PUBLICATION
Comparative genomic and phylogenetic analysis of short-chain dehydrogenases/reductases with dual retinol/sterol substrate specificity
- Authors
- Belyaeva, O.V., and Kedishvili, N.Y.
- ID
- ZDB-PUB-080613-2
- Date
- 2006
- Source
- Genomics 88(6): 820-830 (Journal)
- Registered Authors
- Keywords
- Retinol, 3α-Hydroxysteroids, Dehydrogenase, Orthologs, Homologs, Origin, Vertebrates, Phylogenetics
- MeSH Terms
-
- 11-beta-Hydroxysteroid Dehydrogenase Type 2/chemistry
- 11-beta-Hydroxysteroid Dehydrogenase Type 2/genetics
- 11-beta-Hydroxysteroid Dehydrogenase Type 2/metabolism
- 3-Hydroxysteroid Dehydrogenases/chemistry
- 3-Hydroxysteroid Dehydrogenases/genetics
- 3-Hydroxysteroid Dehydrogenases/metabolism
- Alcohol Dehydrogenase/chemistry
- Alcohol Dehydrogenase/genetics
- Alcohol Dehydrogenase/metabolism
- Alcohol Oxidoreductases/chemistry
- Alcohol Oxidoreductases/genetics
- Alcohol Oxidoreductases/metabolism
- Amino Acid Sequence
- Animals
- Estradiol Dehydrogenases/chemistry
- Estradiol Dehydrogenases/genetics
- Estradiol Dehydrogenases/metabolism
- Genomics*
- Humans
- Hydroxysteroids/metabolism*
- Molecular Sequence Data
- Oxidoreductases/chemistry
- Oxidoreductases/genetics*
- Oxidoreductases/metabolism
- Phylogeny*
- Substrate Specificity
- Vitamin A/metabolism*
- PubMed
- 16860536 Full text @ Genomics
Citation
Belyaeva, O.V., and Kedishvili, N.Y. (2006) Comparative genomic and phylogenetic analysis of short-chain dehydrogenases/reductases with dual retinol/sterol substrate specificity. Genomics. 88(6):820-830.
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 3alpha-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 3alpha-HSD) are significantly less conserved. Orthologs for 3alpha-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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping