Comparative genomic and phylogenetic analysis of short-chain dehydrogenases/reductases with dual retinol/sterol substrate specificity

Academic Article

Abstract

  • Human short-chain dehydrogenases/reductases with dual retinol/sterol substrate specificity (RODH-like enzymes) are thought to contribute to the oxidation of retinol for retinoic acid biosynthesis and to the metabolism of androgenic and neuroactive 3α-hydroxysteroids. Here, we investigated the phylogeny and orthology of these proteins to understand better their origins and physiological roles. Phylogenetic and genomic analysis showed that two proteins (11-cis-RDH and RDHL) are highly conserved, and their orthologs can be identified in the lower taxa, such as amphibians and fish. Two other proteins (RODH-4 and 3α-HSD) are significantly less conserved. Orthologs for 3α-HSD are present in all mammals analyzed, whereas orthologs for RODH-4 can be identified in some mammalian species but not in others due to species-specific gene duplications. Understanding the evolution and divergence of RODH-like enzymes in various vertebrate species should facilitate further investigation of their in vivo functions using animal models. © 2006 Elsevier Inc. All rights reserved.
  • Authors

    Published In

  • Genomics  Journal
  • Digital Object Identifier (doi)

    Author List

  • Belyaeva OV; Kedishvili NY
  • Start Page

  • 820
  • End Page

  • 830
  • Volume

  • 88
  • Issue

  • 6