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Alcohol dehydrogenase 2 is a major hepatic enzyme for human retinol metabolism
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID iD: 0000-0001-5257-6261
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Bellaterra, Barcelona, Spain.
Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Bellaterra, Barcelona, Spain.
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2007 (English)In: Cellular and Molecular Life Sciences (CMLS), ISSN 1420-682X, E-ISSN 1420-9071, Vol. 64, no 4, p. 498-505Article in journal (Refereed) Published
Abstract [en]

The metabolism of all-trans- and 9-cis-retinol/ retinaldehyde has been investigated with focus on the activities of human, mouse and rat alcohol dehydrogenase 2 (ADH2), an intriguing enzyme with apparently different functions in human and rodents. Kinetic constants were determined with an HPLC method and a structural approach was implemented by in silico substrate dockings. For human ADH2, the determined K(m) values ranged from 0.05 to 0.3 microM and k(cat) values from 2.3 to 17.6 min(-1), while the catalytic efficiency for 9-cis-retinol showed the highest value for any substrate. In contrast, poor activities were detected for the rodent enzymes. A mouse ADH2 mutant (ADH2Pro47His) was studied that resembles the human ADH2 setup. This mutation increased the retinoid activity up to 100-fold. The K(m) values of human ADH2 are the lowest among all known human retinol dehydrogenases, which clearly support a role in hepatic retinol oxidation at physiological concentrations. 

Place, publisher, year, edition, pages
Springer, 2007. Vol. 64, no 4, p. 498-505
Keywords [en]
Alcohol dehydrogenase, computer modeling, kinetic constant, retinaldehyde, retinol, substrate docking
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:oru:diva-109973DOI: 10.1007/s00018-007-6449-8ISI: 000244565100010PubMedID: 17279314Scopus ID: 2-s2.0-33847322975OAI: oai:DiVA.org:oru-109973DiVA, id: diva2:1815975
Available from: 2023-11-30 Created: 2023-11-30 Last updated: 2023-12-01Bibliographically approved

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