LECITHIN-CHOLESTEROL ACYLTRANSFERASE - EFFECTS OF MUTAGENESIS AT N-LINKED OLIGOSACCHARIDE ATTACHMENT SITES ON ACYL ACCEPTOR SPECIFICITY

被引：30

作者：

FRANCONE, OL ^{[1
]}

EVANGELISTA, L ^{[1
]}

FIELDING, CJ ^{[1
]}

机构：

[1] UNIV CALIF SAN FRANCISCO,MED CTR,DEPT PHYSIOL,SAN FRANCISCO,CA 94143

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1993年 / 1166卷 / 2-3期

关键词：

LECITHIN CHOLESTEROL ACYLTRANSFERASE; SITE-DIRECTED MUTAGENESIS; N-LINKED OLIGOSACCHARIDE;

D O I：

10.1016/0005-2760(93)90110-U

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：301 / 304

页数：4

共 12 条

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