Regulation of rat-kidney cortex fructose-1,6-bisphosphatase activity. I. Effects of fructose-2,6-bisphosphate and divalent cations |
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| Institution: | 1. Microelectronics and Photonics Graduate Program, University of Arkansas, Fayetteville, AR, 72701, USA;2. Physics Department at the College of Science, Al Baha University, Al Baha, 65527, Saudi Arabia;3. Department of Physics at the College of Education, University of Mustansiriyah, Baghdad, 10052, Iraq;4. Department of Physics, University of Arkansas, Fayetteville, AR, 72701, USA;5. Physics Department, The University of Jordan, Amman, 11942, Jordan;1. Shannon Lab, Huawei Technologies Co., Ltd., Santa Clara, USA;2. Shannon Lab, Huawei Technologies Co., Ltd., Shenzhen, China |
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| Abstract: | - 1.1. The native rat-kidney cortex Fructose-1,6-BPase is differentially regulated by Mg2+ and Mn2+.
- 2.2. Mg2+ binding to the enzyme is hyperbolic and large concentrations of the cation are non-inhibitory.
- 3.3. Mn2+ produces a 10-fold rise in Vmax higher than Mg2+. Mn2+]0.5 is much larger than Mg2+]0.5. At elevated Mn2+] inhibition is observed.
- 4.4. Mg2+ and Mn2+ produce antagonistic effects on the inhibition of the enzyme by high substrate.
- 5.5. Fru-2,6-P2 inhibits the enzyme by rising the S0.5 and favouring a sigmoidal kinetics.
- 6.6. The inhibition by Fru-2,6-P2 is released by Mg2+ and more powerfully by Mn2+ increasing the I0.5.
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