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2.3.1.43: phosphatidylcholine-sterol O-acyltransferase

This is an abbreviated version!
For detailed information about phosphatidylcholine-sterol O-acyltransferase, go to the full flat file.

Word Map on EC 2.3.1.43

Reaction

phosphatidylcholine
+
a sterol
=
1-acylglycerophosphocholine
+
a sterol ester

Synonyms

acyltransferase, lecithin-cholesterol, cholesterol transacyltransferase, LAT, LCAT, lecithin cholesterol acyl transferase, lecithin cholesterol acyltransferase, lecithin-cholesterol acyl transferase, lecithin-cholesterol acyltransferase, lecithin/cholesterol acyltransferase, lecithin: cholesterol acyltransferase, lecithin:cholesterol acyl-transferase, lecithin:cholesterol acyltransferase, lysolecithin acyltransferase, phospholipid-cholesterol acyltransferase, plasma lecithin-cholesterol acyltransferase, TgLCAT, TGME49_272420

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.43 phosphatidylcholine-sterol O-acyltransferase

Crystallization

Crystallization on EC 2.3.1.43 - phosphatidylcholine-sterol O-acyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with antibody 27C3, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.0) and 5% (w/v) PEG 20000
molecular dynamics simulation. LCAT anchors itself to lipoprotein surfaces by utilizing nonpolar amino acids located in the membrane-binding domain and the active site tunnel opening. The membrane-anchoring hydrophobic amino acids attract cholesterol molecules next to them. The apolipoprotein A-I-derived peptides from the LCAT-activating region bind to LCAT and promote its lipid surface interactions, although some of these peptides do not bind lipids individually. The transfer free-energy of phospholipid from the lipid bilayer into the active site is consistent with the activation energy of LCAT