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Information on EC 2.3.1.135 - phosphatidylcholine-retinol O-acyltransferase and Organism(s) Mus musculus and UniProt Accession Q9JI60
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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
-
11-cis-retinoids
- medicine
-
crbp-i
- diagnostics
- analysis
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyltransferase, lecithin-retinol
-
-
-
-
lecithin retinol acyl transferase
-
-
-
-
lecithin-retinol acyltransferase
lecithin:retinol acyltransferase
LRAT
retinyl ester synthase
-
-
-
-
lecithin-retinol acyltransferase
-
-
-
-
lecithin:retinol acyltransferase
-
-
-
-
LRAT
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY
117444-03-8
-
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
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
-
-
?
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]
-
-
-
-
?
phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
-
-
r
phosphatidylcholine + 11-cis-retinoll-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
-
-
r
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
phosphatidylcholine + retinylamine
2-acylglycerophosphocholine + fatty acid N-retinylamide
-
-
product identification
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
-
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
fatty acid retinyl esters are the storage form of vitamin A, all-trans-retinol, and serve as metabolic intermediates in the formation of the visual chromophore 11-cis-retinal, LRAT catalyzes the synthesis of retinyl esters, thereby drawing retinol from the circulation to storage depots
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
the enzyme is responsible for catalyzing retinyl ester formation from retinol
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
retinol bound to cellular retinol-binding protein III, CRBP-III, is an excellent substrate for lecithin-retinol acyltransferase
-
-
?
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-[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 + 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
-
-
?
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
?
-
-
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
-
-
?
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
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
-
-
?
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]
-
-
-
-
?
phosphatidylcholine + 11-cis-retinoll-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein]
-
trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate.
-
-
r
phosphatidylcholine + all-trans-retinol
2-acylglycerophosphocholine + 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-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
-
-
-
?
phosphatidylcholine + retinylamine
2-acylglycerophosphocholine + fatty acid N-retinylamide
-
-
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
fatty acid retinyl esters are the storage form of vitamin A, all-trans-retinol, and serve as metabolic intermediates in the formation of the visual chromophore 11-cis-retinal, LRAT catalyzes the synthesis of retinyl esters, thereby drawing retinol from the circulation to storage depots
-
-
?
lecithin + retinol-[cellular retinol-binding protein III]
2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
the enzyme is responsible for catalyzing retinyl ester formation from retinol
-
-
?
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
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
?
-
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
retinoid levels in tissues of wild-type and enzyme-deficient mice, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
hepatic stellate cells shift their retinyl ester synthesizing capacity from LRAT to acyl-CoA:diacylglycerol acyltransferase DGAT1 during activation
-
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
-
expression both in Sertoli and in spermatocytes marking initiation of spermatogenesis in prepubertal mice
additional information
-
expression in lens and lens epithelium and fibers from embryo to adulthood
-
the enzyme is distributed in both hepatic stellate cells and endothelial cells of normal rodent and human liver
additional information
-
determination of retinoid levels in liver, blood, and lung of wild-type and knockout mutant mice
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
LRATis a single membrane-spanning protein with an N-terminal domain that faces the cytoplasm, C-terminal luminal orientation, membrane topology, overview
-
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
physiological function
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
-
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
-
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LRAT_MOUSE
231
1
25820
Swiss-Prot
Secretory Pathway (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
epitope mapping, the enzyme contains a C-terminal transmembrane domain
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
-
gene Lrat disruption by targeted recombination for generation of a homozygous knockout mutant, the mutant mice develop normally, but the rod outer segments in the retina are about 35% shorter than those of wild-type mice, rod and cone visual functions are severely attenuated at an early age
additional information
-
construction of Ntm LRAT, a truncation mutant lacking the putative C-terminal transmembrane domain corresponding to Met1Ser195, and Ctm LRAT, a mutant lacking the putative N-terminal transmembrane domain corresponding to Gly35Gly231, the Ntm mutant is not located in the endoplasmic reticulum membrane, but localized to small cytoplasmic structures that are distinct from the ER, while the wild-type and the Ctm mutant are localized in the membrane
additional information
-
disruption of the CRBP-III gene and generation of CRBPIII-/- mice, method, overview, [cellular retinol-binding protein III]-deficient female mice produce milk with less retinyl ester content, especially retinyl-palmitate, compared to wild-type mice, the expression of CRBP-I is increased in adipose tissue of CRBP-III-/- mice compared to the wild-type mice
additional information
-
retinoid absorption and storage is impaired in mice lacking lecithin:retinol acyltransferase, Lrat-deficient mice possess only trace amounts of retinyl esters in liver, lung, and kidney, intestinal absorption of retinol is impaired in the absence of LRAT, they possess 23fold elevated concentrations of retinyl esters in adipose tissue compared with wild type mice, they show 3-4fold upregulation in the level of cytosolic retinol-binding protein type III in adipose tissue, and a striking total absence of large lipid-containing droplets that normally store hepatic retinoid within the hepatic stellate cells, despite the absence of significant retinyl ester stores and stellate cell lipid droplets, the livers of Lrat-/- mice upon histologic analysis appear normal and show no histological signs of liver fibrosis, Lra-/- mice absorb dietary retinol primarily as free retinol in chylomicrons, phenotype, overview
additional information
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme partially by membrane preparation from retinal pigment epithelium
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
the Lrat knockout mutant mice may serve as animal model with early onset severe retinal dystrophy and severe retinyl ester deprivation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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
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
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
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
Bos taurus, Mus musculus
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
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
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)
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
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
Ruiz, A.; Bok, D.
Focus on molecules: lecithin retinol acyltransferase
Exp. Eye Res.
90
186-187
2010
Homo sapiens, Mus musculus
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
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)
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
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Mus musculus
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Comparison between the enzymatic activity, structure and substrate binding of mouse and human lecithin retinol acyltransferase
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Homo sapiens (O95237), Homo sapiens, Mus musculus (Q9JI60), Mus musculus
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
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Homo sapiens (O95237), Mus musculus (Q9JI60)
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