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Information on EC 2.3.1.135 - phosphatidylcholine-retinol O-acyltransferase
for references in articles please use BRENDA:EC2.3.1.135
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.135 phosphatidylcholine-retinol O-acyltransferase
IUBMB Comments
A key enzyme in retinoid metabolism, catalysing the transfer of an acyl group from the sn-1 position of phosphatidylcholine to retinol, forming retinyl esters which are then stored. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein, but has higher affinity for the bound form. Can also esterify 11-cis-retinol.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 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
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leber
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s-opsins
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11-cis-retinoids
- medicine
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crbp-i
- diagnostics
- analysis
Reaction Schemes
showSynonyms
lecithin retinol acyltransferase, lecithin-retinol acyltransferase, lecithin retinol acyl transferase, lecithin:retinol acyl transferase, lecithin/retinol acyltransferase, retinyl ester synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyltransferase, lecithin-retinol
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EC 5.2.1.3
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formerly, part transferred
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lecithin retinol acyl transferase
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lecithin retinol acyltransferase
lecithin-retinol acyltransferase
lecithin: retinol acyltransferase
lecithin:retinol acyl transferase
lecithin:retinol acyltransferase
LRAT
retinyl ester synthase
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additional information
lecithin-retinol acyltransferase
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lecithin:retinol acyltransferase
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lecithin:retinol acyltransferase
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LRAT
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LRAT
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LRAT
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additional information
enzyme is the founder of a novel Cys-His enzyme family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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]
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phosphatidylcholine + retinol-[cellular-retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
C161 and H60 form a catalytic dyad essential for activity, Q177 and D67 may play a non-essential role in catalysis, identification of the active site, reaction mechanism
phosphatidylcholine + retinol-[cellular-retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
mechanism, Cys161 and Tyr154 are essential for activity
phosphatidylcholine + retinol-[cellular-retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
enzyme mechanism and role in the visual cycle
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
retinol biosynthesis, the visual cycle I (vertebrates)
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SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine:retinol---[cellular-retinol-binding-protein] O-acyltransferase
A key enzyme in retinoid metabolism, catalysing the transfer of an acyl group from the sn-1 position of phosphatidylcholine to retinol, forming retinyl esters which are then stored. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein, but has higher affinity for the bound form. Can also esterify 11-cis-retinol.
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CAS REGISTRY NUMBER
COMMENTARY
117444-03-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-lauroyl-2-myristoylphosphatidylcholine + retinol-(cellular-retinol-binding-protein)type II
retinyl laurate-(cellular-retinol-binding-protein)type II + 2-myristoylphosphatidylcholine
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Substrates: -
Products: -
Products: -
?
1-myristoyl-2-lauroylphosphatidylcholine + retinol-(cellular-retinol-binding-protein)type II
retinyl myristate-(cellular-retinol-binding-protein)type II + 2-lauroylphosphatidylcholine
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Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-acetyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + 2-acetyl-sn-glycerol-3-phosphorylcholine
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Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-decanoylphosphatidylcholine + retinol-(cellular-retinol-binding-protein)type II
retinyl palmitate-(cellular-retinol-binding-protein)type II + 2-decanoylphosphatidylcholine
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Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-linoleoyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + 2-linoleoyl-sn-glycerol-3-phosphorylcholine
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Substrates: most effective substrate in stimulating palmitate transfer above control levels
Products: -
Products: -
?
1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + 2-oleoyl-sn-glycerol-3-phosphorylcholine
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Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-stearoyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + 2-stearoyl-sn-glycerol-3-phosphorylcholine
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Substrates: -
Products: -
Products: -
?
1-palmitoyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + glycerol-3-phosphorylcholine
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Substrates: -
Products: -
Products: -
?
didecanoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl decanoate + 2-decanoylglycerophosphocholine
Substrates: -
Products: activity is about 10% of that with diheptanoylphosphatidylcholine
Products: activity is about 10% of that with diheptanoylphosphatidylcholine
?
diheptanoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl heptanoate + 2-heptanoylglycerophosphocholine
Substrates: -
Products: -
Products: -
?
dilauroylphosphatidylcholine + all-trans-retinol
all-trans-retinyl laurate + 2-lauroylglycerophosphocholine
dilauroylphosphatidylcholine + retinol-(cellular retinol binding protein)type II
retinyl laurate-(cellular retinol binding protein)type II + 2-lauroyl-phosphatidylcholine
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Substrates: -
Products: -
Products: -
?
dimyristoylphosphatidic acid + retinol-(cellular retinol binding protein) type II
retinyl myristate + myristoylphosphatidic acid
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Substrates: little if any retinyl myristate obtained
Products: -
Products: -
?
dimyristoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl myristate + 2-myristoylglycerophosphocholine
Substrates: activity is about 3% of that with diheptanoylphosphatidylcholine
Products: -
Products: -
?
dimyristoylphosphatidylcholine + retinol(cellular retinol binding protein)type II
retinyl myristate-(cellular retinol binding protein)type II + 2-myristoyl-phosphatidylcholine
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Substrates: -
Products: -
Products: -
?
dimyristoylphosphatidylethanolamine + retinol-(cellular retinol binding protein) type II
retinyl myristate-(cellular retinol binding protein)type II + myristoyl-phosphatidylethanolamine
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Substrates: little if any retinyl myristate obtained
Products: -
Products: -
?
dioctanoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl octanoate + 2-octanoylglycerophosphocholine
Substrates: activity is less than 15% of that with diheptanoylphosphatidylcholine
Products: -
Products: -
?
dioleoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl oleate + 2-oleoylglycerophosphocholine
Substrates: -
Products: -
Products: -
?
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]
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Substrates: -
Products: -
Products: -
r
lecithin + all-trans-retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + all-trans-retinyl ester-[cellular retinol-binding protein]
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Substrates: -
Products: -
Products: -
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
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Substrates: -
Products: -
Products: -
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]
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Substrates: 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.
Products: -
Products: -
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
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
phosphatidylcholine + all-trans-retinol-(bovine serum albumin)
all-trans-retinyl acyl ester-(bovine serum albumin) + 2-acylglycerophosphocholine
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinylamine
2-acylglycerophosphocholine + fatty acid-N-all-trans-retinyl amide
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Substrates: -
Products: product identification
Products: 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]
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
phosphatidylcholine + retinylamine
2-acylglycerophosphocholine + fatty acid N-retinylamide
dilauroylphosphatidylcholine + all-trans-retinol
all-trans-retinyl laurate + 2-lauroylglycerophosphocholine
Substrates: -
Products: activity is about 4% of that with diheptanoylphosphatidylcholine
Products: activity is about 4% of that with diheptanoylphosphatidylcholine
?
dilauroylphosphatidylcholine + all-trans-retinol
all-trans-retinyl laurate + 2-lauroylglycerophosphocholine
Substrates: -
Products: -
Products: -
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
Substrates: -
Products: -
Products: -
r
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
Substrates: mechanistic hypothesis
Products: -
Products: -
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
Substrates: mechanistic hypothesis
Products: -
Products: -
r
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
Substrates: activity is about 2% of that with diheptanoylphosphatidylcholine
Products: -
Products: -
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
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Substrates: the enzyme is responsible for catalyzing retinyl ester formation from retinol
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
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Substrates: 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
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
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Substrates: retinol bound to cellular retinol-binding protein III, CRBP-III, is an excellent substrate for lecithin-retinol acyltransferase
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
Substrates: -
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
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Substrates: the enzyme is responsible for catalyzing retinyl ester formation from retinol
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
Substrates: retinol bound to cellular retinol-binding protein III, CRBP-III, is an excellent substrate for lecithin-retinol acyltransferase
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
Substrates: -
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
Substrates: -
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
Substrates: -
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 11-cis-retinol-[cellular retinol-binding protein]
CoA + 11-cis-retinyl palmitate-[cellular retinol-binding protein]
-
Substrates: esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
Products: -
Products: -
?
palmitoyl-CoA + 11-cis-retinol-[cellular retinol-binding protein]
CoA + 11-cis-retinyl palmitate-[cellular retinol-binding protein]
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + all-trans-retinol-[cellular retinol-binding protein]
CoA + all-trans-retinyl palmitate-[cellular retinol-binding protein]
-
Substrates: esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
Products: -
Products: -
?
palmitoyl-CoA + all-trans-retinol-[cellular retinol-binding protein]
CoA + all-trans-retinyl palmitate-[cellular retinol-binding protein]
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + 11-cis-retinol
2-acylglycerophosphocholine + 11-cis-retinyl acyl ester
Substrates: essential for generation of the precursor for 11-cis-retinal, the visual chromophore in the eye
Products: -
Products: -
?
phosphatidylcholine + 11-cis-retinol
2-acylglycerophosphocholine + 11-cis-retinyl acyl ester
-
Substrates: low activity
Products: -
Products: -
?
phosphatidylcholine + 11-cis-retinol
2-acylglycerophosphocholine + 11-cis-retinyl acyl ester
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: 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.
