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Alcohol dehydrogena...
Alcohol dehydrogenase 2 is a major hepatic enzyme for human retinol metabolism
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- Hellgren, Mikko, 1972- (författare)
- Karolinska Institutet,Dept. of Medical Biochemistry and Biophysics Karolinska Inst. Stockholm
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- Strömberg, P. (författare)
- Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden,Dept. of Medical Biochemistry and Biophysics Karolinska Institutet, Stockholm
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- Gallego, O. (författare)
- Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Bellaterra, Barcelona, Spain
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- Martras, S. (författare)
- Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Bellaterra, Barcelona, Spain
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- Farrés, J. (författare)
- Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Bellaterra, Barcelona, Spain
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- Persson, Bengt, 1961- (författare)
- Linköpings universitet,Karolinska Institutet,Tekniska högskolan,Bioinformatik
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- Parés, X. (författare)
- Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Bellaterra, Barcelona, Spain
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- Höög, Jan-Olov (författare)
- Karolinska Institutet,Dept. of Medical Biochemistry and Biophysics Karolinska Institutet, Stockholm
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Karolinska Institutet Dept of Medical Biochemistry and Biophysics Karolinska Inst. Stockholm (creator_code:org_t)
- 2007-02-05
- 2007
- Engelska.
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Ingår i: Cellular and Molecular Life Sciences (CMLS). - : Springer. - 1420-682X .- 1420-9071. ; 64:4, s. 498-505
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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http://kipublication...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- Alcohol dehydrogenase
- computer modeling
- kinetic constant
- retinaldehyde
- retinol
- substrate docking
- NATURAL SCIENCES
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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Till lärosätets databas
- Av författaren/redakt...
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Hellgren, Mikko, ...
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Strömberg, P.
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Gallego, O.
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Martras, S.
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Farrés, J.
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Persson, Bengt, ...
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visa fler...
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Parés, X.
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Höög, Jan-Olov
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visa färre...
- Om ämnet
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- NATURVETENSKAP
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NATURVETENSKAP
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och Biologi
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och Biokemi och mole ...
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Cellular and Mol ...
- Av lärosätet
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Örebro universitet
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Karolinska Institutet
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Linköpings universitet