Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal.

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Haeseleer F, Huang J, Lebioda L, Saari JC, Palczewski K

Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal.

J Biol Chem. 1998 Aug 21;273(34):21790-9.

PubMed ID

9705317 [ View in PubMed

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Abstract

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.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Vitamin A	Short-chain dehydrogenase/reductase 3	Protein	Humans	Unknown	Substrate	Details

Polypeptides

Name	UniProt ID
Short-chain dehydrogenase/reductase 3	O75911	Details