Products: -
Products: -
r
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
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Substrates: both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
Products: -
Products: -
r
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
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Substrates: both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
Products: -
Products: -
r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acyl ester
Substrates: enzyme is involved in vitamin A storage and mobilization
Products: -
Products: -
r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acyl ester
Substrates: all-trans-retinol is vitamin A, phosphatidylcholine is lecithin
Products: -
Products: -
r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acylester
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acylester
Substrates: transfer of acyl moiety from sn-1 position of lecithin, i.e. phosphatidylcholine, to vitamin A, i.e. all-trans-retinol
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acylester
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl ester
-
Substrates: LRAT catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl ester
-
Substrates: 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
Products: product identification
Products: product identification
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + retinyl ester
-
Substrates: LRAT catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + retinyl ester
-
Substrates: 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
Products: product identification
Products: product identification
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
Substrates: -
Products: -
Products: -
r
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
Substrates: enzyme essential for the biosynthesis of 11-cis-retinal and for dietary mobilization of vitamin A
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
Substrates: -
Products: -
Products: -
r
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
Substrates: important role in absorption and storage of vitamin A
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: enzyme is involved in the visual cycle in the eye
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
Substrates: transfer of acyl moiety from sn-1 position of lecithin, i.e. phosphatidylcholine, to vitamin A, i.e. all-trans-retinol
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: 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.
Products: -
Products: -
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
Products: -
Products: -
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: lecithin-retinol acyltransferase is essential for accumulation of all-trans-retinyl esters and the retinoid cycle in the eye and in the liver
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: 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.
Products: -
Products: -
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
Products: -
Products: -
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: enzyme and cellular retinol binding protein I, CRBP I are involved in retinoid storage regulation, retinoid biosynthetic pathway, overview
Products: 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
Products: 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 + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: -
Products: -
Products: -
r
phosphatidylcholine + retinol-(cellular-retinol-binding protein) type II
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein) type II
-
Substrates: reaction with free fatty acid, fatty acyl-CoA, phosphatidic acid or ethanolamine as acyl donors
Products: -
Products: -
?
phosphatidylcholine + retinol-(cellular-retinol-binding protein) type II
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein) type II
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
Substrates: -
Products: -
Products: -
r
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: renal cell carcinomata contain greatly reduced levels of retinol and retinyl esters relative to healthy kidney tissue
Products: -
Products: -
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: esterification of all-trans-retinol
Products: -
Products: -
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: refolded holo-hRBP from human serum
Products: -
Products: -
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
Mus musculus C57/BL6J / 129 Sv
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
Mus musculus C57/BL6J / 129 Sv
-
Substrates: refolded holo-hRBP from human serum
Products: -
Products: -
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinylamine
2-acylglycerophosphocholine + fatty acid N-retinylamide
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinylamine
2-acylglycerophosphocholine + fatty acid N-retinylamide
-
Substrates: -
Products: product identification
Products: product identification
?
additional information
?
-
-
Substrates: all-trans-retinol is a far better substrate than 11-cis-retinol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the fatty acid in the 2-position is important in substrate recognition
Products: -
Products: -
?
additional information
?
-
-
Substrates: the fatty acid in the 2-position is important in substrate recognition
Products: -
Products: -
?
additional information
?
-
-
Substrates: the fatty acid in the 2-position is important in substrate recognition
Products: -
Products: -
?
additional information
?
-
-
Substrates: ARAT, EC 2.3.1.76, may complement LRAT to provide additional retinyl-ester synthase activity under conditions of high all-trans-retinol
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with Rpe65 protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
Products: -
Products: -
?
additional information
?
-
-
Substrates: only fatty acyl group at the sn-1 is transferred
Products: -
Products: -
?
additional information
?
-
Substrates: only fatty acyl group at the sn-1 is transferred
Products: -
Products: -
?
additional information
?
-
-
Substrates: only fatty acyl group at the sn-1 is transferred
Products: -
Products: -
?
additional information
?
-
-
Substrates: only fatty acyl group at the sn-1 is transferred
Products: -
Products: -
?
additional information
?
-
-
Substrates: the fatty acid in the 2-position is important in substrate recognition
Products: -
Products: -
?
additional information
?
-
-
Substrates: phosphatidylcholine selective
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: low prevalence of lecithin retinol acyltransferase mutations in patients with Leber congenital amaurosis and autosomal recessive retinitis pigmentosa
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme performs formation of all-trans retinyl heptanoate from all-trans-retinol and 1,2-diheptanoyl-sn-glycero-3-phosphocholine, DHPC
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with Rpe65 protein
Products: -
Products: -
?
additional information
?
-
Substrates: LRAT plays a role in maintaining a stable serum retinol concentration when dietary retinol concentration fluctuates
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with Rpe65 protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
Products: -
Products: -
?
additional information
?
-
-
Substrates: little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
Products: -
Products: -
?
additional information
?
-
-
Substrates: little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
Products: -
Products: -
?
additional information
?
-
-
Substrates: little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
Products: -
Products: -
?
additional information
?
-
-
Substrates: only fatty acyl group at the sn-1 is transferred
Products: -
Products: -
?
additional information
?
-
-
Substrates: only fatty acyl group at the sn-1 is transferred
Products: -
Products: -
?
additional information
?
-
-
Substrates: only fatty acyl group at the sn-1 is transferred
Products: -
Products: -
?
additional information
?
-
-
Substrates: the fatty acid in the 2-position is important in substrate recognition
Products: -
Products: -
?
additional information
?
-
-
Substrates: the fatty acid in the 2-position is important in substrate recognition
Products: -
Products: -
?
additional information
?
-
-
Substrates: phosphatidylcholine selective
Products: -
Products: -
?
additional information
?
-
-
Substrates: phosphatidylcholine selective
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
lecithin + 11-cis-retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + 11-cis-retinyl ester-[cellular retinol-binding protein]
-
Substrates: -
Products: -
Products: -
r
lecithin + all-trans-retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + all-trans-retinyl ester-[cellular retinol-binding protein]
-
Substrates: -
Products: -
Products: -
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]
-
Substrates: esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
Products: -
Products: -
?
palmitoyl-CoA + all-trans-retinol-[cellular retinol-binding protein]
CoA + all-trans-retinyl palmitate-[cellular retinol-binding protein]
-
Substrates: esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
Products: -
Products: -
?
phosphatidylcholine + 11-cis-retinol
2-acylglycerophosphocholine + 11-cis-retinyl acyl ester
Substrates: essential for generation of the precursor for 11-cis-retinal, the visual chromophore in the eye
Products: -
Products: -
?
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: 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.
Products: -
Products: -
r
phosphatidylcholine + 11-cis-retinoll-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: 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.
