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Information on EC 2.3.1.135 - phosphatidylcholine-retinol O-acyltransferase
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2.3.1.135 phosphatidylcholine-retinol O-acyltransferaseIUBMB 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.
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Word Map
- 2.3.1.135
-
retinoids
- retinal
-
all-trans-retinyl
- opsin
- 11-cis-retinol
-
isomerohydrolase
- amaurosis
-
leber
-
s-opsins
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11-cis-retinoids
- medicine
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crbp-i
- diagnostics
- analysis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
lecithin retinol acyltransferase, lecithin-retinol acyltransferase, lecithin retinol acyl transferase, lecithin:retinol acyl transferase, lecithin/retinol acyltransferase, retinyl ester synthase, 
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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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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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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-
-
?
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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-
-
?
1-palmitoyl-2-acetyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + 2-acetyl-sn-glycerol-3-phosphorylcholine
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-
-
?
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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-
-
?
1-palmitoyl-2-linoleoyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + 2-linoleoyl-sn-glycerol-3-phosphorylcholine
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most effective substrate in stimulating palmitate transfer above control levels
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?
1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + 2-oleoyl-sn-glycerol-3-phosphorylcholine
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-
-
?
1-palmitoyl-2-stearoyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + 2-stearoyl-sn-glycerol-3-phosphorylcholine
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-
-
?
1-palmitoyl-sn-glycerol-3-phosphorylcholine + retinol
retinyl palmitate + glycerol-3-phosphorylcholine
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-
-
?
didecanoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl decanoate + 2-decanoylglycerophosphocholine
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activity is about 10% of that with diheptanoylphosphatidylcholine
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?
diheptanoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl heptanoate + 2-heptanoylglycerophosphocholine
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-
-
?
dilauroylphosphatidylcholine + all-trans-retinol
all-trans-retinyl laurate + 2-lauroylglycerophosphocholine
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activity is about 4% of that with diheptanoylphosphatidylcholine
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?
dilauroylphosphatidylcholine + retinol-(cellular retinol binding protein)type II
retinyl laurate-(cellular retinol binding protein)type II + 2-lauroyl-phosphatidylcholine
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-
-
?
dimyristoylphosphatidic acid + retinol-(cellular retinol binding protein) type II
retinyl myristate + myristoylphosphatidic acid
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little if any retinyl myristate obtained
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?
dimyristoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl myristate + 2-myristoylglycerophosphocholine
activity is about 3% of that with diheptanoylphosphatidylcholine
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-
?
dimyristoylphosphatidylcholine + retinol(cellular retinol binding protein)type II
retinyl myristate-(cellular retinol binding protein)type II + 2-myristoyl-phosphatidylcholine
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-
-
?
dimyristoylphosphatidylethanolamine + retinol-(cellular retinol binding protein) type II
retinyl myristate-(cellular retinol binding protein)type II + myristoyl-phosphatidylethanolamine
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little if any retinyl myristate obtained
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?
dioctanoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl octanoate + 2-octanoylglycerophosphocholine
activity is less than 15% of that with diheptanoylphosphatidylcholine
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-
?
dioleoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl oleate + 2-oleoylglycerophosphocholine
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-
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?
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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r
lecithin + all-trans-retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + all-trans-retinyl ester-[cellular retinol-binding protein]
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-
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r
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
palmitoyl-CoA + 11-cis-retinol-[cellular retinol-binding protein]
CoA + 11-cis-retinyl palmitate-[cellular retinol-binding protein]
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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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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trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
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r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acyl ester
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
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?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
phosphatidylcholine + all-trans-retinylamine
2-acylglycerophosphocholine + all-trans-retinyl acylamide
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-
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?
phosphatidylcholine + all-trans-retinylamine
2-acylglycerophosphocholine + fatty acid-N-all-trans-retinyl amide
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-
product identification
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?
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]
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-
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?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
phosphatidylcholine + retinylamine
2-acylglycerophosphocholine + fatty acid N-retinylamide
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-
product identification
-
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
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?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
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-
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?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
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-
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r
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
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-
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r
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
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-
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?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
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mechanistic hypothesis
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?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
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mechanistic hypothesis
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?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
mechanistic hypothesis
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r
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
activity is about 2% of that with diheptanoylphosphatidylcholine
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?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
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-
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?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
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-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
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-
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
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fatty acid retinyl esters are the storage form of vitamin A, all-trans-retinol, and serve as metabolic intermediates in the formation of the visual chromophore 11-cis-retinal, LRAT catalyzes the synthesis of retinyl esters, thereby drawing retinol from the circulation to storage depots
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-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
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the enzyme is responsible for catalyzing retinyl ester formation from retinol
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-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
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retinol bound to cellular retinol-binding protein III, CRBP-III, is an excellent substrate for lecithin-retinol acyltransferase
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-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
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the enzyme is responsible for catalyzing retinyl ester formation from retinol
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-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
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retinol bound to cellular retinol-binding protein III, CRBP-III, is an excellent substrate for lecithin-retinol acyltransferase
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?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
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-
-
-
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
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-
-
-
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
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-
-
-
?
