Lecithin-cholesterol acyltransferase: effects of mutagenesis at N-linked oligosaccharide attachment sites on acyl acceptor specificity.
Site-directed mutagenesis was used to generate lecithin-cholesterol acyltransferase (LCAT) species in which individual attachment sites for N-linked oligosaccharide residues were replaced with residues that prevent the attachment of carbohydrate. Mutants at three of four sites retained significant acyltransferase activity, and phospholipase activity in the absence of cholesterol. Mutation at one site (asn272) converted LCAT to a phospholipase generating fatty acids not cholesteryl esters.
Francone
O L
OL
Cardiovascular Research Institute, University of California Medical Center, San Francisco 94143-0130.
Evangelista
L
L
Fielding
C J
CJ
D000595:Amino Acid Sequence; D001665:Binding Sites; D002788:Cholesterol Esters / Q000378:metabolism; D004247:DNA / Q000302:isolation & purification; D004926:Escherichia coli / Q000235:genetics; D005227:Fatty Acids / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D009844:Oligosaccharides / Q000378:metabolism; D007862:Phosphatidylcholine-Sterol O-Acyltransferase / Q000235:genetics* / Q000378:metabolism; D010740:Phospholipases / Q000378:metabolism; D016133:Polymerase Chain Reaction; D013379:Substrate Specificity; D014162:Transfection
D002788:Cholesterol Esters; D005227:Fatty Acids; D009844:Oligosaccharides; D004247:DNA; D007862:Phosphatidylcholine-Sterol O-Acyltransferase; D010740:Phospholipases