Products: -
Products: -
r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acyl ester
Substrates: enzyme is involved in vitamin A storage and mobilization
Products: -
Products: -
r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl ester
-
Substrates: LRAT catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + retinyl ester
-
Substrates: LRAT catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
phosphatidylcholine + retinylamine
2-acylglycerophosphocholine + fatty acid N-retinylamide
-
Substrates: -
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
Substrates: the enzyme is responsible for catalyzing retinyl ester formation from retinol
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
Substrates: 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
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
Substrates: the enzyme is responsible for catalyzing retinyl ester formation from retinol
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
Substrates: -
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
Substrates: -
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
Substrates: -
Products: -
Products: -
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
Substrates: enzyme essential for the biosynthesis of 11-cis-retinal and for dietary mobilization of vitamin A
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
Substrates: important role in absorption and storage of vitamin A
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: enzyme is involved in the visual cycle in the eye
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: 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.
Products: -
Products: -
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: lecithin-retinol acyltransferase is essential for accumulation of all-trans-retinyl esters and the retinoid cycle in the eye and in the liver
Products: -
Products: -
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: 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.
Products: -
Products: -
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: enzyme and cellular retinol binding protein I, CRBP I are involved in retinoid storage regulation, retinoid biosynthetic pathway, overview
Products: 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
Products: 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]
-
Substrates: renal cell carcinomata contain greatly reduced levels of retinol and retinyl esters relative to healthy kidney tissue
Products: -
Products: -
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
Mus musculus C57/BL6J / 129 Sv
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: ARAT, EC 2.3.1.76, may complement LRAT to provide additional retinyl-ester synthase activity under conditions of high all-trans-retinol
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13-demethyl-13,14-dihydro-all-trans-retinyl trifluoroacetate
-
competitive with respect to dipalmitoylphosphocholine, uncompetitive with respect to all-trans-retinol; reversible inhibitor
apo-CRBP-I
-
i.e. apo-[cellular retinol-binding protein I], no inhibition by apo-CRBP-III
-
fenretinide
-
used clinically to presumably lower blood retinol-binding protein levels and thus decrease circulating retinol, targets the functional coupling of STRA6 and LRAT to increase cellular vitamin A uptake in peripheral tissues
N-Boc-L-biocytinyl-11-aminoundecan chloromethylketone
-
0.002 mM, 45% inhibition; irreversible inhibitor; time dependent inhibition
p-chloromercuribenzoic acid
-
0.005 mM, complete inhibition of retinol-(cellular-retinol-binding-protein)type II esterification
N-ethylmaleimide
-
0.001 mM, complete inhibition of retinol-(cellular-retinol-binding-protein)type II esterification
N-ethylmaleimide
-
0.003 mM, complete inhibition of retinol-(cellular-retinol-binding-protein)type II esterification
phenylmethylsulfonyl fluoride
-
2 mM, 90% inhibition of retinol-(cellular-retinol-binding-protein)type II esterification
phenylmethylsulfonyl fluoride
-
1 mM, 90% inhibition of retinol-(cellular-retinol-binding-protein)type II esterification
additional information
-
1-acyl-lysophosphatidylcholine does not inhibit LRAT up to 0.020 mM; product inhibition by retinyl ester can be ruled out
-
additional information
-
not readily inhibitable by serine-directed chemical reagents; readily inactivated by organomercurials in the micromolar range
-
additional information
-
mutant C161S is not significantly inactivated by N-Boc-L-biocytinyl-11-aminoundecan chloromethylketone
-
additional information
-
1% dimethylsulfoxide does not inhibit LRAT activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SDS
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
cellular retinol-binding protein
-
i.e. CRALBP, 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
-
cellular retinol-binding protein
-
CRBP, required for enzyme activity, CRBP-I and CRBP-III each compensate for the absence of the other, specifically in mammary tissue, adipose tissue, muscle, and heart
-
N-(4-hydroxyphenyl)-retinamide
-
restores normal level of LRAT activity in vitamin A depleted rats
retinoic acid
-
restores normal level of liver LRAT activity in vitamin A deficient and depleted rats
retinoic acid
minimal dose for significant increase in LRAT activity and mRNA expression: 0.005 mg
Vitamin A
regulates LRAT activity in the liver but not in the small intestine
additional information
-
activation is blocked completely in vivo by cycloheximide
-
additional information
retinoic acid must be continuously present to maintain LRAT gene expression in the ON position
-
additional information
-
activation and mRNA expression for LRAT is blocked completely in vivo by actinomycin D
-
additional information
activation and mRNA expression for LRAT is blocked completely in vivo by actinomycin D
-
additional information
-
the pollutant 2,3,7,8-tetrachlorodibenzo-4-dioxin, i.e. TCDD, induces enzyme expression in the kidney, induction mechanism, the expression of the cellular retinol binding protein I is unaffected, TCDD alters the retinoid metabolism regulation, expression and activity of cytochrome P450 A1 increases retinoic acid levels in kidney and liver, and enhances enzyme expression in the kidney
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Blindness
Chemical chaperone TUDCA preserves cone photoreceptors in a mouse model of Leber congenital amaurosis.
Blindness
Cone opsin determines the time course of cone photoreceptor degeneration in Leber congenital amaurosis.
Blindness
Deletion of M-opsin prevents "M cone" degeneration in a mouse model of Leber congenital amaurosis.
Blindness
Genetic deletion of S-opsin prevents rapid cone degeneration in a mouse model of Leber congenital amaurosis.
Blindness
Low prevalence of lecithin retinol acyltransferase mutations in patients with Leber congenital amaurosis and autosomal recessive retinitis pigmentosa.
Blindness
Pathophysilogical mechanism and treatment strategies for leber congenital amaurosis.
Carcinoma
Reduced lecithin:retinol acyl transferase activity in cultured squamous cell carcinoma lines results in increased substrate-driven retinoic acid synthesis.
Carcinoma, Squamous Cell
Reduced lecithin:retinol acyl transferase activity in cultured squamous cell carcinoma lines results in increased substrate-driven retinoic acid synthesis.
Leber Congenital Amaurosis
Chemical chaperone TUDCA preserves cone photoreceptors in a mouse model of Leber congenital amaurosis.
Leber Congenital Amaurosis
Cone opsin determines the time course of cone photoreceptor degeneration in Leber congenital amaurosis.
Leber Congenital Amaurosis
Deletion of M-opsin prevents "M cone" degeneration in a mouse model of Leber congenital amaurosis.
Leber Congenital Amaurosis
Genetic deletion of S-opsin prevents rapid cone degeneration in a mouse model of Leber congenital amaurosis.
Leber Congenital Amaurosis
Low prevalence of lecithin retinol acyltransferase mutations in patients with Leber congenital amaurosis and autosomal recessive retinitis pigmentosa.
Leber Congenital Amaurosis
Pathophysilogical mechanism and treatment strategies for leber congenital amaurosis.
Melanoma
Knockdown of lecithin retinol acyltransferase increases all-trans retinoic acid levels and restores retinoid sensitivity in malignant melanoma cells.
Melanoma
Lecithin retinol acyltransferase as a potential prognostic marker for malignant melanoma.
Neoplasm Metastasis
Lecithin retinol acyltransferase as a potential prognostic marker for malignant melanoma.
Neoplasms
Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes.
Neoplasms
Expression of the interleukin-4 receptor alpha in human conjunctival epithelial cells.
Neoplasms
Platelet-derived growth factor receptor ? in hepatocellular carcinoma is a prognostic marker independent of underlying liver cirrhosis.
Neoplasms
Reduced lecithin: retinol acyltransferase expression correlates with increased pathologic tumor stage in bladder cancer.
Nevus, Pigmented
Lecithin retinol acyltransferase as a potential prognostic marker for malignant melanoma.
Obesity
The association of lecithin retinol acyltransferase and the 25(OH)D receptor with pediatric overweight and obesity.
Overweight
The association of lecithin retinol acyltransferase and the 25(OH)D receptor with pediatric overweight and obesity.
Pediatric Obesity
The association of lecithin retinol acyltransferase and the 25(OH)D receptor with pediatric overweight and obesity.
Retinal Degeneration
Genomic organization and mutation analysis of the gene encoding lecithin retinol acyltransferase in human retinal pigment epithelium.
Retinal Dystrophies
Cone opsin determines the time course of cone photoreceptor degeneration in Leber congenital amaurosis.
