Regulatory properties of rat liver glutamine synthetase |
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| Authors: | T F Deuel A Lerner D Albrycht |
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| Affiliation: | 1. Department of Medicine, Section of Hematology, University of Chicago Chicago, Illinois 60637 USA;2. the Argonne Cancer Research Hospital (operated by the University of Chicago for the United States Atomic Energy Commission) Chicago, Illinois 60637 USA;1. Department of Pathology, University of California San Francisco, San Francisco, CA, USA;2. Kaiser Permanente, Woodland Hills, CA, USA;1. INSERM, Sorbonne Université, Centre de Recherche des Cordeliers (CRC), Paris, F-75006, France;2. Équipe labellisée Ligue Nationale Contre le Cancer, France;1. Department of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, New York 11794, USA;2. Department of Applied Mathematics, Stony Brook University, Stony Brook, New York 11794, USA;3. Department of Pathology, Stony Brook University, Stony Brook, New York 11794, USA;4. Department of Physiology, McGill University, Montreal, QC H3G 1Y6, Canada;5. Institute of Cancer Sciences, University of Glasgow, and the CRUK Beatson Institute, Glasgow G61 1BD, UK;6. Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106, USA;7. Department of Chemistry and Lewis-Sigler Institute for Integrative Genomics, Princeton University, NJ 08544, USA;8. Department of Life Sciences, National Cheng Kung University, Tainan City 701, Taiwan |
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| Abstract: | Purified rat liver glutamine synthetase is sensitive to inhibition by glutamine and histidine when studied in a Mn2+ assay system. If Mg2+ is substituted for Mn2+, no inhibition is seen. Both glutamine and histidine are more effective inhibitors when glutamate is limiting in concentration during assay. Alpha-ketoglutarate and citrate activate or inhibit catalytic activity depending on the concentration of divalent cation present during assay, and largely appear to regulate activity by binding the divalent cation required for activity. These results suggest that direct or indirect interaction of divalent cations with enzyme, substrates, inhibitors, and activators may be of major significance in the cellular regulation of rat liver glutamine synthetase. |
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