Abstract
The universal chromophore of visual pigments in higher animals is 11-cisretinaldehyde. The final step in the biosynthetic pathway generating this compound is catalyzed by 11-cisretinol dehydrogenase, a membrane-bound enzyme abundantly expressed in the retinal pigment epithelium of the eye. In this work we demonstrate that the primary structure of human 11-cisretinol dehydrogenase is highly conserved with 91% identity to the bovine enzyme. The gene encoding 11-cisretinol dehydrogenase spans over ≈4.1 kb of DNA and is divided into four translated exons. Analysis of a panel of somatic cells hybrids and fluorescencein situhybridization on metaphase chromosomes revealed that the gene is located on chromosome 12q13–q14. Due to the unique role of 11-cisretinol dehydrogenase in the generation of visual pigments, it is a candidate gene for involvement in hereditary eye disease.
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