Abstract
This chapter focuses on rat liver acetoacetyl-CoA synthetase. Acetoacetyl-CoA synthetase is a cytosolic enzyme, which is found in lipogenic tissues of the rat (and other species) including the infant brain, adult liver, adipose tissue, lactating mammary gland, and adrenal gland. The enzyme-catalyzed reaction produces acetoacetyl-CoA, the first intermediate unique to the pathway of isoprenoid biosynthesis. Its activity level is highly regulated in liver, and in many cases, changes in that level are closely coupled to changes in the activity levels of hydroxymethylglutaryl- CoA synthase and hydroxymethylglutaryl-CoA reductase. Hepatic acetoacetyl-CoA synthetase activity is depressed in starvation, by cholesterol feeding, and by mevalonic acid feeding and is enhanced by feeding drugs such as cholestyramine, gemfibrozil, and mevinolin. Its activity has a diurnal variation with the peak in the middle of the dark cycle. Thus, assaying acetoacetyl-CoA synthesis in cytosolic extracts depends upon quantitating the acetyl-CoA produced. This has been accomplished by coupling acetyl-CoA formed to oxaloacetate by the citrate synthase reaction. Oxaloacetate is formed from malate dehydrogenase, and NADH production is followed spectrophotometrically, 2,4 as we will describe later in this chapter.
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