Literature summary for 2.3.1.135 extracted from

Gauthier, M.E.; Roy, S.; Cantin, L.; Salesse, C.
Comparison between the enzymatic activity, structure and substrate binding of mouse and human lecithin retinol acyltransferase (2019), Biochem. Biophys. Res. Commun., 519, 832-837 .

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Protein Variants

Protein Variants	Comment	Organism
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	Homo sapiens
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	Mus musculus
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)	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O95237	-	-
Mus musculus	Q9JI60	-	-

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Release 2023.1 (January 2023)