Comparative specificity of plasma lecithin: Cholesterol acyltransferase from ten animal species
Comparative specificity of plasma lecithin: Cholesterol acyltransferase from ten animal species
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DOI：
10.1007/bf02536066
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发表时间：
1991-06
期刊：
影响因子：
1.9
通讯作者：
D. Grove;H. Pownall
中科院分区：
文献类型：
--
作者：
D. Grove;H. Pownall
比较了10种动物血浆卵磷脂：胆固醇酰基转移酶（LCAT）的分子特异性。使用含有磷脂酰胆碱混合物的重组高密度脂蛋白，测定不同种类胆固醇酯的相对释放速率。除了两个物种的LCAT集群根据三种模式的底物特异性。包括人类在内的六个物种的LCAT没有转移高度多不饱和脂肪酰基链。此外，人LCAT酯交换饱和脂肪酰基链比不饱和脂肪酰基链更有效。我们的结论是，酶的活性位点的结构不同，这可能与大小的限制，防止大体积的磷脂酰胆碱的有效结合。
The molecular specificities of plasma lecithin:cholesterol acyltransferase (LCAT) from ten animal species have been compared. Using a reassembled high density lipoprotein containing a mixture of phosphatidylcholines, the relative rates of liberation of different species of cholesteryl ester were measured. All but two species of LCAT clustered according to one of three patterns of substrate specificity. The LCAT from six species, including human, did not transfer highly polyunsaturated fatty acyl chains. In addition, human LCAT transesterified saturated fatty acyl chains more effectively than unsaturated fatty acyl chains. We conclude that the structures of the active sites of the enzymes differ, and that this may be related to size constraints that prevent efficient binding of large bulky phosphatidylcholines.