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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2000-7-31
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pubmed:abstractText |
A quantitative stereochemical analysis of the products generated by recombinant mouse (12S)-lipoxygenase isoenzymes was performed with arachidonic acid and linoleic acid as substrates. The leucocyte-type (12S)-lipoxygenase generated, in addition to 12-hydroxyeicosatetraenoic acid (12-HETE) as the main product, 15- and 8-HETE from arachidonic acid and 13- and 9-hydroxyoctadecadienoic acid (13- and 9-HODE) from linoleic acid. The platelet-type enzyme oxygenated arachidonic acid to 12- and 8-HETE and linoleic acid to 13- and 9-HODE, whereas the epidermis-type (12S)-lipoxygenase reaction was essentially mono-specific with arachidonic acid but oxygenated linoleic acid to both 13- and 9-HODE. 12-HETE and 13-HODE were almost exclusively the S enantiomers. 8-HETE was the R enantiomer as a side-product of the platelet-type (12S)-lipoxygenase reaction but the S enantiomer as a side-product of the leucocyte-type reaction. 9-HODE was generated as the R enantiomer by the platelet-type and the epidermis-type isoenzymes and as the S enantiomer by the leucocyte-type (12S)-lipoxygenase. On the basis of published models of lipoxygenase-substrate interaction, the stereochemistry of the products generated by the platelet- and epidermis-type (12S)-lipoxygenases is in agreement with a fixed 'tail-to-head' orientation of the substrate fatty acid in the binding pocket of these enzymes, whereas that of the reaction products of the leucocyte-type (12S)-lipoxygenase can be explained only when the inverse orientation of the substrate or a rotational isomerism along the longitudinal axis of the substrate is allowed. Both the product spectra generated and the sensitivity towards the 12-lipoxygenase selective inhibitors N-benzyl-N-hydroxy-4-phenylpentanamide and cinnamyl-3,4-dihydroxy-alpha-cyanocinnamate indicated the platelet-type and the epidermis-type isoenzymes to be biochemically more related to each other than to the leucocyte-type (12S)-lipoxygenase.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-10078938,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-10100631,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-10225417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-10446122,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-111925,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-1514683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-1900207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-2016727,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-2118902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-2141786,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-3782139,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-6290844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-6774717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-6804460,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-7492614,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-7511046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-7576099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-7712291,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-8005520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-8188678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-8334154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-8440384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-8502991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-8626407,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-8702854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-8718858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-8798535,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-8944751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-9037187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-9177185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-9373619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-9384534,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-9406550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-9501907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-9518531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10816426-9618483
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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/12-Hydroxy-5,8,10,14-eicosatetraenoi...,
http://linkedlifedata.com/resource/pubmed/chemical/13-hydroxy-9,11-octadecadienoic acid,
http://linkedlifedata.com/resource/pubmed/chemical/9-hydroxy-10,12-octadecadienoic acid,
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonate 12-Lipoxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Linoleic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Linoleic Acids, Conjugated,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
348 Pt 2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
329-35
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10816426-12-Hydroxy-5,8,10,14-eicosatetraenoic Acid,
pubmed-meshheading:10816426-Animals,
pubmed-meshheading:10816426-Arachidonate 12-Lipoxygenase,
pubmed-meshheading:10816426-Arachidonic Acid,
pubmed-meshheading:10816426-Blood Platelets,
pubmed-meshheading:10816426-Cell Line,
pubmed-meshheading:10816426-Epidermis,
pubmed-meshheading:10816426-Humans,
pubmed-meshheading:10816426-Isoenzymes,
pubmed-meshheading:10816426-Kinetics,
pubmed-meshheading:10816426-Leukocytes,
pubmed-meshheading:10816426-Linoleic Acids,
pubmed-meshheading:10816426-Linoleic Acids, Conjugated,
pubmed-meshheading:10816426-Mice,
pubmed-meshheading:10816426-Models, Chemical,
pubmed-meshheading:10816426-Recombinant Proteins,
pubmed-meshheading:10816426-Stereoisomerism,
pubmed-meshheading:10816426-Substrate Specificity,
pubmed-meshheading:10816426-Transfection
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pubmed:year |
2000
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pubmed:articleTitle |
Positional- and stereo-selectivity of fatty acid oxygenation catalysed by mouse (12S)-lipoxygenase isoenzymes.
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pubmed:affiliation |
Research Program Tumor Cell Regulation (B0500), Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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