Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.1.135 - phosphatidylcholine-retinol O-acyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q9JI61

for references in articles please use BRENDA:EC2.3.1.135
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: Q9JI61
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
lecithin retinol acyltransferase, lecithin-retinol acyltransferase, lecithin retinol acyl transferase, lecithin:retinol acyl transferase, lecithin/retinol acyltransferase, retinyl ester synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acyltransferase, lecithin-retinol
-
-
-
-
lecithin retinol acyl transferase
-
-
-
-
lecithin retinol acyltransferase
-
-
lecithin-retinol acyltransferase
-
-
-
-
lecithin: retinol acyltransferase
-
-
lecithin:retinol acyltransferase
-
-
-
-
retinyl ester synthase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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 hide
117444-03-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
show the reaction diagram
-
-
-
?
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
show the reaction diagram
1-lauroyl-2-myristoylphosphatidylcholine + retinol-(cellular-retinol-binding-protein)type II
retinyl laurate-(cellular-retinol-binding-protein)type II + 2-myristoylphosphatidylcholine
show the reaction diagram
-
-
-
?
1-myristoyl-2-lauroylphosphatidylcholine + retinol-(cellular-retinol-binding-protein)type II
retinyl myristate-(cellular-retinol-binding-protein)type II + 2-lauroylphosphatidylcholine
show the reaction diagram
-
-
-
?
1-palmitoyl-2-decanoylphosphatidylcholine + retinol-(cellular-retinol-binding-protein)type II
retinyl palmitate-(cellular-retinol-binding-protein)type II + 2-decanoylphosphatidylcholine
show the reaction diagram
-
-
-
?
dilauroylphosphatidylcholine + retinol-(cellular retinol binding protein)type II
retinyl laurate-(cellular retinol binding protein)type II + 2-lauroyl-phosphatidylcholine
show the reaction diagram
-
-
-
?
dimyristoylphosphatidic acid + retinol-(cellular retinol binding protein) type II
retinyl myristate + myristoylphosphatidic acid
show the reaction diagram
-
little if any retinyl myristate obtained
-
?
dimyristoylphosphatidylcholine + retinol(cellular retinol binding protein)type II
retinyl myristate-(cellular retinol binding protein)type II + 2-myristoyl-phosphatidylcholine
show the reaction diagram
-
-
-
?
dimyristoylphosphatidylethanolamine + retinol-(cellular retinol binding protein) type II
retinyl myristate-(cellular retinol binding protein)type II + myristoyl-phosphatidylethanolamine
show the reaction diagram
-
little if any retinyl myristate obtained
-
?
dipalmitoylphosphatidylcholine + all-trans-retinol
all-trans-retinyl palmitate + 2-palmitoylglycerophosphocholine
show the reaction diagram
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
show the reaction diagram
phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein]
show the reaction diagram
phosphatidylcholine + retinol-(cellular-retinol-binding protein) type II
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein) type II
show the reaction diagram
phosphatidylcholine + retinol-(cellular-retinol-binding-protein)
2-acylglycerophosphocholine + retinyl ester-(cellular-retinol-binding-protein)
show the reaction diagram
phosphatidylcholine + retinol-[cellular-retinol-binding-protein type II]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein type II]
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
show the reaction diagram
-
-
-
?
phosphatidylcholine + all-trans-retinol
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
show the reaction diagram
-
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]
show the reaction diagram
-
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
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Apo-cellular-retinol-binding protein
-
-
-
N-ethylmaleimide
p-chloromercuribenzoic acid
-
0.005 mM, complete inhibition of retinol-(cellular-retinol-binding-protein)type II esterification
phenylmethylsulfonyl fluoride
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
retinoic acid
Vitamin A
regulates LRAT activity in the liver but not in the small intestine
N-(4-hydroxyphenyl)-retinamide
retinoic acid
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00044 - 0.00063
retinol
0.00024
retinol-(cellular-retinol-binding protein) type II
-
intestinal LRAT, reaction with phosphatidylcholine
-
0.00032
retinol-[cellular-retinol-binding-proteintype II]
-
liver LRAT, reaction with phosphatidylcholine
-
0.0002 - 0.001
retinol-[cellular-retinol-binding-protein]
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
0.000003
-
hepatocyte fraction LRAT activity of vitamin A-sufficient rats
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
0.00003
-
intestinal LRAT
0.0000309
-
nonparenchymal cell fraction LRAT activity for vitamin A-sufficient rats
0.000036
-
vitamin A-deficient rats treated orally with retinyl palmitate
0.0000401
-
vitamin A-deficient rats treated intraperitoneally with retinoic acid
0.0000415
-
vitamin A-deficient rats treated intraperitoneally with retinol
0.0000434
-
vitamin A-deficient rats treated orally with retinoic acid
0.0000553
-
nonparenchymal cell fraction LRAT activity for vitamin A-deficient rats treated with N-(4-hydroxyphenyl)-retinamide
0.00006
-
mammary gland LRAT
0.000094
-
testis LRAT
0.000145
-
liver LRAT
0.0021
-
liver LRAT activity in vitamin A-deficient rats
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
mRNA expression
Manually annotated by BRENDA team
mRNA expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LRAT_RAT
231
1
25810
Swiss-Prot
Secretory Pathway (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
all operation involving retinoids are performed at darkness, or under red light
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HEK-293T cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
REF.
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
Manually annotated by BRENDA team
MacDonald, P.N.; Ong, D.E.
Evidence for a lecithin-retinol acyltransferase activity in the rat small intestine
J. Biol. Chem.
263
12478-12482
1988
Rattus norvegicus
Manually annotated by BRENDA team
Herr, F.M.; Ong, D.E.
Differential interaction of lecithin-retinol acyltransferase with cellular retinol binding proteins
Biochemistry
31
6748-6755
1992
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Matsuura, T.; Ross, A.C.
Regulation of hepatic lecithin:retinol acyltransferase activity by retinoic acid
Arch. Biochem. Biophys.
301
221-227
1993
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Rando, R.R.
Membrane-bound lecithin-retinol acyltransferase
Biochem. Biophys. Res. Commun.
292
1243-1250
2002
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team