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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

Cloned

Cloned on EC 2.3.1.43 - phosphatidylcholine-sterol O-acyltransferase

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293S cells
expression in baby hamster kidney cells
-
expression in Chinese hamster ovary cells, recombinant enzyme is structurally similar to plasma LCAT
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expression in HEK-293-6E cell, HEK-293S GnTI cell
expression in hepatic Mc-7777 cells
-
expression in mice and rabbit
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expression of a C-terminal histidine tagged enzyme in Chinese hamster ovary cells
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expression of C-terminally His6-tagged LCAT in CHO cells
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expression of mutant enzymes in baby hamster kidney cells
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expression of mutant enzymes in COS-6 cells
-
expression of the naturally occurring mutants T123I and N228K in COS-1 and CHO cells
-
expression of truncated enzymes in COS-1 cells
-
expression of wild-type enzyme and N-terminally truncated enzymes in COS-7 cells, secretion to the cell culture
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gene lcat, located on chromosome VIII, DNA and amino acid sequence determination and analyis, sequence comparisons and phylogenetic analysis, recombinant stable expression of HA- or YFP-tagged enzyme in Toxoplasma gondii, recombinant expression of His-tagged peptide TgLCAT(106-202) in Escherichia coli strain M15, recombinant expression in insect cells, using baculovirus transfection, and secretion to the culture medium
gene lcat, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS, recombinant expression of the enzyme in apoI-deficient mice, recombinant expression in CHO cells
gene lcat, stable recombinant expression in HEK-293Fcells
gene lcat, use of baculovirus as a transducing vector to express the C-or N-terminally His-tagged enzyme in insect cell line Sf9, and to transiently express tagged LCAT in human HEK-293 GnTI cells, deficient in N-acetylglucosaminyl transferase I and expression of the recombinant protein as a high-mannose glycoform (of the MAN9GlcNAc2 or MAN5GlcNAc2 types) suitable for deglycosylation by Endo H, which leaves a single N-acetyl glucosamine (GlcNAc) residue at the glycosylation sites, to avoid protein aggregation coccuring with fully deglycosylated protein. Or expression in HEK-293 6E cells. TEV or Factor Xa sites are introduced for tag cleavage. The enzyme is secreted. Method development and evaluation, overview
LCAT overexpression in transgenic mouse J774 macrophages
optimization of expression in human lung cell line H1299, enzyme is secreted to the culture medium
overexpression of LCAT in male nonhuman primate squirrel monkeys, Saimiri sciureus, using an adenoviral vector affects the lipoprotein metabolism, leading to an antiatherogenic lipoprotein profile by increasing HDL cholesterol and lowering ApoB, overview. Increased LCAT activity is also associated with a change in the size of HDL
-
overexpression of LCAT in rabbit hepatocytes
-
stable expression in CHO cells, expression in insect cells via baculovirus infection, glycosylation pattern of the recombinant enzymes differs from the wild-type, overview
-
transient expression of wild-type and mutant enzymes in COS-1 cells
-