Abstract
Neurospora fructose-1,6-diphosphate aldolase exhibited a hyperbolic substrate saturation curve which changed to sigmoidal in the presence of 0.5 mM sodium pyruvate. The S 0.5 value for fructose-1,6-diphosphate increased from 1.4 mM to 6.6 and 20 mM in the presence of 0.5 and 1.0 mM sodium pyruvate, respectively. The inhibition seems to be cooperative in nature and involves conformational changes. Potassium ions completely blocked the inhibition by sodium pyruvate.
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