A Vertebrate Aldo-keto Reductase Active with Retinoids and Ethanol

Bernat Crosas, Ella Cederlund, Dámaso Torres, Hans Jörnvall, Jaume Farrés, Xavier Parés

Research output: Contribution to journalArticleResearchpeer-review

29 Citations (Scopus)

Abstract

Enzymes of the short chain and medium chain dehydrogenase/reductase families have been demonstrated to participate in the oxidoreduction of ethanol and retinoids. Mammals and amphibians contain, in the upper digestive tract mucosa, alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, active with ethanol and retinol. In the present work, we searched for a similar enzyme in an avian species (Gallus domesticus). We found that chicken does not contain the homologous enzyme from the medium chain dehydrogenase/reductase family but an oxidoreductase from the aldo-keto reductase family, with retinal reductase and alcohol dehydrogenase activities. The amino acid sequence shows 66-69% residue identity with the aldose reductase and aldose reductase-like enzymes. Chicken aldo-keto reductase is a monomer of Mr 36,000 expressed in eye, tongue, and esophagus. The enzyme can oxidize aliphatic alcohols, such as ethanol, and it is very efficient in all-trans- and 9-cis-retinal reduction (kcat/Km = 5,300 and 32,000 mM-1·min-1, respectively). This finding represents the inclusion of the aldo-keto reductase family, with the (α/β)8 barrel structure, into the scenario of retinoid metabolism and, therefore, of the regulation of vertebrate development and tissue differentiation.
Original languageEnglish
Pages (from-to)19132-19140
JournalJournal of Biological Chemistry
Volume276
DOIs
Publication statusPublished - 1 Jun 2001

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