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
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2.3.1.135
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retinoids
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retinal
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all-trans-retinyl
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opsin
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11-cis-retinol
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isomerohydrolase
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amaurosis
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leber
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s-opsins
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11-cis-retinoids
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medicine
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crbp-i
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diagnostics
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analysis
- 2.3.1.135
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retinoids
- retinal
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all-trans-retinyl
- opsin
- 11-cis-retinol
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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
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Natural Substrates Products
Natural Substrates Products on EC 2.3.1.135 - phosphatidylcholine-retinol O-acyltransferase
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REACTION DIAGRAM
lecithin + 11-cis-retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + 11-cis-retinyl ester-[cellular retinol-binding protein]
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r
lecithin + all-trans-retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + all-trans-retinyl ester-[cellular retinol-binding protein]
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-
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-
r
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
palmitoyl-CoA + 11-cis-retinol-[cellular retinol-binding protein]
CoA + 11-cis-retinyl palmitate-[cellular retinol-binding protein]
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esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
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?
palmitoyl-CoA + all-trans-retinol-[cellular retinol-binding protein]
CoA + all-trans-retinyl palmitate-[cellular retinol-binding protein]
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esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
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-
?
phosphatidylcholine + 11-cis-retinol
2-acylglycerophosphocholine + 11-cis-retinyl acyl ester
essential for generation of the precursor for 11-cis-retinal, the visual chromophore in the eye
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-
?
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
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trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
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r
phosphatidylcholine + 11-cis-retinoll-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
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trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
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r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acyl ester
enzyme is involved in vitamin A storage and mobilization
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r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl ester
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LRAT catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
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?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + retinyl ester
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LRAT catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
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?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
phosphatidylcholine + all-trans-retinylamine
2-acylglycerophosphocholine + all-trans-retinyl acylamide
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-
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?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
phosphatidylcholine + retinylamine
2-acylglycerophosphocholine + fatty acid N-retinylamide
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?
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
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fatty acid retinyl esters are the storage form of vitamin A, all-trans-retinol, and serve as metabolic intermediates in the formation of the visual chromophore 11-cis-retinal, LRAT catalyzes the synthesis of retinyl esters, thereby drawing retinol from the circulation to storage depots
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?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
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the enzyme is responsible for catalyzing retinyl ester formation from retinol
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?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
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the enzyme is responsible for catalyzing retinyl ester formation from retinol
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?
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
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?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
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?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
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-
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?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
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?
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
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?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
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enzyme essential for the biosynthesis of 11-cis-retinal and for dietary mobilization of vitamin A
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?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
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?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
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?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
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?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
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?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
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important role in absorption and storage of vitamin A
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?
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
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?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
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enzyme is involved in the visual cycle in the eye
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?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
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trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
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-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
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lecithin-retinol acyltransferase is essential for accumulation of all-trans-retinyl esters and the retinoid cycle in the eye and in the liver
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?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
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trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
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-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
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enzyme and cellular retinol binding protein I, CRBP I are involved in retinoid storage regulation, retinoid biosynthetic pathway, overview
the retinyl ester is the storage form of retinoids, retinol is the precursor for retinal, which has a function as visual chromophore, and subsequently of retinoic acid, which is a signaling hormone
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r
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
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?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
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renal cell carcinomata contain greatly reduced levels of retinol and retinyl esters relative to healthy kidney tissue
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?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
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?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
Mus musculus C57/BL6J / 129 Sv
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?
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ARAT, EC 2.3.1.76, may complement LRAT to provide additional retinyl-ester synthase activity under conditions of high all-trans-retinol
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additional information
?
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LRAT is not required for retinoid isomerase activity beyond synthesis of retinyl-ester substrate, association of Rpe65 protein, a membrane-associated protein in the retinal pigment epithelium, with membranes is neither dependent upon LRAT nor the result of S-palmitoylation on Cys231, Cys329, and Cys330 by the enzyme, overview
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additional information
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LRAT plays an essential role in the regeneration of visual chromophore as well as in the metabolism of vitamin A, and is responsible for amidation of retinylamine, a potent and selective inhibitor of the retinoid cycle and 11-cis-retinal biosynthesis
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?
additional information
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low prevalence of lecithin retinol acyltransferase mutations in patients with Leber congenital amaurosis and autosomal recessive retinitis pigmentosa
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additional information
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retinoids, vitamin A, i.e.retinol, and related metabolites, have been shown to be important in regulating cell growth and differentiation, retinoid signaling, overview, expression of LRAT, which converts retinol to retinyl esters, is reduced in several human carcinomas as compared with adjacent normal tissue from the same organs, LRAT protein progressively decreases with a reduction in the degree of tumor differentiation in invasive breast carcinomas, overview
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additional information
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LRAT is not required for retinoid isomerase activity beyond synthesis of retinyl-ester substrate, association of Rpe65 protein, a membrane-associated protein in the retinal pigment epithelium, with membranes is neither dependent upon LRAT nor the result of S-palmitoylation on Cys231, Cys329, and Cys330 by the enzyme, overview
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?
additional information
?
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LRAT is required for retinoid storage and lipid droplet formation in hepatic stellate cells, LRAT is not the sole enzyme that catalyzes retinyl ester formation in vivo, role of LRAT in retinoid absorption and storage in different tissues, overview
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?
additional information
?
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LRAT plays an essential role in the regeneration of visual chromophore as well as in the metabolism of vitaminA, and is responsible for amidation of retinylamine, a potent and selective inhibitor of the retinoid cycle and 11-cis-retinal biosynthesis
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?
additional information
?
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LRAT plays a role in maintaining a stable serum retinol concentration when dietary retinol concentration fluctuates
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?
additional information
?
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LRAT is not required for retinoid isomerase activity beyond synthesis of retinyl-ester substrate, association of Rpe65 protein, a membrane-associated protein in the retinal pigment epithelium, with membranes is neither dependent upon LRAT nor the result of S-palmitoylation on Cys231, Cys329, and Cys330 by the enzyme, overview
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additional information
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retinoids play an essential role in development and throughout life, levels in rat tissue after treatment with 2,3,7,8-tetrachlorodibenzo-4-dioxin, overview
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