| First Author | Haeseleer F | Year | 1998 |
| Journal | J Biol Chem | Volume | 273 |
| Issue | 34 | Pages | 21790-9 |
| PubMed ID | 9705317 | Mgi Jnum | J:49273 |
| Mgi Id | MGI:1277062 | Doi | 10.1074/jbc.273.34.21790 |
| Citation | Haeseleer F, et al. (1998) Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal. J Biol Chem 273(34):21790-9 |
| abstractText | 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. |
