Title |
Alcohol dehydrogenase 2 is a major hepatic enzyme for human retinol metabolism
|
---|---|
Published in |
Cellular and Molecular Life Sciences, February 2007
|
DOI | 10.1007/s00018-007-6449-8 |
Pubmed ID | |
Authors |
M. Hellgren, P. Strömberg, O. Gallego, S. Martras, J. Farrés, B. Persson, X. Parés, J. -O. Höög |
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. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 22 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 4 | 18% |
Student > Bachelor | 4 | 18% |
Student > Master | 3 | 14% |
Librarian | 1 | 5% |
Student > Doctoral Student | 1 | 5% |
Other | 1 | 5% |
Unknown | 8 | 36% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 6 | 27% |
Medicine and Dentistry | 4 | 18% |
Chemistry | 2 | 9% |
Social Sciences | 1 | 5% |
Chemical Engineering | 1 | 5% |
Other | 0 | 0% |
Unknown | 8 | 36% |