Strom K A, Galeos W L, Davidson L A, Kumar S
J Biol Chem. 1979 Sep 10;254(17):8153-8.
The NADPH-dependent enoyl coenzyme A reductase activity of bovine mammary fatty acid synthetase has been characterized with regard to substrate specificity and the product formed. A relatively high specificity for an unsubstituted, four-carbon, 2,3-enoyl chain in trans configuration is obtained. Reduction of trans-crotonyl-CoA results in butyrate, 50% of which is coenzyme A-bound. The reaction is subject to product inhibition, specifically by butyryl-CoA and NADP. Free coenzyme A, on the other hand, is an activator. The pH profile, susceptibility to inhibition by -SH reagents, the results of the relative activities obtained with substrate analogues and homologues, and the ready use of crotonyl-CoA as a primer in fatty acid synthesis are consistent with a mechanism in which the crotonyl group is transferred to an -SH group, is reduced, and then is either transferred back to CoA or hydrolyzed.
已对牛乳腺脂肪酸合成酶的烟酰胺腺嘌呤二核苷酸磷酸（NADPH）依赖性烯酰辅酶A还原酶活性在底物特异性和所形成产物方面进行了表征。对于反式构型的未取代四碳2,3 - 烯酰链具有相对较高的特异性。反式巴豆酰辅酶A的还原产生丁酸盐，其中50%与辅酶A结合。该反应受到产物抑制，特别是被丁酰辅酶A和NADP抑制。另一方面，游离辅酶A是一种激活剂。pH曲线、对 -SH试剂抑制的敏感性、用底物类似物和同系物获得的相对活性结果，以及巴豆酰辅酶A作为脂肪酸合成起始物的现成用途，都与一种机制相符，即巴豆酰基转移到一个 -SH基团上，被还原，然后要么再转移回辅酶A，要么被水解。
