Abstract

Mevalonate-activating enzymes from chick brain and liver were stable when 105,000 x g supernatants were stored at -4 degrees C for 168 h. Mevalonate kinase and mevalonate 5-phosphate kinase retained their activities for 72 h at 4 degrees C while mevalonate 5-pyrophosphate decarboxylase activity significantly decreased after 24-48 h of storage at 4 degrees C. Direct addition of 2.5 mM phenylpyruvate to the reaction mixture produced a significant inhibition of decarboxylase activity in brain and liver. When enzyme preparations were preincubated with 2.5 mM phenylpyruvate for 20 min before the addition of substrate, an increased inhibition was observed. Mevalonate kinase and mevalonate 5-phosphate kinase from both tissues were not affected in the same conditions. The inhibition of brain and liver decarboxylase was progressive with increasing concentrations (2.5-10.0 mM) of phenylpyruvate. No significant difference was observed in the inhibition of decarboxylase after 10 or 20 min of preincubation.

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