Retinal Dystrophies
Early onset retinal dystrophy due to mutations in LRAT: molecular analysis and detailed phenotypic study.
Retinal Dystrophies
Mutations in the gene encoding lecithin retinol acyltransferase are associated with early-onset severe retinal dystrophy.
Retinal Dystrophies
Pathophysilogical mechanism and treatment strategies for leber congenital amaurosis.
Retinitis Pigmentosa
A novel LRAT mutation affecting splicing in a family with early onset retinitis pigmentosa.
Retinitis Pigmentosa
Low prevalence of lecithin retinol acyltransferase mutations in patients with Leber congenital amaurosis and autosomal recessive retinitis pigmentosa.
Urinary Bladder Neoplasms
Reduced lecithin: retinol acyltransferase expression correlates with increased pathologic tumor stage in bladder cancer.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00024
all-trans-retinol-[cellular-retinol-binding-protein]
-
pH and temperature not specified in the publication
-
0.00024
retinol-(cellular-retinol-binding protein) type II
-
intestinal LRAT, reaction with phosphatidylcholine
-
0.0005
retinol-(cellular-retinol-binding-protein)
-
reaction with phosphatidylcholine
-
0.00032
retinol-[cellular-retinol-binding-proteintype II]
-
liver LRAT, reaction with phosphatidylcholine
-
0.0023
11-cis-retinol-[cellular retinol-binding protein]
-
pH 7.5, 37°C, retinal pigment epithelium microsomes
0.00036
all-trans-retinol
-
with dipalmitoylphosphatidylcholine, cloned enzyme, expressed in HEK-293T cells
0.00046
all-trans-retinol
-
with dipalmitoylphosphatidylcholine, chemically dimerized enzyme
0.00094
all-trans-retinol
-
with dipalmitoylphosphatidylcholine, cloned enzyme, expressed in HEK-296T cells
0.00033
all-trans-retinol-[cellular retinol-binding protein]
-
pH 7.5, 37°C, retinal pigment epithelium microsomes
0.0002
retinol-[cellular-retinol-binding-protein]
-
intestinal LRAT, reaction with phosphatidylcholine
0.00078
retinol-[cellular-retinol-binding-protein]
-
liver LRAT, reaction with phosphatidylcholine
0.001
retinol-[cellular-retinol-binding-protein]
-
liver LRAT, reaction with phosphatidylcholine
additional information
additional information
-
steady-state kinetic analysis using purified truncated mutant tLRAT
-
additional information
additional information
the water-soluble phospholipid:retinol molar ratio is very critical in the assay. It should be equal to at least 12.5:1 to allow proper solubilization of retinol by water-soluble phospholipid. A water-soluble phospholipid:tLRAT molar ratio of 4200000:1 should not be exceeded, otherwise a large decrease in activity occurs
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000001
-
nonparenchymal cell fraction LRAT activity and hepatocyte cell fraction LRAT activity for vitamin A-deficient rats
0.0000012
-
hepatocyte cell fraction LRAT activity for vitamin A-deficient rats treated with retinoic acid
0.0000054
-
hepatocyte cell fraction LRAT activity for vitamin A-deficient rats treated with N-(4-hydroxyphenyl)-retinamide
0.0000132
-
nonparenchymal cell fraction LRAT activity for vitamin A-deficient rats treated with retinoic acid
0.0000309
-
nonparenchymal cell fraction LRAT activity for vitamin A-sufficient rats
0.0000401
-
vitamin A-deficient rats treated intraperitoneally with retinoic acid
0.0000415
-
vitamin A-deficient rats treated intraperitoneally with retinol
0.0000553
-
nonparenchymal cell fraction LRAT activity for vitamin A-deficient rats treated with N-(4-hydroxyphenyl)-retinamide
0.166
-
11-cis-retinyl ester synthesis in presence of cellular retinol-binding protein
additional information
additional information
activity of recombinant mutant enzymes and recombinant truncated wild-type, overview
additional information
-
retinoid levels in tissues of wild-type and enzyme-deficient mice, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5 - 8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH profile of recombinant mutant enzymes and recombinant truncated wild-type
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in the glomeruli of normal, neoplastic kidney sections
brenda
-
breast carcinoma cells have lower LRAT activity
brenda
-
neoplastic and adjacent, non-neoplastic glandular breast tissue specimens from human patients, expression analysis, reduced enzyme expression, LRAT protein progressively decreases with a reduction in the degree of tumor differentiation in invasive breast carcinomas, overview
brenda
-
LRAT acts together with Cyp26A1, one of the enzymes that catalyze the degradation of retinoic acid, and possibly with STRA6, the cell surface receptor for retinol-retinol-binding protein, in maintaining adequate levels of retinoids in embryonic and extraembryonic tissues
brenda
additional information
-
expression in lens and lens epithelium and fibers from embryo to adulthood
brenda
the enzyme is distributed in both hepatic stellate cells and endothelial cells of normal rodent and human liver
brenda
-
the enzyme is distributed in both hepatic stellate cells and endothelial cells of normal rodent and human liver
brenda
-
nonparenchymal cells LRAT activity is approximately 10 fold greater than the hepatocyte LRAT activity from both vitamin A-sufficient and retinoid acid treated vitamin A-depleted rats
brenda
LRAT and cellular retinol-binding protein CRBP I are well colocalized within the liver lobules of polar bears
brenda
-
GATA transcription factors are involved in the transcriptional activation of LRAT in normal human prostate epithelial cells
brenda
-
adenocarcinoma, LRAT is downregulated as a result of oncogenic transformation
brenda
-
transcriptional regulation of the human LRAT gene is aberrant in human prostate cancer cells
brenda
-
-
brenda
hepatic stellate cells shift their retinyl ester synthesizing capacity from LRAT to acyl-CoA:diacylglycerol acyltransferase DGAT1 during activation
brenda
hepatic stellate cells shift their retinyl ester synthesizing capacity from LRAT to acyl-CoA:diacylglycerol acyltransferase DGAT1 during activation
brenda
-
expression both in Sertoli and in spermatocytes marking initiation of spermatogenesis in prepubertal mice
brenda
additional information
-
renal tissue expression pattern, expression is higher in renal tumor than in normal tissue
brenda
additional information
expression of multiple mRNAs in a tissue-specific manner
brenda
additional information
-
determination of retinoid levels in liver, blood, and lung of wild-type and knockout mutant mice
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
upon initiating retinyl ester biosynthesis in cells, Crpb1 remains with MAM, and both Crbp1 and MAM re-localize with LRAT. LRAT formed rings around the growing lipid droplets. LRAT-containing rings colocalize with the lipid-droplet surface proteins, desnutrin/adipose triglyceride lipase and perilipin 2. Colocalization with lipid droplets requires the 38 N-terminal amino acid residues of LRAT, and specifically K36 and R38. Formation of rings around the growing lipid droplets does not require functional microtubules
brenda
-
before initiation of retinyl ester biosynthesis, LRAT distributes throughout the endoplasmic reticulum, and Crpb1 localizes with mitochondria associated membranes, surrounded by LRAT. Upon initiating retinyl ester biosynthesis in cells, Crpb1 remains with MAM, and both Crbp1 and MAM re-localize with LRAT. LRAT formed rings around the growing lipid droplets
brenda
-
LRATis a single membrane-spanning protein with an N-terminal domain that faces the cytoplasm, C-terminal luminal orientation, membrane topology, overview
brenda
-
LRAT is localized to the membrane of the LRAT is localized to the membrane of the endoplasmic reticulum. Single membrane-spanning protein with an N-terminal domain that faces the cytoplasm
brenda
-
bound, membrane topology model of LRAT using I-TASSER, membrane interaction probes of LRAT and truncated LRAT with phospholipid monolayers, circular dichroism, overview
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
as retinol, by its metabolite retinoic acid, stimulates fibroblasts to synthesize collagen fibres and inhibits collagen-degrading enzymes, the inhibition of LRAT presents an strategy for anti-ageing ingredients by increasing the available retinol in the skin
evolution
malfunction
metabolism
-
the key step of vitamin A metabolism is the esterification of all-trans retinol, catalyzed by lecithin/retinol acyltransferase, LRAT. Vitamin A metabolism in benign and malignant melanocytic skin cells with regard to expression, functional activity of LRAT, RPE65, and cRBP2 and their regulation, overview
physiological function
additional information
evolution
