Burritt M F, Henderson T O
J Bacteriol. 1975 Sep;123(3):972-7. doi: 10.1128/jb.123.3.972-977.1975.
Cardiolipin (CL) synthetase of Lactobacillus plantarum 17-5 catalyzed the stoichiometric conversion of 2 mol of phosphatidylglycerol to 1 mol of CL. The enzyme activity was linear with time for 30 min at 37 C and with protein concentration between 20 and 200 mug of protein per ml. The enzyme was membrane associated, had a pH optimum of 5.1 in phosphate buffer, and was not stimulated by Mg2+, and the activity was not affected by the addition of ethylenediaminetetraacetic acid, cytidine diphosphate diglyceride, or cytidine triphosphate. The reaction was inhibited about 95% by Triton X-100 (0.5% final concentration) and by CL, the end product of the reaction. The activity of this enzyme was studied as a function of growth. The CL synthetase specific activity was highest during the early and midexponential growth phases, as was the cellular content of CL. The results demonstrate a correlation between enzyme-specific activity and lipid content of the cells.
植物乳杆菌17-5的心磷脂（CL）合成酶催化2摩尔磷脂酰甘油化学计量转化为1摩尔CL。在37℃下，酶活性在30分钟内与时间呈线性关系，在每毫升20至200微克蛋白质的蛋白质浓度范围内也呈线性关系。该酶与膜相关，在磷酸盐缓冲液中的最适pH为5.1，不受Mg2+刺激，添加乙二胺四乙酸、胞苷二磷酸甘油酯或三磷酸胞苷对其活性没有影响。反应被Triton X-100（终浓度0.5%）和反应终产物CL抑制约95%。研究了该酶活性随生长的变化。CL合成酶比活性在指数生长早期和中期最高，CL的细胞含量也是如此。结果表明酶比活性与细胞脂质含量之间存在相关性。
