Role of AMP deaminase reaction in the control of fructose 1,6-bisphosphatase activity in yeast |
| |
| Authors: | M Yoshino K Murakami |
| |
| Affiliation: | 1. Department of Biochemistry, Yokohama City University School of Medicine, Yokohama 232, Japan;2. Department of Laboratory Medicine, St. Marianna University School of Medicine, Kawasaki 213, Japan;1. Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan;2. Collaborative Research Institute for Innovative Microbiology, The University of Tokyo, Tokyo 113-8657, Japan;3. Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan;4. RIKEN Center for Sustainable Resource Science, Saitama 351-0198, Japan;1. Institute of Immunology and immunotherapy, School of Mathematics and Centre of Membrane Proteins and Receptors (COMPARE), University of Birmingham, Birmingham, UK;2. Department of Physics, King’s College London, London, UK;3. Institute of Microbiology and Infection and School of Biosciences, University of Birmingham, Birmingham, UK;4. School of Biosciences, Institute of Metabolism and Systems Research and Centre of Membrane Proteins and Receptors (COMPARE), University of Birmingham, Birmingham, UK;1. Center for Quantitative Biology, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, 100871, China;2. The Key Laboratory of Cell Proliferation and Differentiation of Ministry of Education, School of Life Sciences, Peking University, Beijing, 100871, China;3. Peking-Tsinghua Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, 100871, China;4. School of Physics, Peking University, Beijing, 100871, China;5. College of Life Science and Technology, Huazhong Agriculture University, Wuhan, 430070, China |
| |
| Abstract: | The physiological role of the inhibition of AMP deaminase (EC 3.5.4.6) by Pi was analyzed using permeabilized yeast cells. (a) Fructose 1,6-bisphosphatase (EC 3.1.3.11) was inhibited only a little by AMP, which was readily degraded by AMP deaminase under the in situ conditions. (b) The addition of Pi, which showed no direct effect on fructose 1,6-bisphosphatase, effectively enhanced the inhibition of the enzyme by AMP increased through the inhibition of AMP deaminase. (c) Pi activated phosphofructokinase (EC 2.7.1.11) and inhibited AMP deaminase activity. AMP deaminase reaction can act as a control system of fructose 1,6-bisphosphatase activity and gluconeogenesis/glycolysis reaction through the change in the AMP level. Pi may contribute to the stimulation of glycolysis through the inhibition of fructose 1,6-bisphosphatase by the increase in AMP in addition to the direct activation of phosphofructokinase. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
