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Article

Effects of natural mutations in lecithin:cholesterol acyltransferase on the enzyme structure and activity.

Journal of lipid research - 1 Jan 1999

Peelman F, Verschelde J L, Vanloo B, Ampe C, Labeur C, Tavernier J, Vandekerckhove J, Rosseneu M

Abstract excerpt

A molecular model was built for human lecithin:cholesterol acyltransferase (LCAT) based upon the structural homology between this enzyme and lipases (Peelman et al. 1998. Prot. Sci. 7: 585-597). We proposed that LCAT belongs to the alpha/beta hydrolase fold family, and that the central domain of LCAT consists of a mixed seven-stranded beta-pleated sheet with four alpha-helices and loops linking the beta-strands....

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Source

Identifiers

PMID: 9869650

Genes

LCAT

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Effects of natural mutations in lecithin:cholesterol acyltransferase on the enzyme structure and activity.PMID 9869650Read ↗

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Relationship between structure and biochemical phenotype of lecithin:cholesterol acyltransferase (LCAT) mutants causing fish-eye disease.Semantic proximity Read ↗

Lecithin:cholesterol acyltransferase deficiency: identification of a causative gene mutation and a co-inherited protein polymorphism.Semantic proximity Read ↗

Genetic and phenotypic heterogeneity in familial lecithin: cholesterol acyltransferase (LCAT) deficiency. Six newly identified defective alleles further contribute to the structural heterogeneity in this disease.Semantic proximity Read ↗

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