Estrada P, Acebal C, Arche R
Mol Cell Biochem. 1985 Nov;69(1):49-54. doi: 10.1007/BF00225926.
The influence of both polar head and acyl chain of lysophospholipid on the activity of partially purified acyl-CoA:lysolecithin acyltransferase from rabbit lung was studied. It was concluded that the presence of methyl groups on the nitrogen of the base was essential for recognition of lysophospholipid as substrate by the enzyme. With respect to the acyl chain length and saturation, the activity followed the order: 16:0 approximately equal to 18:1 greater than 14:0 greater than greater than greater than 18:0 approximately equal to 12:0. Also, the effect on the activity of the acyl chain on acyl-CoA was studied. The activity showed great selectivity for saturated acyl-CoAs. The activity with polyunsaturated fatty acids was very low and in the case of arachidonoyl-CoA was almost negligible. The comparison between crude microsomal preparations and partially purified preparations allowed to suggest that it could exist two different acyl-CoA:lysolecithin acyltransferases differing in their selectivity towards saturated and unsaturated fatty acids.
研究了溶血磷脂的极性头部和酰基链对兔肺部分纯化的酰基辅酶A：溶血卵磷脂酰基转移酶活性的影响。得出的结论是，碱基氮上甲基的存在对于酶将溶血磷脂识别为底物至关重要。关于酰基链长度和饱和度，活性顺序为：16:0约等于18:1大于14:0远大于大于大于18:0约等于12:0。此外，还研究了酰基链对酰基辅酶A活性的影响。该活性对饱和酰基辅酶A表现出极大的选择性。对多不饱和脂肪酸的活性非常低，在花生四烯酰基辅酶A的情况下几乎可以忽略不计。粗微粒体制剂和部分纯体制剂之间的比较表明，可能存在两种不同的酰基辅酶A：溶血卵磷脂酰基转移酶，它们对饱和脂肪酸和不饱和脂肪酸的选择性不同。
