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 (Engineering
Engineering on EC 2.3.1.135 - phosphatidylcholine-retinol O-acyltransferase
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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
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site-directed mutagenesis, construction of an N-glycosylation site for enzyme membrane localization and orientation studies, overview
I42N
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site-directed mutagenesis, construction of an N-glycosylation site for enzyme membrane localization and orientation studies, overview
additional information
S175R
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naturally occurring missense mutation, causing recessive earlyonset severe retinal dystrophy, the mutant enzyme shows highly reduced activity
S175R
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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
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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
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ectopic expression of human lecithin:retinol acyltransferase in murine basal layer of mouse skin and oral cavity epithelia
additional information
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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
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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
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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
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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
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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
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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
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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
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
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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
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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
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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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