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1-lauroyl-2-myristoylphosphatidylcholine + retinol-(cellular-retinol-binding-protein)type II
retinyl laurate-(cellular-retinol-binding-protein)type II + 2-myristoylphosphatidylcholine
-
-
-
?
1-myristoyl-2-lauroylphosphatidylcholine + retinol-(cellular-retinol-binding-protein)type II
retinyl myristate-(cellular-retinol-binding-protein)type II + 2-lauroylphosphatidylcholine
-
-
-
?
1-palmitoyl-2-acetyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + 2-acetyl-sn-glycerol-3-phosphorylcholine
-
-
-
?
1-palmitoyl-2-decanoylphosphatidylcholine + retinol-(cellular-retinol-binding-protein)type II
retinyl palmitate-(cellular-retinol-binding-protein)type II + 2-decanoylphosphatidylcholine
-
-
-
?
1-palmitoyl-2-linoleoyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + 2-linoleoyl-sn-glycerol-3-phosphorylcholine
-
most effective substrate in stimulating palmitate transfer above control levels
-
?
1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + 2-oleoyl-sn-glycerol-3-phosphorylcholine
-
-
-
?
1-palmitoyl-2-stearoyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + 2-stearoyl-sn-glycerol-3-phosphorylcholine
-
-
-
?
1-palmitoyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + glycerol-3-phosphorylcholine
-
-
-
?
didecanoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl decanoate + 2-decanoylglycerophosphocholine
-
activity is about 10% of that with diheptanoylphosphatidylcholine
-
?
diheptanoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl heptanoate + 2-heptanoylglycerophosphocholine
-
-
-
?
dilauroylphosphatidylcholine + all-trans-retinol
all-trans-retinyl laurate + 2-lauroylglycerophosphocholine
-
activity is about 4% of that with diheptanoylphosphatidylcholine
-
?
dilauroylphosphatidylcholine + retinol-(cellular retinol binding protein)type II
retinyl laurate-(cellular retinol binding protein)type II + 2-lauroyl-phosphatidylcholine
-
-
-
?
dimyristoylphosphatidic acid + retinol-(cellular retinol binding protein) type II
retinyl myristate + myristoylphosphatidic acid
-
little if any retinyl myristate obtained
-
?
dimyristoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl myristate + 2-myristoylglycerophosphocholine
activity is about 3% of that with diheptanoylphosphatidylcholine
-
-
?
dimyristoylphosphatidylcholine + retinol(cellular retinol binding protein)type II
retinyl myristate-(cellular retinol binding protein)type II + 2-myristoyl-phosphatidylcholine
-
-
-
?
dimyristoylphosphatidylethanolamine + retinol-(cellular retinol binding protein) type II
retinyl myristate-(cellular retinol binding protein)type II + myristoyl-phosphatidylethanolamine
-
little if any retinyl myristate obtained
-
?
dioctanoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl octanoate + 2-octanoylglycerophosphocholine
activity is less than 15% of that with diheptanoylphosphatidylcholine
-
-
?
dioleoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl oleate + 2-oleoylglycerophosphocholine
-
-
-
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
lecithin + 11-cis-retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + 11-cis-retinyl ester-[cellular retinol-binding protein]
-
-
-
-
r
lecithin + all-trans-retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + all-trans-retinyl ester-[cellular retinol-binding protein]
-
-
-
-
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]
palmitoyl-CoA + all-trans-retinol-[cellular retinol-binding protein]
CoA + all-trans-retinyl palmitate-[cellular retinol-binding protein]
phosphatidylcholine + 11-cis-retinol
11-cis-retinyl acyl ester + 2-acylglycerophosphocholine
-
-
-
r
phosphatidylcholine + 11-cis-retinol
2-acylglycerophosphocholine + 11-cis-retinyl acyl ester
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
phosphatidylcholine + 11-cis-retinoll-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
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.