-
based on its secondary structure LRAT belongs to a superfamily of enzymes generically referred as NIpC/P60. Within this superfamily, a multiple sequence alignment of LRAT and LRAT-like family members shows that they share three conserved amino acid residues; cysteine, histidine and a polar residue that is thought to complete a catalytic triad similar to the papain-like thiol peptidases
evolution
-
based on its secondary structure LRAT belongs to a superfamily of enzymes generically referred as NIpC/P60. Within this superfamily, a multiple sequence alignment of LRAT and LRAT-like family members shows that they share three conserved amino acid residues; cysteine, histidine and a polar residue that is thought to complete a catalytic triad similar to the papain-like thiol peptidases
malfunction
-
a truncated form of LRAT as well as its S175R mutant lead to retinis pigmentosa, a severe form of retinal dystrophy
malfunction
-
vitamin A uptake from recombinant holo-retinol-binding protein exhibited by wild-type mice is impaired in Lrat-deficient mice. Lrat-/- mice show elevated cellular vitamin A-binding protein 1, CRBP1, protein in the liver, lung, and adipose tissue as compared with wild type control animals
malfunction
-
homozygous mutation S175R occurs in two patients diagnosed with severe early-onset retinal degeneration
malfunction
-
generation of an animal model in which the lrat gene is disrupted by homologous recombination gives Lrat-/- mice, which show slow degeneration of their retinas, essentially a shortening of rod outer segments and highly attenuated electroretinograms
malfunction
Lrat-/- mice lack the retinyl ester storage in large lipid droplets in hepatic stellate cells
malfunction
Mycobacterium tuberculosis infection is exacerbated in mice lacking lecithin:retinol acyltransferase. Mce lacking LRAT are potentially at increased risk for an aggravated response to Mycobacterium tuberculosis infection because of their lower lung retonol levels
malfunction
Mus musculus C57/BL6J / 129 Sv
-
vitamin A uptake from recombinant holo-retinol-binding protein exhibited by wild-type mice is impaired in Lrat-deficient mice. Lrat-/- mice show elevated cellular vitamin A-binding protein 1, CRBP1, protein in the liver, lung, and adipose tissue as compared with wild type control animals
-
physiological function
-
downregulation of LRAT expression in rat hepatic stellate cells is required for mobilization of retinyl ester in liver injury for tissue repair and wound healing, interleukin-1 is a potent suppressor of LRAT with a hierarchy role in the transcriptional regulation, interleukin-1 does not regulate the stability of LRAT protein. Interleukin-1 is a key mediator to down-regulate LRAT in liver injury
physiological function
-
relationship between LRAT and Crbp1 during retinyl ester biosynthesis in which mitochondria associated membranes-associated Crpb1 and LRAT colocalize, and both surround the growing retinyl ester-containing lipid droplet. The N-terminus of LRAT, especially K36 and R38, is essential to colocalization with the lipid droplet
physiological function
-
lecithin:retinol acyltransferase is critical for cellular uptake of vitamin A from serum retinol-binding protein, which depends on functional coupling of STRA6 with intracellular lecithin:retinol acyltransferase. Vitamin A uptake is regulated by all-trans-retinoic acid in nonocular tissues of mice. When in excess, vitamin A is rapidly taken up and converted to its inert ester form in peripheral tissues, such as lung, whereas in vitamin A deficiency, ocular retinoid uptake is favored
physiological function
-
activities of LRAT and RPE65 may be important for removal of all-trans retinal which is the substrate for retinoic acid production in skin cells. Decreasing cellular amount of retinoic acid and its precursor molecules might result in a change of gene regulation
physiological function
-
lecithin:retinol acyltransferase, LRAT, is a membrane-bound protein that plays an essential function in the visual cycle. It catalyzes the esterification of retinol into retinyl esters in the retinal pigment epithelium as well as in other tissues including testis, liver, and intestine
physiological function
-
function of LRAT is to catalyze a trans-esterification reaction that occurs between the sn-1 position of lecithin molecules in the lipid bilayer of the smooth endoplasmic reticulum and all-trans-retinol in the formation of all-trans-retinyl esters. Functional role of LRAT in the visual cycle
physiological function
-
function of LRAT is to catalyze a trans-esterification reaction that occurs between the sn-1 position of lecithin molecules in the lipid bilayer of the smooth endoplasmic reticulum and all-trans-retinol in the formation of all-trans-retinyl esters. Functional role of LRAT in the visual cycle
physiological function
quiescent LRAT knockout hepatic stellate cells retain the capacity to synthesize retinyl esters and to store neutral lipids in lipid droplets ex vivo. The median lipid droplet size in LRAT knockout hepatic stellate cells (1080 nm) is significantly smaller than in wild-type stellate cells (1618 nm). Upon prolonged (24h) incubation, the amounts of small (less than 700 nm) lipid droplets strongly increases both in wild type and in LRAT knockout hepatic stellate cells
physiological function
quiescent LRAT knockout hepatic stellate cells retain the capacity to synthesize retinyl esters and to store neutral lipids in lipid droplets ex vivo. The median lipid droplet size in LRAT knockout hepatic stellate cells (1080 nm) is significantly smaller than in wild-type stellate cells (1618 nm). Upon prolonged (24h) incubation, the amounts of small (less than 700 nm) lipid droplets strongly increases both in wild type and in LRAT knockout hepatic stellate cells
physiological function
cellular retinol-binding protein CRBP I effectively conveys retinol to the LRAT, thereby circumventing the low enzymatic activity of LRAT in polar bear livers
physiological function
retinoid isomerohydrolase RPE65 palmitoylation level is highly regulated by lecithin:retinol acyltransferase (LRAT) enzyme. In the presence of LRAT substrate all-trans retinol, there is a significant decrease in the level of palmitoylation of RPE65
physiological function
LRAT is the main enzyme producing retinyl esters in the liver
physiological function
main enzyme catalysing the esterification of retinol to retinyl esters and, hence, is of central importance for retinol homeostasis
physiological function
Mus musculus C57/BL6J / 129 Sv
-
lecithin:retinol acyltransferase is critical for cellular uptake of vitamin A from serum retinol-binding protein, which depends on functional coupling of STRA6 with intracellular lecithin:retinol acyltransferase. Vitamin A uptake is regulated by all-trans-retinoic acid in nonocular tissues of mice. When in excess, vitamin A is rapidly taken up and converted to its inert ester form in peripheral tissues, such as lung, whereas in vitamin A deficiency, ocular retinoid uptake is favored
-
additional information
-
the catalytic triad includes histidine 60, tyrosine 154 and cysteine 161 in the LRAT structure
additional information
-
malignant melanoma cells are able to esterify all-trans retinol and subsequently isomerize all-trans retinyl esters into 11-cis retinol, whereas their benign counterpart melanocytes are not able to catalyze these reactions
Show AA Sequence and Transmembrane Helices (438 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20000
25000
40000
-
nonreducing PAGE, higher aggregation, up to pentamers, occurs in absence of denaturing agents
20000
-
1 * 25000, full-length wild-type enzyme, SDS-PAGE, 1 * 20000, recombinant truncated enzyme, SDS-PAGE
20000
-
2 * 25000, full-length wild-type enzyme, SDS-PAGE, 2 * 20000, recombinant truncated enzyme, SDS-PAGE
25000
-
1 * 25000, full-length wild-type enzyme, SDS-PAGE, 1 * 20000, recombinant truncated enzyme, SDS-PAGE
25000
-
2 * 25000, full-length wild-type enzyme, SDS-PAGE, 2 * 20000, recombinant truncated enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
-
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.2 A crystal structure of HRAS-like tumor suppressor 3 /LRAT chimeric enzyme in a thioester catalytic intermediate state reveals a major structural rearrangement accompanied by 3D-domain swapping dimerization not observed in native HRASLS proteins. Structural changes affecting the active site environment contribute to slower hydrolysis of the catalytic intermediate supporting efficient acyl transfer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
K180R