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
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-
-
-
?
palmitoyl-CoA + 11-cis-retinol-[cellular retinol-binding protein]
CoA + 11-cis-retinyl palmitate-[cellular retinol-binding protein]
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-
-
-
?
palmitoyl-CoA + 11-cis-retinol-[cellular retinol-binding protein]
CoA + 11-cis-retinyl palmitate-[cellular retinol-binding protein]
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esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
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-
?
palmitoyl-CoA + all-trans-retinol-[cellular retinol-binding protein]
CoA + all-trans-retinyl palmitate-[cellular retinol-binding protein]
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-
-
-
?
palmitoyl-CoA + all-trans-retinol-[cellular retinol-binding protein]
CoA + all-trans-retinyl palmitate-[cellular retinol-binding protein]
-
esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
-
-
?
phosphatidylcholine + 11-cis-retinol
2-acylglycerophosphocholine + 11-cis-retinyl acyl ester
-
-
-
?
phosphatidylcholine + 11-cis-retinol
2-acylglycerophosphocholine + 11-cis-retinyl acyl ester
-
low activity
-
-
?
phosphatidylcholine + 11-cis-retinol
2-acylglycerophosphocholine + 11-cis-retinyl acyl ester
essential for generation of the precursor for 11-cis-retinal, the visual chromophore in the eye
-
-
?
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
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-
r
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
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r
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
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r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acyl ester
enzyme is involved in vitamin A storage and mobilization
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-
r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acyl ester
all-trans-retinol is vitamin A, phosphatidylcholine is lecithin
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r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acylester
-
-
-
-
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl acylester
transfer of acyl moiety from sn-1 position of lecithin, i.e. phosphatidylcholine, to vitamin A, i.e. all-trans-retinol
-
-
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl ester
-
LRAT catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
-
-
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + all-trans-retinyl ester
-
LRAT catalyzes the transfer of an acyl group, chain length C14-C18, from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
product identification
-
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + retinyl ester
-
LRAT catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
-
-
?
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + retinyl ester
-
LRAT catalyzes the transfer of an acyl group, chain length C14-C18, from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A
product identification
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
r
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
r
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
enzyme essential for the biosynthesis of 11-cis-retinal and for dietary mobilization of vitamin A
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
r
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
r
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
important role in absorption and storage of vitamin A
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
enzyme is involved in the visual cycle in the eye
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
transfer of acyl moiety from sn-1 position of lecithin, i.e. phosphatidylcholine, to vitamin A, i.e. all-trans-retinol
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
-
-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
-
-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
lecithin-retinol acyltransferase is essential for accumulation of all-trans-retinyl esters and the retinoid cycle in the eye and in the liver
-
-
?
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
-
-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
-
-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
-
enzyme and cellular retinol binding protein I, CRBP I are involved in retinoid storage regulation, retinoid biosynthetic pathway, overview
the retinyl ester is the storage form of retinoids, retinol is the precursor for retinal, which has a function as visual chromophore, and subsequently of retinoic acid, which is a signaling hormone
-
r
phosphatidylcholine + retinol-(cellular-retinol-binding protein) type II
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein) type II
-
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding protein) type II
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein) type II
-
reaction with free fatty acid, fatty acyl-CoA, phosphatidic acid or ethanolamine as acyl donors
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
r
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
renal cell carcinomata contain greatly reduced levels of retinol and retinyl esters relative to healthy kidney tissue
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
esterification of all-trans-retinol
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
refolded holo-hRBP from human serum
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
Mus musculus C57/BL6J / 129 Sv
-
-
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
Mus musculus C57/BL6J / 129 Sv
-
refolded holo-hRBP from human serum
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
additional information
?
-
-
all-trans-retinol is a far better substrate than 11-cis-retinol
-
-
?
additional information
?
-
-
the fatty acid in the 2-position is important in substrate recognition
-
-
?
additional information
?
-
-
the fatty acid in the 2-position is important in substrate recognition
-
-
?
additional information
?
-
-
the fatty acid in the 2-position is important in substrate recognition
-
-
?
additional information
?
-
-
ARAT, EC 2.3.1.76, may complement LRAT to provide additional retinyl-ester synthase activity under conditions of high all-trans-retinol
-
-
?
additional information
?
