Ishinaga M, Nishihara M, Kato M, Kito M
Biochim Biophys Acta. 1976 Jun 22;431(3):426-32.
SN-Glycerol 3-phosphate acyltrasferase (EC 2.3.1.15) bound to the elaidate enriched membranes of an unsaturated fatty acid auxotroph of Escherichia coli had a lower specific activity than the acyltrasferase associated with the wild-type membranes. The 1-saturated-2-cis-unsaturated and 1,2-di-cis-unsaturated molecular species of phosphatidylglycerol activated this enzyme. However, these molecular species did not change the original temperature profile obtained by Arrhenius plots of the enzyme activity bound to the elaidate-enriched membranes.
与大肠杆菌不饱和脂肪酸营养缺陷型富含反油酸的膜结合的sn-甘油-3-磷酸酰基转移酶（EC 2.3.1.15）的比活性低于与野生型膜相关的酰基转移酶。磷脂酰甘油的1-饱和-2-顺式不饱和分子物种和1,2-二顺式不饱和分子物种激活了该酶。然而，这些分子物种并没有改变通过对富含反油酸的膜结合酶活性进行阿伦尼乌斯图得到的原始温度曲线。
