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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1989-9-28
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pubmed:abstractText |
We identified type II P-450(15)alpha as mouse coumarin 7-hydroxylase (P-450coh). Unlike type I P-450(15)alpha, the other member within the mouse steroid 15 alpha-hydroxylase gene family, type II catalyzed little steroid 15 alpha-hydroxylase activity, yet structurally there were only 11 substitutions between type I and type II P-450(15)alphaS within their 494 amino acid residues (Lindberg et al., 1989), and the N-terminal sequence (21 residues) of P-450coh was identical with that of both P-450(15)alphaS. Induction by pyrazole of coumarin 7-hydroxylase activity correlated well with the increase of type II P-450(15)alpha mRNA in 129/J male and female mice. Pyrazole, on the other hand, was less in males or not effective in females in inducing the 15 alpha-hydroxylase activity and type I P-450(15)alpha mRNA. Expression of type I and II in COS-1 cells revealed that the latter catalyzed coumarin 7-hydroxylase activity at 10 to approximately 14 pmol min-1 (mg of cellular protein)-1. The former, on the other hand, had a high testosterone 15 alpha-hydroxylase but little coumarin 7-hydroxylase activity. It was concluded, therefore, that type II P-450(15)alpha is the mouse coumarin 7-hydroxylase. Identification of type II as the P-450 specific to coumarin 7-hydroxylase activity and characterization of its cDNA and gene, therefore, were significant advances toward understanding the basis of genetic regulation of this activity in mice (known as Coh locus).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aryl Hydrocarbon Hydroxylases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyp2a4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Steroid Hydroxylases,
http://linkedlifedata.com/resource/pubmed/chemical/coumarin 7-hydroxylase,
http://linkedlifedata.com/resource/pubmed/chemical/pyrazole,
http://linkedlifedata.com/resource/pubmed/chemical/steroid 15-alpha-hydroxylase
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4169-72
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pubmed:dateRevised |
2005-10-15
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pubmed:meshHeading |
pubmed-meshheading:2765478-Animals,
pubmed-meshheading:2765478-Aryl Hydrocarbon Hydroxylases,
pubmed-meshheading:2765478-Cytochrome P-450 Enzyme System,
pubmed-meshheading:2765478-DNA,
pubmed-meshheading:2765478-Enzyme Induction,
pubmed-meshheading:2765478-Female,
pubmed-meshheading:2765478-Gene Expression Regulation,
pubmed-meshheading:2765478-Male,
pubmed-meshheading:2765478-Mice,
pubmed-meshheading:2765478-Mixed Function Oxygenases,
pubmed-meshheading:2765478-Multigene Family,
pubmed-meshheading:2765478-Pyrazoles,
pubmed-meshheading:2765478-Steroid Hydroxylases
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pubmed:year |
1989
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pubmed:articleTitle |
Mouse steroid 15 alpha-hydroxylase gene family: identification of type II P-450(15)alpha as coumarin 7-hydroxylase.
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pubmed:affiliation |
Pharmacogenetics Section, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina 27709.
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pubmed:publicationType |
Journal Article
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