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
-
2.3.1.135
-
retinoids
-
retinal
-
all-trans-retinyl
-
opsin
-
11-cis-retinol
-
isomerohydrolase
-
amaurosis
-
leber
-
s-opsins
-
11-cis-retinoids
-
medicine
-
crbp-i
-
diagnostics
-
analysis
- 2.3.1.135
-
retinoids
- retinal
-
all-trans-retinyl
- opsin
- 11-cis-retinol
-
isomerohydrolase
- amaurosis
-
leber
-
s-opsins
-
11-cis-retinoids
- medicine
-
crbp-i
- diagnostics
- analysis
Reaction
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
Advanced search results
Subunits
Subunits on EC 2.3.1.135 - phosphatidylcholine-retinol O-acyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
dimer
-
2 * 25000, full-length wild-type enzyme, SDS-PAGE, 2 * 20000, recombinant truncated enzyme, SDS-PAGE
homodimer
monomer
additional information
monomer
-
1 × 25300, SDS-PAGE in presence of 2-mercaptoethanol, fully active catalytically
monomer
-
1 * 25000, full-length wild-type enzyme, SDS-PAGE, 1 * 20000, recombinant truncated enzyme, SDS-PAGE
-
LRAT monomer interact in membranes and form functional homodimers, the dimer formation is mediated by disulfide bond formation and protein-protein interactions
additional information
-
the enzyme exists as a mixture of monomer and dimer, determined by sedimentation equilibrium analysis and mass spectrometry, higher aggregation, up to pentamers, occurs in absence of denaturing agents
additional information
-
epitope mapping, the enzyme contains a C-terminal transmembrane domain