site-directed mutagenesis, reduced activity compared to the truncated wild-type enzyme
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)
S175R
Y118F
site-directed mutagenesis, activity similar to the truncated wild-type enzyme
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
additional information
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
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
-
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
-
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
-
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
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
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.4
inactivation of recombinant truncated wild-type enzyme, reversible by dialysis against a buffer with pH 8.4
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
all operation involving retinoids are performed at darkness, or under red light
all operation involving retinoids are performed at darkness, or under red light
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Triton X-100
-
the high similarity between the secondary structure of tLRAT in the absence and the presence of Triton X-100 suggests that this detergent has no detectable effect on the structure of this protein
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 20 mM Tris-HCl pH 9, 2 mM dithiothreitol, 1 mM EDTA, 0.1% Triton X-100, 0.1 mg/ml dipalmitoylphosphatidylcholine, NaCl, stable for months
-
-80°C, 10 mM Tris acetate, pH 7, 1 mM dithiothreitol, microsomal fraction, stable for at least 6 months
-
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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
-
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 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 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
-
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
-
native enzyme partially by membrane preparation from retinal pigment epithelium
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis of the full length gene including the 3'- and 5'-ends, genetic organization analysis, at least 2 splicing variants, the second of which lacks a 103 nt polynucleotide in the 5'-UTR of the full length transcript
expression in HEK-293T cells
expression of a truncated enzyme form lacking the transmembrane N- and C-termini in Escherichia coli as His-tagged protein, which is insoluble in absence of detergents
-
expression of His-tagged truncated wild-type enzyme and His-tagged mutant enzymes in Escherichia coli strain BL21(DE3)
expression of wild-type and/or mutant enzymes inducibly in HEK-293 cells, transiently in COS-7 cells, and in Escherichia coli strain BL21(DE3) cells
-
inducible expression of LRAT in HEK-293S cells
LRAT, quantitative real-time RT-PCR expression analysis in melanoma cell lines
-
stable expression in HEK-293T cells
stable expression of GFP-tagged LRAT in CHO cells and of GFP-tagged LRAT in COS7 cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of Lrat is strongly decreased (about 63fold) upon growth on plastic for 7 days. Hepatic stellate cells cultured in gel show about 2.6fold reduction in Lrat expression
interleukin-1 can potently downregulate mRNA and protein levels of LRAT and act as injury signal resulting in mobilization of retinyl esters in primary rat hepatic stellate cells. Secreted factors from Kupffer cells are able to suppress LRAT expression in hepatic stellate cells, which is neutralized by interleukin-1 receptor antagonist. The regulation is likely at transcriptional level. Interleukin-1 fails to downregulate recombinant LRAT protein expressed in the cells by adenovirus, while transcription of endogenous LRAT is promptly decreased. Interleukin-1 is a key mediator to down-regulate LRAT in liver injury
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
ARPE-19 cell system is appropriate for studying the visual cycle enzymes
diagnostics
medicine
diagnostics
-
enzyme might be a prognostic or therapeutic marker in renal cancer
diagnostics
-
the Lrat knockout mutant mice may serve as animal model with early onset severe retinal dystrophy and severe retinyl ester deprivation
medicine
-
LRAT mutations are likely a rare cause of Leber congenital amaurosis among patients from North America
medicine
-
study on the effects of ectopic expression of human lecithin:retinol acyltransferase on murine oral cavity carcinogenesis induced by the carcinogen 4-nitroquinoline 1-oxide. In transgenic mice with targeted human LRAT expression to the basal layer of mouse skin and oral cavity epithelia, the retinyl ester levels in skin are 32% greater than those in wild-type mice, and topical treatment of the back skin with retinol results in greater increases in retinyl esters than in wild-type mouse skin. While 4-nitroquinoline 1-oxide treatment induces multifocal precancerous and cancer lesions in the tongues of both transgene positive and negative mice, higher percentages of transgene positive mice develop more severe tongue lesions of grades 3 and 4 than transgene negative mice after 4-nitroquinoline 1-oxide treatment. Carcinogen treatment also results in greater percentages of transgene positive mouse tongues with hyperplasia, dysplasia, and carcinoma than transgene negative mouse tongues. There are higher cyclooxygenase-2 and lower RARbeta(2) mRNA levels in transgene positive mouse tongues as compared to wild-type mouse tongues after 4-nitroquinoline 1-oxide treatment
medicine
-
expression of RPE65 involved in vitamin A metabolism is downregulated in malignant melanoma compared with benign melanocytic nevi. In contrast, expression of LRAT is not significantly different. High LRAT expression in melanoma metastases is inversely correlated with patient survival, Kaplan-Meier analysis reveals earlier melanoma-related death
medicine
among overweight/obese and lean children (aged 6-12 years), LRAT expression is remarkably lower in the overweight/obese group than in the lean group. Compared with the lean group, the overweight/obese group has elevated vitamin A level. The levels of 25-hydroxyvitamin D and its receptor are lower in overweight/obese subjects than in lean subjects. LRAT is negatively correlated with body mass index and waist circumference and positively correlated with high-density lipoprotein
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AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saari, J.C.; Bredberg, D.L.
Acyl-CoA:retinol acyltransferase and lecithin:retinol acyltransferase activities of bovine retinal pigment epithelial microsomes
Methods Enzymol.
190
156-163
1990
Bos taurus, Rattus norvegicus
brenda
Saari, J.C.; Bredberg, D.L.
Lecithin:retinol acyltransferase in retinal pigment epithelial microsomes
J. Biol. Chem.
264
8636-8640
1989
Bos taurus
brenda
MacDonald, P.N.; Ong, D.E.
Evidence for a lecithin-retinol acyltransferase activity in the rat small intestine
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263
12478-12482
1988
Rattus norvegicus
brenda
Shi, Y.Q.; Hubacek, I.; Rando, R.R.
Kinetic mechanism of lecithin retinol acyl transferase
Biochemistry
32
1257-1263
1993
Bos taurus
brenda
Herr, F.M.; Ong, D.E.
Differential interaction of lecithin-retinol acyltransferase with cellular retinol binding proteins
Biochemistry
31
6748-6755
1992
Rattus norvegicus
brenda
MacDonald, P.N.; Ong, D.E.
A lecithin:retinol acyltransferase activity in human and rat liver
Biochem. Biophys. Res. Commun.
156
157-163
1988
Homo sapiens, Rattus norvegicus
brenda
Matsuura, T.; Ross, A.C.
Regulation of hepatic lecithin:retinol acyltransferase activity by retinoic acid
Arch. Biochem. Biophys.
301
221-227
1993
Rattus norvegicus
brenda
Saari, J.C.; Bredberg, D.L.; Farrell, D.F.
Retinol esterification in bovine retinal pigment epithelium: reversibility of lecithin:retinol acyltransferase
Biochem. J.
291
697-700
1993
Bos taurus
-
brenda
Matsuura, T.; Gad, M.Z.; Harrison, E.H.; Ross, A.C.
Lecithin:retinol acyltransferase and retinyl ester hydrolase activities are differentially regulated by retinoids and have distinct distributions between hepatocyte and nonparenchymal cell fractions of rat liver
J. Nutr.
127
218-224
1997
Rattus norvegicus
brenda
Ruiz, A.; Winston, A.; Lim, Y.H.; Gilbert, B.A.; Rando, R.R.; Bok, D.
Molecular and biochemical characterization of lecithin retinol acyltransferase
J. Biol. Chem.
274
3834-3841
1999
Bos taurus, Homo sapiens (O95237), Homo sapiens
brenda
Mondal, M.S.; Ruiz, A.; Bok, D.; Rando, R.R.
Lecithin retinol acyltransferase contains cysteine residues essential for catalysis
Biochemistry
39
5215-5220
2000
Homo sapiens
brenda
Zolfaghari, R.; Ross, A.C.
