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http://purl.uniprot.org/citations/9600267http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9600267http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9600267http://www.w3.org/2000/01/rdf-schema#comment"Kinetic constants of human class IV alcohol dehydrogenase (sigmasigma-ADH) support a role of the enzyme in retinoid metabolism, fatty acid omega-oxidation, and elimination of cytotoxic aldehydes produced by lipid peroxidation. Class IV is the human ADH form most efficient in the reduction of 4-hydroxynonenal (k(cat)/Km: 39,500 mM(-1) min(-1)). Class IV shows high activity with all-trans-retinol and 9-cis-retinol, while 13-cis-retinol is not a substrate but an inhibitor. Both all-trans-retinoic and 13-cis-retinoic acids are potent competitive inhibitors of retinol oxidation (Ki: 3-10 microM) which can be a basis for the regulation of the retinoic acid generation and of the pharmacological actions of the 13-cis-isomer. The inhibition of class IV retinol oxidation by ethanol (Ki: 6-10 mM) may be the origin of toxic and teratogenic effects of ethanol. H2-receptor antagonists are poor inhibitors of human and rat classes I and IV (Ki > 0.3 mM) suggesting a small interference in ethanol metabolism at the pharmacological doses of these common drugs."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(98)00374-3"xsd:string
http://purl.uniprot.org/citations/9600267http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(98)00374-3"xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/author"Allali-Hassani A."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/author"Allali-Hassani A."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/author"Farres J."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/author"Farres J."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/author"Pares X."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/author"Pares X."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/author"Martras S."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/author"Martras S."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/author"Peralba J.M."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/author"Peralba J.M."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/pages"362-366"xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/pages"362-366"xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/title"Retinoids, omega-hydroxyfatty acids and cytotoxic aldehydes as physiological substrates, and H2-receptor antagonists as pharmacological inhibitors, of human class IV alcohol dehydrogenase."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/title"Retinoids, omega-hydroxyfatty acids and cytotoxic aldehydes as physiological substrates, and H2-receptor antagonists as pharmacological inhibitors, of human class IV alcohol dehydrogenase."xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/volume"426"xsd:string
http://purl.uniprot.org/citations/9600267http://purl.uniprot.org/core/volume"426"xsd:string