| pubmed-article:10816426 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10816426 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
| pubmed-article:10816426 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:10816426 | lifeskim:mentions | umls-concept:C1552126 | lld:lifeskim |
| pubmed-article:10816426 | lifeskim:mentions | umls-concept:C0282636 | lld:lifeskim |
| pubmed-article:10816426 | lifeskim:mentions | umls-concept:C0015684 | lld:lifeskim |
| pubmed-article:10816426 | lifeskim:mentions | umls-concept:C0022173 | lld:lifeskim |
| pubmed-article:10816426 | lifeskim:mentions | umls-concept:C0023837 | lld:lifeskim |
| pubmed-article:10816426 | pubmed:dateCreated | 2000-7-31 | lld:pubmed |
| pubmed-article:10816426 | 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. | lld:pubmed |
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| pubmed-article:10816426 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10816426 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10816426 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10816426 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10816426 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10816426 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:10816426 | pubmed:author | pubmed-author:MarksFF | lld:pubmed |
| pubmed-article:10816426 | pubmed:author | pubmed-author:Fürstenberger... | lld:pubmed |
| pubmed-article:10816426 | pubmed:author | pubmed-author:KriegPP | lld:pubmed |
| pubmed-article:10816426 | pubmed:author | pubmed-author:BürgerFF | lld:pubmed |
| pubmed-article:10816426 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10816426 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:10816426 | pubmed:volume | 348 Pt 2 | lld:pubmed |
| pubmed-article:10816426 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10816426 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10816426 | pubmed:pagination | 329-35 | lld:pubmed |
| pubmed-article:10816426 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10816426 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10816426 | pubmed:articleTitle | Positional- and stereo-selectivity of fatty acid oxygenation catalysed by mouse (12S)-lipoxygenase isoenzymes. | lld:pubmed |
| pubmed-article:10816426 | pubmed:affiliation | Research Program Tumor Cell Regulation (B0500), Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany. | lld:pubmed |
| pubmed-article:10816426 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10816426 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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