Lecithin:retinol acyltransferase from mouse and rat liver: cDNA cloning and liver-specific regulation by dietary vitamin A and retinoic acid
J. Lipid Res.
41
2024-2034
2000
Mus musculus (Q9JI60), Rattus norvegicus (Q9JI61)
brenda
Ruiz, A.; Bok, D.
Molecular characterization of lecithin-retinol acyltransferase
Methods Enzymol.
316
400-413
2000
Bos taurus, Homo sapiens
brenda
Mondal, M.S.; Ruiz, A.; Hu, J.; Bok, D.; Rando, R.R.
Two histidine residues are essential for catalysis by lecithin retinol acyl transferase
FEBS Lett.
489
14-18
2001
Bos taurus, Homo sapiens
brenda
Guo, X.; Knudsen, B.S.; Peehl, D.M.; Ruiz, A.; Bok, D.; Rando, R.R.; Rhim, J.S.; Nanus, D.M.; Gudas, L.J.
Retinol metabolism and lecithin:retinol acyltransferase levels are reduced in cultured human prostate cancer cells and tissue specimens
Cancer Res.
62
1654-1661
2002
Homo sapiens
brenda
Jahng, W.J.; Cheung, E.; Rando, R.R.
Lecithin retinol acyltransferase forms functional homodimers
Biochemistry
41
6311-6319
2002
Bos taurus
brenda
Zolfaghari, R.; Wang, Y.; Chen, Q.; Sancher, A.; Ross, A.C.
Cloning and molecular expression analysis of large and small lecithin:retinol acyltransferase mRNAs in the liver and other tissues of adult rats
Biochem. J.
368
621-631
2002
Rattus norvegicus (Q9JI61)
brenda
Rando, R.R.
Membrane-bound lecithin-retinol acyltransferase
Biochem. Biophys. Res. Commun.
292
1243-1250
2002
Bos taurus, Rattus norvegicus, Homo sapiens
brenda
Jahng, W.J.; Xue, L.; Rando, R.R.
Lecithin retinol acyltransferase is a founder member of a novel family of enzymes
Biochemistry
42
12805-12812
2003
Homo sapiens (O95237)
brenda
Bok, D.; Ruiz, A.; Yaron, O.; Jahng, W.J.; Ray, A.; Xue, L.; Rando, R.R.
Purification and characterization of a transmembrane domain-deleted form of lecithin retinol acyltransferase
Biochemistry
42
6090-6098
2003
Homo sapiens
brenda
Xue, L.; Rando, R.R.
Roles of cysteine 161 and tyrosine 154 in the lecithin-retinol acyltransferase mechanism
Biochemistry
43
6120-6126
2004
Homo sapiens (O95237)
brenda
Hoegberg, P.; Schmidt, C.K.; Nau, H.; Catharine Ross, A.; Zolfaghari, R.; Fletcher, N.; Trossvik, C.; Nilsson, C.B.; Hakansson, H.
2,3,7,8-Tetrachlorodibenzo-p-dioxin induces lecithin: retinol acyltransferase transcription in the rat kidney
Chem. Biol. Interact.
145
1-16
2003
Rattus norvegicus
brenda
Zhan, H.C.; Gudas, L.J.; Bok, D.; Rando, R.; Nanus, D.M.; Tickoo, S.K.
Differential expression of the enzyme that esterifies retinol, lecithin:retinol acyltransferase, in subtypes of human renal cancer and normal kidney
Clin. Cancer Res.
9
4897-4905
2003
Homo sapiens
brenda
Trevino, S.G.; Schuschereba, S.T.; Bowman, P.D.; Tsin, A.
Lecithin:retinol acyltransferase in ARPE-19
Exp. Eye Res.
80
897-900
2005
Homo sapiens, no activity in Gallus gallus
brenda
Kaschula, C.H.; Jin, M.H.; Desmond-Smith, N.S.; Travis, G.H.
Acyl CoA:retinol acyltransferase (ARAT) activity is present in bovine retinal pigment epithelium
Exp. Eye Res.
82
111-121
2005
Bos taurus
brenda
Zolfaghari, R.; Ross, A.C.
Cloning, gene organization and identification of an alternative splicing process in lecithin:retinol acyltransferase cDNA from human liver
Gene
341
181-188
2004
Homo sapiens (O95237)
brenda
Batten, M.L.; Imanishi, Y.; Maeda, T.; Tu, D.C.; Moise, A.R.; Bronson, D.; Possin, D.; Van Gelder, R.N.; Baehr, W.; Palczewski, K.
Lecithin-retinol acyltransferase is essential for accumulation of all-trans-retinyl esters in the eye and in the liver
J. Biol. Chem.
279
10422-10432
2004
Mus musculus
brenda
Muniz, A.; Villazana-Espinoza, E.T.; Thackeray, B.; Tsin, A.T.
11-cis-Acyl-CoA:retinol O-acyltransferase activity in the primary culture of chicken Muller cells
Biochemistry
45
12265-12273
2006
Gallus gallus
brenda
Sheren-Manoff, M.; Shin, S.J.; Su, D.; Bok, D.; Rando, R.R.; Gudas, L.J.
Reduced lecithin:retinol acyltransferase expression in human breast cancer
Int. J. Oncol.
29
1193-1199
2006
Homo sapiens
brenda
Piantedosi, R.; Ghyselinck, N.; Blaner, W.S.; Vogel, S.
Cellular retinol-binding protein type III is needed for retinoid incorporation into milk
J. Biol. Chem.
280
24286-24292
2005
Mus musculus, Mus musculus C57/BL6J
brenda
O'Byrne, S.M.; Wongsiriroj, N.; Libien, J.; Vogel, S.; Goldberg, I.J.; Baehr, W.; Palczewski, K.; Blaner, W.S.
Retinoid absorption and storage is impaired in mice lacking lecithin:retinol acyltransferase (LRAT)
J. Biol. Chem.
280
35647-35657
2005
Mus musculus
brenda
Golczak, M.; Imanishi, Y.; Kuksa, V.; Maeda, T.; Kubota, R.; Palczewski, K.
Lecithin:retinol acyltransferase is responsible for amidation of retinylamine, a potent inhibitor of the retinoid cycle
J. Biol. Chem.
280
42263-42273
2005
Mus musculus, Bos taurus
brenda
Moise, A.R.; Golczak, M.; Imanishi, Y.; Palczewski, K.
Topology and membrane association of lecithin: retinol acyltransferase
J. Biol. Chem.
282
2081-2090
2007
Mus musculus
brenda
Jin, M.; Yuan, Q.; Li, S.; Travis, G.H.
Role of LRAT on the retinoid isomerase activity and membrane association of Rpe65
J. Biol. Chem.
282
20915-20924
2007
Bos taurus, Mus musculus, Mus musculus 129S2/Sv
brenda
Sweeney, M.O.; McGee, T.L.; Berson, E.L.; Dryja, T.P.
Low prevalence of lecithin retinol acyltransferase mutations in patients with Leber congenital amaurosis and autosomal recessive retinitis pigmentosa
Mol. Vis.
13
588-593
2007
Homo sapiens
brenda
Liu, L.; Tang, X.H.; Gudas, L.J.
Homeostasis of retinol in lecithin: retinol acyltransferase gene knockout mice fed a high retinol diet
Biochem. Pharmacol.
75
2316-2324
2008
Mus musculus (Q9JI60)
brenda
Bussieres, S.; Buffeteau, T.; Desbat, B.; Breton, R.; Salesse, C.
Secondary structure of a truncated form of lecithin retinol acyltransferase in solution and evidence for its binding and hydrolytic action in monolayers
Biochim. Biophys. Acta
1778
1324-1334
2008
Escherichia coli BL21
brenda
Cai, K.; Gudas, L.J.
Retinoic acid receptors and GATA transcription factors activate the transcription of the human lecithin:retinol acyltransferase gene
Int. J. Biochem. Cell Biol.