-
-
r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acyl ester
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acylester
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl ester
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + retinyl ester
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
phosphatidylcholine + all-trans-retinol-(bovine serum albumin)
all-trans-retinyl acyl ester-(bovine serum albumin) + 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
-
-
-
-
?
phosphatidylcholine + all-trans-retinylamine
2-acylglycerophosphocholine + fatty acid-N-all-trans-retinyl amide
-
-
product identification
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding protein) type II
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein) type II
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
phosphatidylcholine + retinol-[cellular-retinol-binding-protein type II]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein type II]
-
-
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
phosphatidylcholine + retinylamine
2-acylglycerophosphocholine + fatty acid N-retinylamide
-
-
product identification
-
?
additional information
?
-
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
-
-
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
-
-
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
-
-
r
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
-
-
r
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
-
-
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
mechanistic hypothesis
-
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
mechanistic hypothesis
-
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
mechanistic hypothesis
-
r
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
activity is about 2% of that with diheptanoylphosphatidylcholine
-
-
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
-
-
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
-
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
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
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
the enzyme is responsible for catalyzing retinyl ester formation from retinol
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
retinol bound to cellular retinol-binding protein III, CRBP-III, is an excellent substrate for lecithin-retinol acyltransferase
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
the enzyme is responsible for catalyzing retinyl ester formation from retinol
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
retinol bound to cellular retinol-binding protein III, CRBP-III, is an excellent substrate for lecithin-retinol acyltransferase
-
-
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
-
-
-
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
-
-
-
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
-
-
-
?
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]
-
-
-
-
?
palmitoyl-CoA + 11-cis-retinol-[cellular retinol-binding protein]
CoA + 11-cis-retinyl palmitate-[cellular retinol-binding protein]
-
esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
-
-
?
palmitoyl-CoA + all-trans-retinol-[cellular retinol-binding protein]
CoA + all-trans-retinyl palmitate-[cellular retinol-binding protein]
-
-
-
-
?
palmitoyl-CoA + all-trans-retinol-[cellular retinol-binding protein]
CoA + all-trans-retinyl palmitate-[cellular retinol-binding protein]
-
esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
-
-
?
phosphatidylcholine + 11-cis-retinol
2-acylglycerophosphocholine + 11-cis-retinyl acyl ester
-
-
-
?
phosphatidylcholine + 11-cis-retinol
2-acylglycerophosphocholine + 11-cis-retinyl acyl ester
-
low activity
-
-
?
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
-
-
?
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
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.
-
-
r
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
-
-
r
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
-
-
r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acyl ester
enzyme is involved in vitamin A storage and mobilization
-
-
r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acyl ester
all-trans-retinol is vitamin A, phosphatidylcholine is lecithin
-
-
r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acylester
-
-
-
-
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acylester
transfer of acyl moiety from sn-1 position of lecithin, i.e. phosphatidylcholine, to vitamin A, i.e. all-trans-retinol
-
-
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl ester
-
LRAT catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
-
-
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl ester
-
LRAT catalyzes the transfer of an acyl group, chain length C14-C18, from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
product identification
-
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + retinyl ester
-
LRAT catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
-
-
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + retinyl ester
-
LRAT catalyzes the transfer of an acyl group, chain length C14-C18, from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
product identification
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
r
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
r
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
enzyme essential for the biosynthesis of 11-cis-retinal and for dietary mobilization of vitamin A
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
r
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
r
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
important role in absorption and storage of vitamin A
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
enzyme is involved in the visual cycle in the eye
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
transfer of acyl moiety from sn-1 position of lecithin, i.e. phosphatidylcholine, to vitamin A, i.e. all-trans-retinol
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
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.
-
-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
-
-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
lecithin-retinol acyltransferase is essential for accumulation of all-trans-retinyl esters and the retinoid cycle in the eye and in the liver
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
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.
-
-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
-
-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
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
-
r
phosphatidylcholine + retinol-(cellular-retinol-binding protein) type II
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein) type II
-
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding protein) type II
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein) type II
-
reaction with free fatty acid, fatty acyl-CoA, phosphatidic acid or ethanolamine as acyl donors
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
r
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
renal cell carcinomata contain greatly reduced levels of retinol and retinyl esters relative to healthy kidney tissue
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
esterification of all-trans-retinol
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
refolded holo-hRBP from human serum
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
refolded holo-hRBP from human serum
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
all-trans-retinol is a far better substrate than 11-cis-retinol
-
-
?
additional information
?
