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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
17
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pubmed:dateCreated |
1993-7-13
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pubmed:databankReference |
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pubmed:abstractText |
17 beta-Hydroxysteroid dehydrogenase (17 beta-HSD) is an enzyme crucial to the regulation of intracellular levels of biologically active steroid hormones in a variety of tissues. Here, we report the isolation, structure, and characterization of a cDNA encoding the human 17 beta-HSD type 2. A 1.4-kilobase cDNA was identified, and DNA sequence analysis indicated that 17 beta-HSD type 2 was a protein of 387 amino acids with a predicted molecular weight of 42,782. The protein contained an amino-terminal type II signal-anchor motif and a carboxyl-terminal endoplasmic reticulum retention motif, which suggested that 17 beta-HSD type 2 was associated with the membranes of the endoplasmic reticulum. 17 beta-HSD type 2 was capable of catalyzing the interconversion of testosterone and androstenedione as well as estradiol and estrone. The enzyme also demonstrated 20 alpha-HSD activity toward 20 alpha-dihydroprogesterone. The amount of 17 beta-HSD type 2 mRNA in placenta was found to be high. The data suggest that the 17 beta-HSD type 2 cDNA encodes the microsomal 17 beta-HSD of human placenta, described by several laboratories.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12964-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8099587-17-Hydroxysteroid Dehydrogenases,
pubmed-meshheading:8099587-20-Hydroxysteroid Dehydrogenases,
pubmed-meshheading:8099587-20-alpha-Hydroxysteroid Dehydrogenase,
pubmed-meshheading:8099587-Amino Acid Sequence,
pubmed-meshheading:8099587-Base Sequence,
pubmed-meshheading:8099587-Cell Line,
pubmed-meshheading:8099587-Cloning, Molecular,
pubmed-meshheading:8099587-Female,
pubmed-meshheading:8099587-Gene Library,
pubmed-meshheading:8099587-Humans,
pubmed-meshheading:8099587-Isoenzymes,
pubmed-meshheading:8099587-Kinetics,
pubmed-meshheading:8099587-Male,
pubmed-meshheading:8099587-Microsomes,
pubmed-meshheading:8099587-Molecular Sequence Data,
pubmed-meshheading:8099587-Oligodeoxyribonucleotides,
pubmed-meshheading:8099587-Placenta,
pubmed-meshheading:8099587-Poly A,
pubmed-meshheading:8099587-Pregnancy,
pubmed-meshheading:8099587-Prostate,
pubmed-meshheading:8099587-Protein Structure, Secondary,
pubmed-meshheading:8099587-RNA, Messenger,
pubmed-meshheading:8099587-Recombinant Proteins,
pubmed-meshheading:8099587-Sequence Homology, Amino Acid,
pubmed-meshheading:8099587-Substrate Specificity,
pubmed-meshheading:8099587-Transfection
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pubmed:year |
1993
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pubmed:articleTitle |
Expression cloning and characterization of human 17 beta-hydroxysteroid dehydrogenase type 2, a microsomal enzyme possessing 20 alpha-hydroxysteroid dehydrogenase activity.
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pubmed:affiliation |
Departments of Biochemistry, Merck Research Laboratories, Rahway, New Jersey 07065.
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pubmed:publicationType |
Journal Article,
Comparative Study
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