Lippe G, Deana R, Cavallini L, Galzigna L
Biochem Pharmacol. 1985 Sep 15;34(18):3293-7. doi: 10.1016/0006-2952(85)90348-x.
The activity of the microsomal 3-hydroxy-3-methylglutaryl-coenzyme A reductase was assayed with a procedure based on the extraction of the product mevalonolactone in a benzene phase. Diamide is an uncompetitive inhibitor of the reaction, while coenzyme A disulfide and tetraethylthiouram disulfide act as non-competitive inhibitors. Diamide inhibition cooperatively increases with the inhibitor concentration. HMG produces a decrease in enzyme activity that combines with that of coenzyme A disulfide. Both CoASH and coenzyme A esters strongly inhibit the reductase activity. Three new synthetic compounds with either thio-ether or thio-ester groups also show inhibitory effect on the enzyme activity.
采用基于在苯相中提取产物甲羟戊酸内酯的方法测定微粒体3-羟基-3-甲基戊二酰辅酶A还原酶的活性。二酰胺是该反应的非竞争性抑制剂，而辅酶A二硫化物和四乙基秋兰姆二硫化物作为竞争性抑制剂。二酰胺抑制作用随抑制剂浓度协同增加。HMG使酶活性降低，这与辅酶A二硫化物的作用相结合。辅酶A和辅酶A酯均强烈抑制还原酶活性。三种具有硫醚或硫酯基团的新型合成化合物也对酶活性表现出抑制作用。
