PMID: 8443248Feb 24, 1993Paper

Lecithin-cholesterol acyltransferase: effects of mutagenesis at N-linked oligosaccharide attachment sites on acyl acceptor specificity

Biochimica Et Biophysica Acta
O L FranconeC Fielding

Abstract

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.

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Citations

Jun 23, 1997·Biochimica Et Biophysica Acta·J WangJ S Parks
Mar 25, 2009·Current Opinion in Endocrinology, Diabetes, and Obesity·Xavier RoussetAlan T Remaley
Oct 8, 1999·Clinica Chimica Acta; International Journal of Clinical Chemistry·M Dobiásová, J J Frohlich
Mar 17, 2009·Bioorganic & Medicinal Chemistry·Danielle Skropeta
Mar 27, 1997·Biochemical and Biophysical Research Communications·S Adimoolam, A Jonas
Feb 1, 2009·Clinical Lipidology·Mary G Sorci-ThomasMichael J Thomas
Nov 3, 1995·The Journal of Biological Chemistry·E Hengstschläger-OttnadW J Schneider
Apr 21, 1995·The Journal of Biological Chemistry·H G KleinS Santamarina-Fojo
Apr 8, 1999·Progress in Lipid Research·A Jonas
Jan 15, 2004·Chemical Reviews·Minghan Wang, Michael R Briggs

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