-
-
the fatty acid in the 2-position is important in substrate recognition
-
-
?
additional information
?
-
-
the fatty acid in the 2-position is important in substrate recognition
-
-
?
additional information
?
-
-
the fatty acid in the 2-position is important in substrate recognition
-
-
?
additional information
?
-
-
ARAT, EC 2.3.1.76, may complement LRAT to provide additional retinyl-ester synthase activity under conditions of high all-trans-retinol
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
no activity with Rpe65 protein
-
-
?
additional information
?
-
-
in presence of palmitoyl-CoA and CRALBP, Muller cell membranes synthesize 11-cis-retinyl ester from 11-cis-retinol at a rate which is 20fold higher than that of all-trans-retinyl ester, in absence of CRALBP, 11-cis-retinyl ester synthesis is greatly reduced by 7fold, in absence of palmitoyl-CoA, retinyl ester synthesis is not observed
-
-
?
additional information
?
-
-
little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
-
-
?
additional information
?
-
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
-
the fatty acid in the 2-position is important in substrate recognition
-
-
?
additional information
?
-
-
phosphatidylcholine selective
-
-
?
additional information
?
-
-
low prevalence of lecithin retinol acyltransferase mutations in patients with Leber congenital amaurosis and autosomal recessive retinitis pigmentosa
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme performs formation of all-trans retinyl heptanoate from all-trans-retinol and 1,2-diheptanoyl-sn-glycero-3-phosphocholine, DHPC
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
no activity with Rpe65 protein
-
-
?
additional information
?
-
LRAT plays a role in maintaining a stable serum retinol concentration when dietary retinol concentration fluctuates
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
no activity with Rpe65 protein
-
-
?
additional information
?
-
-
little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
-
-
?
additional information
?
-
-
little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
-
-
?
additional information
?
-
-
little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
-
-
?
additional information
?
-
-
little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
-
-
?
additional information
?
-
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
-
the fatty acid in the 2-position is important in substrate recognition
-
-
?
additional information
?
-
-
the fatty acid in the 2-position is important in substrate recognition
-
-
?
additional information
?
-
-
phosphatidylcholine selective
-
-
?
additional information
?
-
-
phosphatidylcholine selective
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
lecithin + 11-cis-retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + 11-cis-retinyl ester-[cellular retinol-binding protein]
-
-
-
-
r
lecithin + all-trans-retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + all-trans-retinyl ester-[cellular retinol-binding protein]
-
-
-
-
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]
-
esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
-
-
?
palmitoyl-CoA + all-trans-retinol-[cellular retinol-binding protein]
CoA + all-trans-retinyl palmitate-[cellular retinol-binding protein]
-
esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
-
-
?
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
-
-
?
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
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.
-
-
r
phosphatidylcholine + 11-cis-retinoll-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
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.
-
-
r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acyl ester
enzyme is involved in vitamin A storage and mobilization
-
-
r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl ester
-
LRAT catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
-
-
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + retinyl ester
-
LRAT catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
-
-
?
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
-
-
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
phosphatidylcholine + retinylamine
2-acylglycerophosphocholine + fatty acid N-retinylamide
-
-
-
-
?
additional information
?
-
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
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
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
the enzyme is responsible for catalyzing retinyl ester formation from retinol
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
the enzyme is responsible for catalyzing retinyl ester formation from retinol
-
-
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
-
-
-
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
-
-
-
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
-
-
-
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
enzyme essential for the biosynthesis of 11-cis-retinal and for dietary mobilization of vitamin A
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
important role in absorption and storage of vitamin A
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
enzyme is involved in the visual cycle in the eye
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
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.
-
-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
lecithin-retinol acyltransferase is essential for accumulation of all-trans-retinyl esters and the retinoid cycle in the eye and in the liver
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
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.
-
-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
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
-
r
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
renal cell carcinomata contain greatly reduced levels of retinol and retinyl esters relative to healthy kidney tissue
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
additional information
?
