Effect of cyclic amp on suncus murinus liver serine-aminotransferase and serine dehydratase |
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| Institution: | 1. University of Bergen, Department of Physics and Technology, Bergen, Norway;2. Western Norway University of Applied Sciences, Department of Mechanical and Marine Engineering, Bergen, Norway;3. Department of Thermal Physics, National Research Nuclear University MEPhI, Russia |
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| Abstract: | - 1.1. Suncus murinus was injected dibutyryl adenosine 3′,5′-cyclic monophosphate (Bt2cAMP) and assayed serine-glyoxylate aminotransferase (EC 2.6.1.45) and serine dehydratase (EC 4.2.1.13).
- 2.2. Serine dehydratase was induced 4-fold by Bt2cAMP. The Km values of the induced enzyme for l-serine and pyridoxal 5′-phosphate was 57 mM and 3.0 μM, respectively. The enzyme had a pH optimum at pH 10.0. These kinetic properties and pH optimum were same as those of the enzyme from the control. Both the holoenzyme and the apoenzyme increased to the same extent by Bt2cAMP.
- 3.3. Serine-glyoxyate aminotransferase activity was decreased slightly by the Bt2cAMP injection. The holoenzyme activity was increased, but the apoenzyme decreased. Km values for l-serine and glyoxylate of this enzyme were 6mM and 0.2 mM, respectively, without change by Bt2cAMP.
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