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Literature summary extracted from

  • Moise, A.R.; Golczak, M.; Imanishi, Y.; Palczewski, K.
    Topology and membrane association of lecithin: retinol acyltransferase (2007), J. Biol. Chem., 282, 2081-2090.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.135
-
 Mus musculus
2.3.1.135 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 Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.135 D128N site-directed mutagenesis, construction of an N-glycosylation site for enzyme membrane localization and orientation studies, overview Mus musculus
2.3.1.135 I42N site-directed mutagenesis, construction of an N-glycosylation site for enzyme membrane localization and orientation studies, overview Mus musculus
2.3.1.135 additional information construction of Ntm LRAT, a truncation mutant lacking the putative C-terminal transmembrane domain corresponding to Met1–Ser195, and Ctm LRAT, a mutant lacking the putative N-terminal transmembrane domain corresponding to Gly35–Gly231, 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 Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.135 endoplasmic reticulum membrane LRATis a single membrane-spanning protein with an N-terminal domain that faces the cytoplasm, C-terminal luminal orientation, membrane topology, overview Mus musculus 5789
-
2.3.1.135 endoplasmic reticulum membrane 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 Mus musculus 5789
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.135 lecithin + retinol-[cellular retinol-binding protein III] Mus musculus 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 2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.135 Mus musculus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.135 lecithin + retinol-[cellular retinol-binding protein III]
-
 Mus musculus 2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
 ?
2.3.1.135 lecithin + retinol-[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 Mus musculus 2-acylglycerophosphocholine + retinyl ester-[cellular retinol-binding protein III]
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.135 More epitope mapping, the enzyme contains a C-terminal transmembrane domain Mus musculus

Synonyms

EC Number Synonyms Comment Organism
2.3.1.135 lecithin:retinol acyltransferase
-
 Mus musculus
2.3.1.135 LRAT
-
 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.135 37
-
 assay at Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.135 7.5
-
 assay at Mus musculus