2.3.1.135: phosphatidylcholine-retinol O-acyltransferase
This is an abbreviated version!
For detailed information about phosphatidylcholine-retinol O-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.135
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2.3.1.135
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retinoids
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retinal
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all-trans-retinyl
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opsin
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11-cis-retinol
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isomerohydrolase
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amaurosis
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leber
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s-opsins
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11-cis-retinoids
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medicine
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crbp-i
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diagnostics
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analysis
- 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
Reaction
Synonyms
11-cis-acyl-CoA:retinol O-acyltransferase, acyltransferase, lecithin-retinol, EC 5.2.1.3, lecithin retinol acyl transferase, lecithin retinol acyltransferase, lecithin-retinol acyltransferase, lecithin/retinol acyltransferase, lecithin: retinol acyltransferase, lecithin:retinol acyl transferase, lecithin:retinol acyltransferase, LRAT, More, retinyl ester synthase, retinyl-ester synthase
ECTree
2.3.1.135 phosphatidylcholine-retinol O-acyltransferaseAdvanced search results
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results (Activating Compound
Activating Compound on EC 2.3.1.135 - phosphatidylcholine-retinol O-acyltransferase
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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
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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
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cellular retinol-binding protein
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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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N-(4-hydroxyphenyl)-retinamide
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restores normal level of LRAT activity in vitamin A depleted rats
retinoic acid
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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
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activation is blocked completely in vivo by cycloheximide
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additional information
retinoic acid must be continuously present to maintain LRAT gene expression in the ON position
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additional information
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activation and mRNA expression for LRAT is blocked completely in vivo by actinomycin D
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additional information
activation and mRNA expression for LRAT is blocked completely in vivo by actinomycin D
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additional information
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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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