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Literature summary for 2.3.1.135 extracted from
- Focus on molecules: lecithin retinol acyltransferase (2010), Exp. Eye Res., 90, 186-187.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene lrat is localized on chromosome 4 at locus 4q31.2 | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetic analysis using purified truncated mutant tLRAT | Homo sapiens | |
| 0.00024 | - |
all-trans-retinol-[cellular-retinol-binding-protein] | pH and temperature not specified in the publication | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | boound | Mus musculus | 16020 | - |
| membrane | boound | Homo sapiens | 16020 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 25000 | - |
x * 25000, about | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein] | Homo sapiens | 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. | 2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein] | - |
r |  |
| phosphatidylcholine + 11-cis-retinoll-[cellular-retinol-binding-protein] | Mus musculus | 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. | 2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein] | - |
r | |
| phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein] | Mus musculus | 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. | 2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein] | - |
r | |
| phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein] | Homo sapiens | 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. | 2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein] | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
gene Lrat | - |
| Mus musculus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| eye | - |
Mus musculus | - |
| eye | - |
Homo sapiens | - |
| additional information | LRAT is expressed in multiple tissues | Mus musculus | - |
| additional information | LRAT is expressed in multiple tissues | Homo sapiens | - |
| retinal pigment epithelium | - |
Mus musculus | - |
| retinal pigment epithelium | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| phosphatidylcholine + 11-cis-retinol-[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. | Homo sapiens | 2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein] | - |
r | |
| phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein] | both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate. | Mus musculus | 2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein] | - |
r | |
| phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein] | both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate. | Homo sapiens | 2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein] | - |
r | |
| phosphatidylcholine + 11-cis-retinoll-[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. | Mus musculus | 2-acylglycerophosphocholine + 11-cis-retinyl-ester-[cellular-retinol-binding-protein] | - |
r | |
| phosphatidylcholine + all-trans-retinol-[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. | Mus musculus | 2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein] | - |
r | |
| phosphatidylcholine + all-trans-retinol-[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. | Homo sapiens | 2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein] | - |
r | |
| phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein] | both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate. | Mus musculus | 2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein] | - |
r | |
| phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein] | both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate. | Homo sapiens | 2-acylglycerophosphocholine + all-trans-retinyl-ester-[cellular-retinol-binding-protein] | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 25000, about | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| lecithin retinol acyltransferase | - |
Mus musculus |
| lecithin retinol acyltransferase | - |
Homo sapiens |
| LRAT | - |
Mus musculus |
| LRAT | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Mus musculus |
| 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 | Homo sapiens |
| 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 | Mus musculus |
| malfunction | homozygous mutation S175R occurs in two patients diagnosed with severe early-onset retinal degeneration | Homo sapiens |
| 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 | Mus musculus |
| 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 | Homo sapiens |
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Release 2023.1 (January 2023)
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