Journal of Biological Chemistry
Volume 273, Issue 34, 21 August 1998, Pages 21790-21799
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ENZYMOLOGY
Molecular Characterization of a Novel Short-chain Dehydrogenase/Reductase That Reduces All-trans-retinal*

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The reduction of all-trans-retinal in photoreceptor outer segments is the first step in the regeneration of bleached visual pigments. We report here the cloning of a dehydrogenase, retSDR1, that belongs to the short-chain dehydrogenase/reductase superfamily and localizes predominantly in cone photoreceptors. retSDR1 expressed in insect cells displayed substrate specificities of the photoreceptor all-trans-retinol dehydrogenase. Homology modeling of retSDR1 using the carbonyl reductase structure as a scaffold predicted a classical Rossmann fold for the nucleotide binding, and an N-terminal extension that could facilitate binding of the enzyme to the cell membranes. The presence of retSDR1 in a subset of inner retinal neurons and in other tissues suggests that the enzyme may also be involved in retinol metabolism outside of photoreceptors.

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*

This work was supported in part by National Institutes of Health NEI Grants EY02317, EY01730, and EY09339; by an award from Research to Prevent Blindness, Inc.; and by an award from the Royalty Research Foundation of the University of Washington.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank™/EMBL Data Bank with accession number(s) AF061741, AF061742, AF061743 for human, bovine, and mouse retSDR1, respectively.

Senior Scientific Investigator of Research to Prevent Blindness, Inc.