Purification,characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity |
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| Authors: | Jianfeng Jin Adrie J. J. Straathof Martijn W. H. Pinkse Ulf Hanefeld |
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| Affiliation: | (1) Biocatalysis and Organic Chemistry, Department of Biotechnology, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands;(2) Bioseparation Technology, Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands;(3) Analytical Biotechnology, Department of Biotechnology, Netherlands Proteomics Centre, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands |
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| Abstract: | A bifunctional hydratase/alcohol dehydrogenase was isolated from the cyclohexanol degrading bacterium Alicycliphilus denitrificans DSMZ 14773. The enzyme catalyzes the addition of water to α,β-unsaturated carbonyl compounds and the subsequent alcohol oxidation. The purified enzyme showed three subunits in SDS gel, and the gene sequence revealed that this enzyme belongs to the molybdopterin binding oxidoreductase family containing molybdopterins, FAD, and iron-sulfur clusters. |
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