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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2006-11-20
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/11-beta-Hydroxysteroid...,
http://linkedlifedata.com/resource/pubmed/chemical/3-Hydroxysteroid Dehydrogenases,
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/DHRS9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Estradiol Dehydrogenases,
http://linkedlifedata.com/resource/pubmed/chemical/HSD11B2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/HSD17B1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxysteroids,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Vitamin A,
http://linkedlifedata.com/resource/pubmed/chemical/retinol dehydrogenase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0888-7543
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
820-30
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pubmed:dateRevised |
2009-9-9
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pubmed:meshHeading |
pubmed-meshheading:16860536-11-beta-Hydroxysteroid Dehydrogenase Type 2,
pubmed-meshheading:16860536-3-Hydroxysteroid Dehydrogenases,
pubmed-meshheading:16860536-Alcohol Dehydrogenase,
pubmed-meshheading:16860536-Alcohol Oxidoreductases,
pubmed-meshheading:16860536-Amino Acid Sequence,
pubmed-meshheading:16860536-Animals,
pubmed-meshheading:16860536-Estradiol Dehydrogenases,
pubmed-meshheading:16860536-Genomics,
pubmed-meshheading:16860536-Humans,
pubmed-meshheading:16860536-Hydroxysteroids,
pubmed-meshheading:16860536-Molecular Sequence Data,
pubmed-meshheading:16860536-Oxidoreductases,
pubmed-meshheading:16860536-Phylogeny,
pubmed-meshheading:16860536-Substrate Specificity,
pubmed-meshheading:16860536-Vitamin A
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pubmed:year |
2006
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pubmed:articleTitle |
Comparative genomic and phylogenetic analysis of short-chain dehydrogenases/reductases with dual retinol/sterol substrate specificity.
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pubmed:affiliation |
Department of Biochemistry and Molecular Genetics, Schools of Medicine and Dentistry, University of Alabama at Birmingham, 720 20th Street South, 466 Kaul Genetics Building, Birmingham, AL 35294, USA. belyaeva@uab.edu
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, N.I.H., Extramural
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