Abstract

Lecithin retinol acyltransferase (LRAT) is a membrane protein that transforms all-trans retinol into all-trans retinyl ester. LRAT mutations lead to vision loss. A high activity is obtained with truncated LRAT (tLRAT; LRAT 30-196) purified in the presence of sodium dodecyl sulfate (SDS) whereas its natural mutations lead to a loss of its activity. Moreover, our data show that tLRAT is not properly structured on the basis of our NMR analyses. Structural information of LRAT must however be obtained to better understand the mechanism of its enzymatic activity.

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