EC number:2.3.1.43

Enzyme

Download
EC Tree
     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.43
Description:Phosphatidylcholine--sterol O-acyltransferase.
Alternative Name: Phospholipid--cholesterol acyltransferase.
Lecithin--cholesterol acyltransferase.
LCAT.
Prosite: PDOC00110;
PDB:
PDBScop
5CH8 8066156; 8066157;
1Y7H 8031587; 8043965; 8031587; 8043965; 8031587; 8043965; 8031587; 8043965; 8031587; 8043965; 8031587; 8043965; 8031587; 8043965; 8031587; 8043965;
1XKL 8031587; 8043965; 8031587; 8043965; 8031587; 8043965; 8031587; 8043965;
1Y7I 8031587; 8043965; 8031587; 8043965;
1K8Q 8027722; 8040101; 8027722; 8040101;
 » show all
Cath: 3.40.50.1820;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.
PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.43
BRENDA Enzyme Link: BRENDA 2.3.1.43
KEGG Enzyme Link: KEGG2.3.1.43
BioCyc Enzyme Link: BioCyc 2.3.1.43
ExPASy Enzyme Link: ExPASy2.3.1.43
EC2PDB Enzyme Link: EC2PDB 2.3.1.43
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.43
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.43
IntEnz Enzyme Link: IntEnz 2.3.1.43
MEDLINE Enzyme Link: MEDLINE 2.3.1.43

EC number:2.3.1.43

MSA:

2.3.1.43;
Phylogenetic Tree:

2.3.1.43;
Uniprot:
M-CSA:
RHEA:21204 a 1,2-diacyl-sn-glycero-3-phosphocholine + a sterol = a 1-acyl-sn-glycero-3-phosphocholine + a steryl ester
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[O;H0;+0:6]-[*:7]>>[*:7]-[OH;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Comparative studies on the substrate specificity of lecithin:cholesterol acyltransferase towards the molecular species of phosphatidylcholine in the plasma of 14 vertebrates.Subbaiah PV, Liu M1996 Jan8820107
Chicken lecithin-cholesterol acyltransferase. Molecular characterization reveals unusual structure and expression pattern.Hengstschläger-Ottnad E, Kuchler K, Schneider WJ1995 Nov 37592817
Cloning and expression of human lecithin-cholesterol acyltransferase cDNA.McLean J, Fielding C, Drayna D, Dieplinger H, Baer B, Kohr W, Henzel W, Lawn R1986 Apr3458198
The high-resolution crystal structure of human LCAT.Piper DE, Romanow WG, Gunawardane RN, Fordstrom P, Masterman S, Pan O, Thibault ST, Zhang R, Meininger D, Schwarz M, Wang Z, King C, Zhou M, Walker NP2015 Sep26195816
Structure and function of lysosomal phospholipase A2 and lecithin:cholesterol acyltransferase.Glukhova A, Hinkovska-Galcheva V, Kelly R, Abe A, Shayman JA, Tesmer JJ2015 Mar 225727495
LCAT synthesized by primary astrocytes esterifies cholesterol on glia-derived lipoproteins.Hirsch-Reinshagen V, Donkin J, Stukas S, Chan J, Wilkinson A, Fan J, Parks JS, Kuivenhoven JA, Lütjohann D, Pritchard H, Wellington CL2009 May19065001
Apolipoprotein E is the major physiological activator of lecithin-cholesterol acyltransferase (LCAT) on apolipoprotein B lipoproteins.Zhao Y, Thorngate FE, Weisgraber KH, Williams DL, Parks JS2005 Jan 2515654758
Negative charge at amino acid 149 is the molecular determinant for substrate specificity of lecithin: cholesterol acyltransferase for phosphatidylcholine containing 20-carbon sn-2 fatty acyl chains.Zhao Y, Wang J, Gebre AK, Chisholm JW, Parks JS2003 Dec 214636062
Binding affinity and reactivity of lecithin cholesterol acyltransferase with native lipoproteins.Kosek AB, Durbin D, Jonas A1999 May 1910329423
Secretion of lecithin:cholesterol acyltransferase by brain neuroglial cell lines.Collet X, Francone O, Besnard F, Fielding CJ1999 Apr 2910222237