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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
1993-6-24
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pubmed:abstractText |
The sequence of reactions catalyzed by sterol 27-hydroxylase (CYP27) in the oxidation of 5 beta-cholestane-3 alpha,7 alpha,12 alpha,27-tetrol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid was studied with apparently homogeneous preparations of the cytochrome P-450 from rabbit liver mitochondria. Conditions are described for the formation and characterization of 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestane-27-al as an enzymatically generated intermediate in the oxidation process. Incubation of 5 beta-cholestane-3 alpha,7 alpha,12 alpha-triol or 5 beta-cholestane-3 alpha,7 alpha,12 alpha,27-tetrol with sterol 27-hydroxylase in 18O2 atmosphere resulted in the incorporation of one or two 18O atoms in the carboxyl group of 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid. Similar incubations with 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestane-27-al resulted in the incorporation of one 18O atom in the 27-carboxyl group. The results strongly indicate that the sterol 27-hydroxylase performs multiple monooxygenations in the conversion of 5 beta-cholestane-3 alpha,7 alpha,12 alpha-triol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid. The following reaction sequence (Reaction 1) at carbon 27 is proposed. [formula: see text] Reaction 1.
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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/3,7,12-trihydroxycoprostanic acid,
http://linkedlifedata.com/resource/pubmed/chemical/Bile Acids and Salts,
http://linkedlifedata.com/resource/pubmed/chemical/Cholestanols,
http://linkedlifedata.com/resource/pubmed/chemical/Cholic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 CYP27A1,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen Isotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Steroid Hydroxylases,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium,
http://linkedlifedata.com/resource/pubmed/chemical/cholestane-3,7,12,26-tetrol
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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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 |
11079-85
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8496170-Animals,
pubmed-meshheading:8496170-Bile Acids and Salts,
pubmed-meshheading:8496170-Cholestanols,
pubmed-meshheading:8496170-Cholic Acids,
pubmed-meshheading:8496170-Cytochrome P-450 CYP27A1,
pubmed-meshheading:8496170-Cytochrome P-450 Enzyme System,
pubmed-meshheading:8496170-Kinetics,
pubmed-meshheading:8496170-Liver,
pubmed-meshheading:8496170-Mass Spectrometry,
pubmed-meshheading:8496170-Oxidation-Reduction,
pubmed-meshheading:8496170-Oxygen Isotopes,
pubmed-meshheading:8496170-Rabbits,
pubmed-meshheading:8496170-Steroid Hydroxylases,
pubmed-meshheading:8496170-Tritium
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pubmed:year |
1993
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pubmed:articleTitle |
Sterol 27-hydroxylase in bile acid biosynthesis. Mechanism of oxidation of 5 beta-cholestane-3 alpha,7 alpha,12 alpha,27-tetrol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid.
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pubmed:affiliation |
Department of Pharmaceutical Biochemistry, University of Uppsala, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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