-
-
LRAT is not required for retinoid isomerase activity beyond synthesis of retinyl-ester substrate, association of Rpe65 protein, a membrane-associated protein in the retinal pigment epithelium, with membranes is neither dependent upon LRAT nor the result of S-palmitoylation on Cys231, Cys329, and Cys330 by the enzyme, overview
-
-
?
additional information
?
-
-
LRAT plays an essential role in the regeneration of visual chromophore as well as in the metabolism of vitamin A, and is responsible for amidation of retinylamine, a potent and selective inhibitor of the retinoid cycle and 11-cis-retinal biosynthesis
-
-
?
additional information
?
-
-
in presence of palmitoyl-CoA and CRALBP, Muller cell membranes synthesize 11-cis-retinyl ester from 11-cis-retinol at a rate which is 20fold higher than that of all-trans-retinyl ester, in absence of CRALBP, 11-cis-retinyl ester synthesis is greatly reduced by 7fold, in absence of palmitoyl-CoA, retinyl ester synthesis is not observed
-
-
?
additional information
?
-
-
little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
-
-
?
additional information
?
-
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
-
the fatty acid in the 2-position is important in substrate recognition
-
-
?
additional information
?
-
-
low prevalence of lecithin retinol acyltransferase mutations in patients with Leber congenital amaurosis and autosomal recessive retinitis pigmentosa
-
-
?
additional information
?
-
-
retinoids, vitamin A, i.e.retinol, and related metabolites, have been shown to be important in regulating cell growth and differentiation, retinoid signaling, overview, expression of LRAT, which converts retinol to retinyl esters, is reduced in several human carcinomas as compared with adjacent normal tissue from the same organs, LRAT protein progressively decreases with a reduction in the degree of tumor differentiation in invasive breast carcinomas, overview
-
-
?
additional information
?
-
-
the enzyme performs formation of all-trans retinyl heptanoate from all-trans-retinol and 1,2-diheptanoyl-sn-glycero-3-phosphocholine, DHPC
-
-
?
additional information
?
-
-
LRAT is not required for retinoid isomerase activity beyond synthesis of retinyl-ester substrate, association of Rpe65 protein, a membrane-associated protein in the retinal pigment epithelium, with membranes is neither dependent upon LRAT nor the result of S-palmitoylation on Cys231, Cys329, and Cys330 by the enzyme, overview
-
-
?
additional information
?
-
-
LRAT is required for retinoid storage and lipid droplet formation in hepatic stellate cells, LRAT is not the sole enzyme that catalyzes retinyl ester formation in vivo, role of LRAT in retinoid absorption and storage in different tissues, overview
-
-
?
additional information
?
-
-
LRAT plays an essential role in the regeneration of visual chromophore as well as in the metabolism of vitaminA, and is responsible for amidation of retinylamine, a potent and selective inhibitor of the retinoid cycle and 11-cis-retinal biosynthesis
-
-
?
additional information
?
-
LRAT plays a role in maintaining a stable serum retinol concentration when dietary retinol concentration fluctuates
-
-
?
additional information
?
-
-
LRAT is not required for retinoid isomerase activity beyond synthesis of retinyl-ester substrate, association of Rpe65 protein, a membrane-associated protein in the retinal pigment epithelium, with membranes is neither dependent upon LRAT nor the result of S-palmitoylation on Cys231, Cys329, and Cys330 by the enzyme, overview
-
-
?
additional information
?
-
-
little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
-
-
?
additional information
?
-
-
little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
-
-
?
additional information
?
-
-
little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
-
-
?
additional information
?
-
-
little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidylethanolamine or phosphatidic acid to retinol-(cellular-retinol-binding protein)
-
-
?
additional information
?
-
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
-
only fatty acyl group at the sn-1 is transferred
-
-
?
additional information
?
-
-
the fatty acid in the 2-position is important in substrate recognition
-
-
?
additional information
?
-
-
the fatty acid in the 2-position is important in substrate recognition
-
-
?
additional information
?
-
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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]
-
-
-
-
r
lecithin + all-trans-retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + all-trans-retinyl ester-[cellular retinol-binding protein]
-
-
-
-
r
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
lecithin + retinol-[cellular retinol-binding protein]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein]
palmitoyl-CoA + 11-cis-retinol-[cellular retinol-binding protein]
CoA + 11-cis-retinyl palmitate-[cellular retinol-binding protein]
-
esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
-
-
?
palmitoyl-CoA + all-trans-retinol-[cellular retinol-binding protein]
CoA + all-trans-retinyl palmitate-[cellular retinol-binding protein]
-
esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells
-
-
?
phosphatidylcholine + 11-cis-retinol
2-acylglycerophosphocholine + 11-cis-retinyl acyl ester
essential for generation of the precursor for 11-cis-retinal, the visual chromophore in the eye
-
-
?
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.