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http://purl.uniprot.org/citations/15369820http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15369820http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15369820http://www.w3.org/2000/01/rdf-schema#comment"Human alcohol dehydrogenases (ADH1 and ADH4) actively use retinoids oxidized at the cyclohexenyl ring (4-oxo-, 4-hydroxy-, and 3,4-didehydro-retinoids), which are functional compounds in several cells and tissues (i.e., in human skin). Remarkably, activities with 4-oxo-retinal and 4-hydroxy-retinol (kcat = 2050 min(-1) for ADH4) are the highest among retinoids, similar to those of the best aliphatic alcohols. Thus, ADH1 and ADH4 provide a metabolic pathway for the synthesis of the corresponding retinoic acids. Tween 80, a widely used detergent in the retinoid activity assay, behaves as a competitive inhibitor. The Km values for all-trans-retinol (2-3 microM), estimated in the absence of detergent, are 10-fold lower than those obtained at the usual 0.02% Tween 80. This suggests a contribution of ADH to retinoid metabolism more relevant than previously expected. However, Tween 80 stabilizes retinoids in water solution and provides a reliable and reproducible assay, suitable for comparing different ADHs and different retinoid substrates."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.org/dc/terms/identifier"doi:10.1016/j.abb.2004.07.002"xsd:string
http://purl.uniprot.org/citations/15369820http://purl.org/dc/terms/identifier"doi:10.1016/j.abb.2004.07.002"xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"Alvarez R."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"Alvarez R."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"Farres J."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"Farres J."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"Pares X."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"Pares X."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"Dominguez M."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"Dominguez M."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"Gallego O."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"Gallego O."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"Martras S."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"Martras S."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"de Lera A.R."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/author"de Lera A.R."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/pages"210-217"xsd:string
http://purl.uniprot.org/citations/15369820http://purl.uniprot.org/core/pages"210-217"xsd:string