Structural requirements for allosteric activators of rat liver microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase.

Several compounds containing various structural moieties of NAD(P)(H), were examined as possible effectors of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase activity. Microsomal reductase was activated with 4.5mM GSH, assayed with subsaturating NADPH concentration and increasing amounts of the tested compounds. Under these conditions, the essential and sufficient structure required to allosterically enhance the activity of the reductase is that of 5'-AMP. When the 2' position of the nucleotide is phosphorylated, this allosteric activation is diminished.