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- W2054847669 abstract "Abstract 1. 1. Phosphoenolpyruvate carboxykinase was found to be almost equally distributed between the mitochondrial and cytosol fractions of monkey liver. The two forms of the enzyme were partially purified and characterized. 2. 2. For the carboxylation reaction the mitochondrial and cytosol enzymes had similar pH optima (7.0 and 6.8, respectively), whereas for the decarboxylation reaction the cytosol enzyme had a broader pH optimum (7.0–8.0) than the mitochondrial form (7.0–7.2). 3. 3. When assayed in either direction, both enzymes were more active with MnCl2 than with MgCl2, although the activity with MgCl2, relative to that with MnCl2, was lower for the cytosol enzyme than for the mitochondrial form. 4. 4. The mitochondrial and cytosol enzymes had similar Michaelis constants for phosphoenolpyruvate (0.15 and 0.14 mM), NaHCO3 (12.5 and 9.7 mM) or CO2 (2.5 and 1.9 mM), oxaloacetate (0.022 and 0.027 mM) and GTP (0.13 and 0.16mM). The Michaelis constants of the cytosol enzyme for IDP (0.29 mM), GDP (0.033 mM) and ITP (1.1 mM) were somewhat higher than those of the mitochondrial enzyme (0.12, 0.014 and 0.32 mM, respectively). 5. 5. In the decarboxylation direction, the two enzymes showed differences with respect to inhibition by IDP, GDP, quinolinic acid and hydrazine sulphate. 6. 6. Both enzymes had mol. wts of the order 66,000." @default.
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- W2054847669 date "1978-01-01" @default.
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- W2054847669 title "Kinetic studies on phosphoenolpyruvate carboxykinase purified from the mitochondrial and cytosol fractions of monkey liver" @default.
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- W2054847669 doi "https://doi.org/10.1016/0020-711x(78)90150-7" @default.
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