Lee F T, Adams J B
Biochem Biophys Res Commun. 1987 Apr 29;144(2):569-75. doi: 10.1016/s0006-291x(87)80004-9.
Acylcoenzyme A:estradiol-17 beta acyltransferase in microsomes of bovine placenta cotyledons was strongly membrane bound. The enzyme was solubilised from microsomes by sodium cholate and was reconstituted into phospholipid vesicles. The apparent Km for estradiol-17 beta was 11 microM which was close to the value of 8 microM previously found with the membrane-bound enzyme. Testosterone was also a substrate for the reconstituted enzyme (apparent Km 62 microM) and was a competitive inhibitor (Ki 74 microM) of the acylation of estradiol-17 beta. Although various long-chained fatty acyl CoAs acted as acyl donors, these proved to have widely differing apparent Km values with palmitoleoyl CoA having the highest affinity (Km 24 microM) and arachidonoyl CoA the lowest affinity (Km 330 microM).
牛胎盘子叶微粒体中的酰基辅酶A：雌二醇-17β酰基转移酶与膜紧密结合。该酶可通过胆酸钠从微粒体中溶解出来，并重新组装到磷脂囊泡中。雌二醇-17β的表观Km值为11微摩尔，这与先前在膜结合酶中发现的8微摩尔的值相近。睾酮也是重组酶的底物（表观Km为62微摩尔），并且是雌二醇-17β酰化的竞争性抑制剂（Ki为74微摩尔）。尽管各种长链脂肪酰基辅酶A可作为酰基供体，但事实证明它们的表观Km值差异很大，其中棕榈油酰辅酶A具有最高亲和力（Km为24微摩尔），花生四烯酰辅酶A具有最低亲和力（Km为330微摩尔）。