-
-
ARAT, EC 2.3.1.76, may complement LRAT to provide additional retinyl-ester synthase activity under conditions of high all-trans-retinol
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
low prevalence of lecithin retinol acyltransferase mutations in patients with Leber congenital amaurosis and autosomal recessive retinitis pigmentosa
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
LRAT plays a role in maintaining a stable serum retinol concentration when dietary retinol concentration fluctuates
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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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E14L
naturally occuring substitution localized in an N-terminal alpha-helix. The mutant protein is instable and shows accelerated proteosomal degradation. The instability of E14L does not abrogate the production of the visual chromophore in a cell-based assay. Eexpression of E14L leads to a rapid increase in cellular levels of retinoic acid upon retinoid supplementation
K104A
site-directed mutagenesis, reduced activity compared to the truncated wild-type enzyme
K133A
site-directed mutagenesis, increased activity compared to the truncated wild-type enzyme
K133A/K134A
site-directed mutagenesis, slightly increased activity compared to the truncated wild-type enzyme
K134A
site-directed mutagenesis, increased activity compared to the truncated wild-type enzyme
K147A
site-directed mutagenesis, reduced activity compared to the truncated wild-type enzyme
K180A
site-directed mutagenesis, nearly inactive mutant
K180R
site-directed mutagenesis, reduced activity compared to the truncated wild-type enzyme
K186A
site-directed mutagenesis, nearly inactive mutant
K186R
site-directed mutagenesis, reduced activity compared to the truncated wild-type enzyme
K90A
site-directed mutagenesis, highly reduced activity compared to the truncated wild-type enzyme
K95A
site-directed mutagenesis, highly reduced activity compared to the truncated wild-type enzyme
P173L
mutation caused night blindness in a patient. The enzymatic activity of truncated mutant P173L LRAT is 6.3fold lower compared to that of truncated wild-type (P173)
Y118F
site-directed mutagenesis, activity similar to the truncated wild-type enzyme
Y154F
site-directed mutagenesis, inactive mutant
Y167F
site-directed mutagenesis, activity similar to the truncated wild-type enzyme
Y64F
site-directed mutagenesis, highly increased activity compared to the truncated wild-type enzyme
D128N
-
site-directed mutagenesis, construction of an N-glycosylation site for enzyme membrane localization and orientation studies, overview
I42N
-
site-directed mutagenesis, construction of an N-glycosylation site for enzyme membrane localization and orientation studies, overview
S175R
-
naturally occurring missense mutation, causing recessive earlyonset severe retinal dystrophy, the mutant enzyme shows highly reduced activity
S175R
-
site-directed mutagenesis, the mutation in the truncated LRAT results in an inactive enzyme. The S175R mutation has no effect on the membrane binding properties of tLRAT, the global secondary structure of tLRAT remains almost unchanged with the S175R mutation. The loss of enzymatic activity associated with the S175R mutant is related to loss of an essential nucleophile near the active site, or alternatively to steric obstruction of the active site that impedes substrate binding
additional information
-
screening for and analysis of naturally occurring mutants, low prevalence of lecithin retinol acyltransferase mutations in patients with Leber congenital amaurosis and autosomal recessive retinitis pigmentosa, overview
additional information
-
ectopic expression of human lecithin:retinol acyltransferase in murine basal layer of mouse skin and oral cavity epithelia
additional information
-
construction of a truncated enzyme version, tLRAT, that shows enzyme activity, but leads to physiological dysfunction of the protein by causing retinis pigmentosa
additional information
-
construction of a truncated enzyme version, tLRAT, that shows enzyme activity, but leads to physiological dysfunction of the protein by causing retinis pigmentosa
additional information
-
siRNA knockdown of LRAT and RPE65 expression
additional information
human and mouse enzyme differ in residue 173. A significant difference is observed between the intrinsic fluorescence emission as well as between the circular dichroism spectra of a truncated mouse LRAT (R173) and truncated human LRAT (P173). Truncated mouse LRAT is less thermostable than truncated human LRAT
additional information
-
human and mouse enzyme differ in residue 173. A significant difference is observed between the intrinsic fluorescence emission as well as between the circular dichroism spectra of a truncated mouse LRAT (R173) and truncated human LRAT (P173). Truncated mouse LRAT is less thermostable than truncated human LRAT
