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...
Topics
- Amino Acid Sequence
- Animals
- Catalytic Domain
- Conserved Sequence
- Humans
- Lecithin Cholesterol Acyltransferase Deficiency
- Models, Molecular
- Molecular Sequence Data
- Phenotype
- Phosphatidylcholine-Sterol O-Acyltransferase
- Point Mutation
- Protein Conformation
- Sequence Homology, Amino Acid