Abstract
An enzymic activity which competes with 3-hydroxy-3-methylglutaryl coenzyme A reductase for d-hydroxymethylglutaryl CoA has been found in isolated rat liver microsomes and in microsomal extracts. The presence of this activity in enzyme preparations causes a decrease in the rate of mevalonate formation leading to an underestimation of reductaae activity and an overestimation of the apparent K m of the reductase. The product formed by this competing enzymic activity behaves similarly to, but not identically with, mevalonolactone when chromatographed on Bio-Rad AG l-x8 formate, which is used in many reductase assay procedures to separate mevalonolactone from hydroxymethylglutaryl CoA. Removal of this competing enzymic activity from reductase preparations can be accomplished by gel filtration using Bio-Gel A 1.5m, by washing the microsomes or by incubating the microsomal extract at 37°C. Using enzyme preparations free of this competing enzymic activity, the apparent K m values of the reductase for d-hydroxymethylglutaryl CoA and NADPH were found to be 1.3 and 26 μM respectively.
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