additional information
-
gene Lrat disruption by targeted recombination for generation of a homozygous knockout mutant, the mutant mice develop normally, but the rod outer segments in the retina are about 35% shorter than those of wild-type mice, rod and cone visual functions are severely attenuated at an early age
additional information
-
construction of Ntm LRAT, a truncation mutant lacking the putative C-terminal transmembrane domain corresponding to Met1Ser195, and Ctm LRAT, a mutant lacking the putative N-terminal transmembrane domain corresponding to Gly35Gly231, the Ntm mutant is not located in the endoplasmic reticulum membrane, but localized to small cytoplasmic structures that are distinct from the ER, while the wild-type and the Ctm mutant are localized in the membrane
additional information
-
disruption of the CRBP-III gene and generation of CRBPIII-/- mice, method, overview, [cellular retinol-binding protein III]-deficient female mice produce milk with less retinyl ester content, especially retinyl-palmitate, compared to wild-type mice, the expression of CRBP-I is increased in adipose tissue of CRBP-III-/- mice compared to the wild-type mice
additional information
-
retinoid absorption and storage is impaired in mice lacking lecithin:retinol acyltransferase, Lrat-deficient mice possess only trace amounts of retinyl esters in liver, lung, and kidney, intestinal absorption of retinol is impaired in the absence of LRAT, they possess 23fold elevated concentrations of retinyl esters in adipose tissue compared with wild type mice, they show 3-4fold upregulation in the level of cytosolic retinol-binding protein type III in adipose tissue, and a striking total absence of large lipid-containing droplets that normally store hepatic retinoid within the hepatic stellate cells, despite the absence of significant retinyl ester stores and stellate cell lipid droplets, the livers of Lrat-/- mice upon histologic analysis appear normal and show no histological signs of liver fibrosis, Lra-/- mice absorb dietary retinol primarily as free retinol in chylomicrons, phenotype, overview
additional information
construction of chimeric proteins between LRAT and human HRASLS2, HRASLS3 and HRASLS4 by by replacing the native sequence of HRASLS2, 3, and 4 (residues 39-57) with the 30 aa mouse LRAT sequence 76DILLALTNDKERTQKVVSNKRLLLGVICKV106
additional information
-
generation of a transgenic reporter mouse expressing green fluorescence protein under the control of region containing -1166 bps from promoter upstream from the putative transcriptional start site of LRAT and 262 bps downstream of this start. Transgenic reporter mice exhibit specific expression in eyes and testes
additional information
human and mouse enzyme differ in residue 173. A significant difference is observed between the intrinsic fluorescence emission as well as between the circular dichroism spectra of a truncated mouse LRAT (R173) and truncated human LRAT (P173). Truncated mouse LRAT is less thermostable than truncated human LRAT and displays lower catalytic activity
additional information
-
human and mouse enzyme differ in residue 173. A significant difference is observed between the intrinsic fluorescence emission as well as between the circular dichroism spectra of a truncated mouse LRAT (R173) and truncated human LRAT (P173). Truncated mouse LRAT is less thermostable than truncated human LRAT and displays lower catalytic activity
additional information
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disruption of the CRBP-III gene and generation of CRBPIII-/- mice, method, overview, [cellular retinol-binding protein III]-deficient female mice produce milk with less retinyl ester content, especially retinyl-palmitate, compared to wild-type mice, the expression of CRBP-I is increased in adipose tissue of CRBP-III-/- mice compared to the wild-type mice
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Homo sapiens
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Rattus norvegicus
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Homo sapiens (O95237)
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Homo sapiens
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Homo sapiens (O95237), Homo sapiens, Mus musculus (Q9JI60), Mus musculus
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Homo sapiens (O95237)
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Homo sapiens (O95237), Mus musculus (Q9JI60)
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Homo sapiens (O95237), Homo sapiens
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Bos taurus (Q9BGL2)
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