Francone_1996_J.Lipid.Res_37_1609

Reference

Title : Effects of carboxy-terminal truncation on human lecithin:cholesterol acyltransferase activity - Francone_1996_J.Lipid.Res_37_1609
Author(s) : Francone OL , Evangelista L , Fielding CJ
Ref : J Lipid Res , 37 :1609 , 1996
Abstract :

Mutagenesis was carried out in human lecithin:cholesterol acyltransferase (LCAT) to generate mutants with stop codons at positions corresponding to amino acids 315, 341, 359, 375, 388, 394, and 398 of the 416-amino acid sequence of the mature enzyme protein. Deletion of the 18 terminal amino acids of the protein was without effect on LCAT phospholipase or acyltransferase activity, or the stability of the protein to denaturation at 37 degrees C. Further deletion led to loss of most of the activity, associated with a 10-fold increase in the rate of denaturation at 37 degrees C. These data indicate that the proline-rich C-terminus of LCAT is not required for effective enzyme activity. The loss of activity that accompanied deletion of residues 394-398 suggests a structural role for these residues, part of a series of predicted beta-sheet sequences in the C-terminal third of the LCAT primary sequence.

PubMedSearch : Francone_1996_J.Lipid.Res_37_1609
PubMedID: 8827531
Gene_locus related to this paper: mouse-Ces3a

Related information

Gene_locus mouse-Ces3a

Citations formats

Francone OL, Evangelista L, Fielding CJ (1996)
Effects of carboxy-terminal truncation on human lecithin:cholesterol acyltransferase activity
J Lipid Res 37 :1609

Francone OL, Evangelista L, Fielding CJ (1996)
J Lipid Res 37 :1609