41
546-553
2009
Homo sapiens
brenda
Kim, Y.K.; Wassef, L.; Hamberger, L.; Piantedosi, R.; Palczewski, K.; Blaner, W.S.; Quadro, L.
Retinyl ester formation by lecithin: retinol acyltransferase is a key regulator of retinoid homeostasis in mouse embryogenesis
J. Biol. Chem.
283
5611-5621
2008
Mus musculus
brenda
Nagatsuma, K.; Hayashi, Y.; Hano, H.; Sagara, H.; Murakami, K.; Saito, M.; Masaki, T.; Lu, T.; Tanaka, M.; Enzan, H.; Aizawa, Y.; Tajiri, H.; Matsuura, T.
Lecithin: retinol acyltransferase protein is distributed in both hepatic stellate cells and endothelial cells of normal rodent and human liver
Liver Int.
29
47-54
2009
Homo sapiens (O95237), Homo sapiens, Mus musculus
brenda
Tang, X.H.; Su, D.; Albert, M.; Scognamiglio, T.; Gudas, L.J.
Overexpression of lecithin:retinol acyltransferase in the epithelial basal layer makes mice more sensitive to oral cavity carcinogenesis induced by a carcinogen
Cancer Biol. Ther.
8
1212-1213
2009
Homo sapiens
brenda
Amann, P.M.; Luo, C.; Owen, R.W.; Hofmann, C.; Freudenberger, M.; Schadendorf, D.; Eichmueller, S.B.; Bazhin, A.V.
Vitamin A metabolism in benign and malignant melanocytic skin cells: importance of lecithin/retinol acyltransferase and RPE65
J. Cell. Physiol.
227
718-728
2012
Homo sapiens
brenda
Jiang, W.; Napoli, J.L.
Reorganization of cellular retinol-binding protein type 1 and lecithin:retinol acyltransferase during retinyl ester biosynthesis
Biochim. Biophys. Acta
1820
859-869
2012
Homo sapiens
brenda
Ruiz, A.; Bok, D.
Focus on molecules: lecithin retinol acyltransferase
Exp. Eye Res.
90
186-187
2010
Homo sapiens, Mus musculus
brenda
Bussieres, S.; Cantin, L.; Salesse, C.
Lecithin retinol acyltransferase and its S175R mutant have a similar secondary structure content and maximum insertion pressure but different enzyme activities
Exp. Eye Res.
93
778-781
2011
Homo sapiens
brenda
Amengual, J.; Golczak, M.; Palczewski, K.; von Lintig, J.
Lecithin:retinol acyltransferase is critical for cellular uptake of vitamin A from serum retinol-binding protein
J. Biol. Chem.
287
24216-24227
2012
Mus musculus, Mus musculus C57/BL6J / 129 Sv
brenda
Bussieres, S.; Cantin, L.; Desbat, B.; Salesse, C.
Binding of a truncated form of lecithin:retinol acyltransferase and its N- and C-terminal peptides to lipid monolayers
Langmuir
28
3516-3523
2012
Homo sapiens
brenda
Kida, Y.; Xia, Z.; Zheng, S.; Mordwinkin, N.M.; Louie, S.G.; Zheng, S.G.; Feng, M.; Shi, H.; Duan, Z.; Han, Y.P.
Interleukin-1 as an injury signal mobilizes retinyl esters in hepatic stellate cells through down regulation of lecithin retinol acyltransferase
PLoS ONE
6
e26644
2011
Rattus norvegicus
brenda
Horchani, H.; Bussires, S.; Cantin, L.; Lhor, M.; Lalibert-Gemme, J.S.; Breton, R.; Salesse C.
Enzymatic activity of lecithin:retinol acyltransferase: a thermostable and highly active enzyme with a likely mode of interfacial activation
Biochim. Biophys. Acta
1844
1128-1836
2014
Homo sapiens (O95237)
brenda
Hassel, J.C.; Amann, P.M.; Schadendorf, D.; Eichmueller, S.B.; Nagler, M.; Bazhin, A.V.
Lecithin retinol acyltransferase as a potential prognostic marker for malignant melanoma
Exp. Dermatol.
22
757-759
2013
Homo sapiens
brenda
Golczak, M.; Sears, A.E.; Kiser, P.D.; Palczewski, K.
LRAT-specific domain facilitates vitamin A metabolism by domain swapping in HRASLS3
Nat. Chem. Biol.
11
26-32
2015
Mus musculus (Q9JI60)
brenda
Prukova, D.; Ileninova, Z.; Antosova, B.; Kasparek, P.; Gregor, M.; Sedlacek, R.
Transgenic reporter mice with promoter region of murine LRAT specifically marks lens and meiosis spermatocytes
Physiol. Res.
64
247-254
2015
Mus musculus
brenda
Gauthier, M.E.; Roy, S.; Cantin, L.; Salesse, C.
Comparison between the enzymatic activity, structure and substrate binding of mouse and human lecithin retinol acyltransferase
Biochem. Biophys. Res. Commun.
519
832-837
2019
Homo sapiens (O95237), Homo sapiens, Mus musculus (Q9JI60), Mus musculus
brenda
Chelstowska, S.; Widjaja-Adhi, M.A.K.; Silvaroli, J.A.; Golczak, M.
Impact of LCA-associated E14L LRAT mutation on protein stability and retinoid homeostasis
Biochemistry
56
4489-4499
2017
Homo sapiens (O95237)
brenda
Ajat, M.; Molenaar, M.; Brouwers, J.F.H.M.; Vaandrager, A.B.; Houweling, M.; Helms, J.B.
Hepatic stellate cells retain the capacity to synthesize retinyl esters and to store neutral lipids in small lipid droplets in the absence of LRAT
Biochim. Biophys. Acta
1862
176-187
2017
Mus musculus (Q9JI60), Homo sapiens (O95237)
brenda
Liang, X.; He, Y.; Chen, M.; Ping, Q.; Chen, J.
The association of lecithin retinol acyltransferase and the 25(OH)D receptor with pediatric overweight and obesity
Eur. J. Clin. Nutr.
73
1626-1629
2019
Homo sapiens (O95237), Homo sapiens
brenda
Mezaki, Y.; Nagatsuma, K.; Yokoyama, H.; Park, J.; Nakamura, M.; Masaki, T.; Blomhoff, R.; Senoo, H.; Matsuura, T.
Biochemical and histochemical analyses of lecithin retinol acyltransferase from polar bear (Ursus maritimus) livers
Polar Biol.
41
805-815
2018
Ursus maritimus (A0A384BN88)
-
brenda
Uppal, S.; Liu, T.; Poliakov, E.; Gentleman, S.; Redmond, T.M.
The dual roles of RPE65 S-palmitoylation in membrane association and visual cycle function
Sci. Rep.
9
5218
2019
Bos taurus (Q9BGL2)
brenda
Trasino, S.; Tang, X.; Trujillo, C.; Andres, J.; Ehrt, S.; Gudas, L.
Mycobacterium tuberculosis infection is exacerbated in mice lacking lecithin retinol acyltransferase
Biochim. Biophys. Acta Mol. Basis Dis.
1866
165909
2020
Mus musculus (Q9JI60)
brenda
Haaker, M.W.; Goossens, V.; Hoogland, N.A.N.; van Doorne, H.; Wang, Z.; Jansen, J.W.A.; Kaloyanova, D.V.; van de Lest, C.H.A.; Houweling, M.; Vaandrager, A.B.; Helms, J.B.
Early activation of hepatic stellate cells induces rapid initiation of retinyl ester breakdown while maintaining lecithin retinol acyltransferase (LRAT) activity
Biochim. Biophys. Acta Mol. Cell Biol. Lipids
1869
159540
2024
Mus musculus (Q9JI60)
brenda
Imfeld, D.; Fischer, A.; Budel, L.; Stoll, C.; Schuetz, R.; Rawlings, A.V.
Boosting of retinol activity using novel lecithin Retinol acyltransferase inhibitors
Int. J. Cosmet. Sci.
46
544-552
2024
Homo sapiens (O95237)
brenda
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