Source:http://linkedlifedata.com/resource/pubmed/id/11306067
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-3
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pubmed:dateCreated |
2001-4-18
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pubmed:databankReference | |
pubmed:abstractText |
We have previously characterized the first human NAD(+)-dependent short chain dehydrogenase capable of oxidizing all-trans-retinol and androgens, and found only in the liver and skin. In a search for related human enzymes, we identified a partial open reading frame, which exhibited >60% sequence identity to human RoDH-4. The full-length cDNA for this enzyme was determined in our laboratory by 5'-RACE PCR and was found to be identical to the recently reported novel type of oxidative human 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD). Analysis of the genomic structure revealed that the gene for RoDH-like 3alpha-HSD has four translated exons and, possibly, a fifth exon that codes for the 5'-untranslated region. The gene for RoDH-4 appears to have only four exons. The positions of exon-intron boundaries and the sizes of the protein coding regions are identical in 3alpha-HSD and RoDH-4. Moreover, both genes are mapped to chromosome 12q13, and are located in a close proximity to each other. Both genes appear to have satellite pseudogenes. Thus, RoDH-4 and 3alpha-HSD genes share similar structural organization and cluster on human chromosome 12, near the gene for 11-cis retinol dehydrogenase.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3-Hydroxysteroid Dehydrogenases,
http://linkedlifedata.com/resource/pubmed/chemical/3-alpha-Hydroxysteroid...,
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/retinol dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/trans-retinol dehydrogenase
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0009-2797
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
130-132
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
457-67
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11306067-3-Hydroxysteroid Dehydrogenases,
pubmed-meshheading:11306067-3-alpha-Hydroxysteroid Dehydrogenase (B-Specific),
pubmed-meshheading:11306067-Alcohol Oxidoreductases,
pubmed-meshheading:11306067-Amino Acid Sequence,
pubmed-meshheading:11306067-Base Sequence,
pubmed-meshheading:11306067-Chromosome Mapping,
pubmed-meshheading:11306067-Cloning, Molecular,
pubmed-meshheading:11306067-DNA, Complementary,
pubmed-meshheading:11306067-DNA Primers,
pubmed-meshheading:11306067-Exons,
pubmed-meshheading:11306067-Humans,
pubmed-meshheading:11306067-Introns,
pubmed-meshheading:11306067-Molecular Sequence Data,
pubmed-meshheading:11306067-Sequence Homology, Amino Acid
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pubmed:year |
2001
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pubmed:articleTitle |
Cloning of the human RoDH-related short chain dehydrogenase gene and analysis of its structure.
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pubmed:affiliation |
Division of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, 5007 Rockhill Road, 103 BSB, 64110, Kansas City, MO, USA. kedishvilin@umkc.edu
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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