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Alcohol dehydrogenase 2 is a major hepatic enzyme for human retinol metabolism.
- Source :
-
Cellular and molecular life sciences : CMLS [Cell Mol Life Sci] 2007 Feb; Vol. 64 (4), pp. 498-505. - Publication Year :
- 2007
-
Abstract
- 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.
Details
- Language :
- English
- ISSN :
- 1420-682X
- Volume :
- 64
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Cellular and molecular life sciences : CMLS
- Publication Type :
- Academic Journal
- Accession number :
- 17279314
- Full Text :
- https://doi.org/10.1007/s00018-007-6449-8