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

  • Belyaeva O
  • Kedishvili N
  • 8

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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.

Author-supplied keywords

  • 3 α -hydroxysteroids
  • comprise a
  • dehydrogenase
  • heterogeneous proteins that
  • homologs
  • large family of functionally
  • of steroids
  • origin
  • orthologs
  • participate in the metabolism
  • phylogenetics
  • prostaglandins
  • reductases
  • retinol
  • sdr
  • short-chain dehydrogenases
  • vertebrates

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Authors

  • Olga V Belyaeva

  • Natalia Y Kedishvili

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