochemistry, Medical College of Ohio, C.S. 10008, Toledo, OH 43699 USA;1. Graduate School of Biomedical Sciences, Rowan University, Stratford, NJ 08084, USA;2. School of Osteopathic Medicine, Rowan University, Stratford, NJ 08084, USA;1. Department of Chemistry, Faculty of Arts and Sciences, Sakarya University, Sakarya, Turkey;2. Department of Food Engineering, Faculty of Engineering, Istanbul Aydin University, Istanbul, Turkey;1. CiC BioGUNE, Parque Tecnológico de Bizkaia, Ed. 800, 48460, Derio, Spain;2. Pharma Biotech Development Penzberg, Roche Diagnostics GmbH, 82377, Penzberg, Germany;3. Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Veterinärstr. 13, 80539, Munich, Germany;4. Department of Biochemistry, Molecular Biology & Biophysics, University of Minnesota, Minneapolis, MN, 55455, USA;3. p53 Laboratory, Agency for Science, Technology, and Research (A*STAR), 8A Biomedical Grove, Singapore 138648, Singapore,;4. Mahidol-Oxford Tropical Medicine Research Unit, Mahidol University, Bangkok 10400, Thailand, and;5. Institute of Molecular and Cellular Biology, A*STAR, 61 Biopolis Drive, Singapore 138673, Singapore;3. From the Central European Institute of Technology and;4. Faculty of Science, National Centre for Biomolecular Research, Masaryk University, Kamenice 5, CZ-625 00 Brno, Czech Republic and;5. the Institute of Biotechnology, University of Helsinki, Viikinkaari 1 (P. O. Box 65), 00014 Helsinki, Finland;4. York Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5DD, United Kingdom;3. Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, v.v.i., Flemingovo nám 2, 166 10 Prague 6, Czech Republic |
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| Abstract: | Glycogen synthase I (EC 2.4.1.11) from rat and from rabbit skeletal muscle was phosphorylated in vitro by glycogen synthase kinase 4 (EC 2.7.1.37) to the extent of 0.8 phosphates/subunit. For both phosphorylated enzymes, the activity ratio (activity without glucose 6-P divided by activity with 8 mM glucose 6-P) was 0.8 when determined with low concentrations of glycogen synthase and/or short incubation times. However, the activity ratio was 0.5 with high enzyme concentrations and longer incubation times. It was found that the lower activity ratios result largely from UDP inhibition of activity measured in the absence of glucose 6-P. Inhibition by UDP was much less pronounced for glycogen synthase I, indicating that a major consequence of phosphorylation by glycogen synthase kinase 4 is an increased sensitivity to UDP inhibition. |
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