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2.3.1.135: phosphatidylcholine-retinol O-acyltransferase

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

Word Map on EC 2.3.1.135

Reaction

phosphatidylcholine
+
retinol-[cellular-retinol-binding-protein]
=
2-acylglycerophosphocholine
 +
retinyl-ester-[cellular-retinol-binding-protein]

Synonyms

11-cis-acyl-CoA:retinol O-acyltransferase, acyltransferase, lecithin-retinol, EC 5.2.1.3, lecithin retinol acyl transferase, lecithin retinol acyltransferase, lecithin-retinol acyltransferase, lecithin/retinol acyltransferase, lecithin: retinol acyltransferase, lecithin:retinol acyl transferase, lecithin:retinol acyltransferase, LRAT, More, retinyl ester synthase, retinyl-ester synthase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.135 phosphatidylcholine-retinol O-acyltransferase

Purification

Purification on EC 2.3.1.135 - phosphatidylcholine-retinol O-acyltransferase

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity labeling with all-trans-retinyl-alpha-bromoacetate, SDS electrophoresis, prior to affinity labelling, incubation with cholesterol chloroacetate to block nucleophilic reagents, or streptavidin column to remove endogenously biotinylated proteins enhance protein purification
-
affinity labeling with N-Boc-L-biocytinyl-11-aminoundecan chloromethylketone, precipitation and gel electrophoresis, prior to affinity labelling, incubation with cholesterol chloroacetate to block nucleophilic reagents, or streptavidin column to remove endogenously biotinylated proteins enhance protein purification
-
enzyme transfected in HEK-293T cells partially purificated by solubilization and centrifugation
-
histidine-tagged truncated LRAT
-
labeling with N-Boc-L-biocytinyl-11-aminoundecan chloromethylketone, affinity chromatography, avidin, prior to affinity chromatography or affinity labelling, incubation with cholesterol chloroacetate to block nucleophilic reagents, or streptavidin column to remove endogenously biotinylated proteins enhance protein purification
-
native enzyme partially by membrane preparation
-
native enzyme partially by membrane preparation from retinal pigment epithelium
native enzyme partially by microsome preparation from eyes, recombinant enzyme partially from HEK-293T cells by membrane preparation
-
recombinant His-tagged LRAT by affinity chromatography
-
recombinant His-tagged truncated wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography in presence of 1% SDS
recombinant truncated enzyme from Escherichia coli in presence of 1% SDS, by nickel affinity chromatography to homogeneity
-
recombinant truncated tLRAT and its S175R mutant
-
SDS is necessary for tLRAT extraction from cell lysates. tLRAT enzymatic activity drastically diminishes at SDS concentrations below 0.05% and remains unchanged when SDS concentration is increased from 0.05 to 1%. SDS is very important for tLRAT stability. Detergents such as 0.2% Triton X-100, 0.7% CHAPSO,and 1.2 mM n-dodecyl-beta-D-maltoside and sodium are not effective
solubilization of membranes and centrifugation, chromatography on DEAE-column and Mono-Q column later on, quantitative information
-
solubilization of membranes and centrifugation, chromatography: mono Q column and Green 5-agarose column
-
solubilization, centrifugation and dialysis
-