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

J Biol Chem. 1998 Aug 21;273(34):21790-9. doi: 10.1074/jbc.273.34.21790.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alcohol Oxidoreductases / genetics*
  • Alcohol Oxidoreductases / metabolism*
  • Animals
  • Cattle
  • Chromosome Mapping
  • Chromosomes, Human, Pair 1*
  • Cloning, Molecular
  • Humans
  • In Situ Hybridization, Fluorescence
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • RNA, Messenger / metabolism
  • Rats
  • Retina / enzymology*
  • Rod Cell Outer Segment / enzymology*
  • Tretinoin / metabolism*


  • RNA, Messenger
  • Tretinoin
  • Alcohol Oxidoreductases
  • alcohol dehydrogenase (NAD(P)+)

Associated data

  • GENBANK/AF061741
  • GENBANK/AF061742
  • GENBANK/AF061743