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Comparative specificity of plasma lecithin: Cholesterol acyltransferase from ten animal species
Author(s) -
Grove Douglas,
Pownall Henry J.
Publication year - 1991
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02536066
Subject(s) - sterol o acyltransferase , lecithin , biochemistry , cholesteryl ester , chemistry , cholesterylester transfer protein , cholesterol , acyltransferase , clinical chemistry , polyunsaturated fatty acid , enzyme , phosphatidylcholine , intermediate density lipoprotein , human plasma , acyl coa , acyl group , lipoprotein , chromatography , phospholipid , fatty acid , very low density lipoprotein , organic chemistry , membrane , alkyl
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.