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Updated: Jun 6, 2026

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
Purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase
Jianfeng Jin1, Adrie J J Straathof, Martijn W H Pinkse
1Biocatalysis and Organic Chemistry, Department of Biotechnology, Delft University of Technology, Delft, The Netherlands. j.jin@tudelft.nl
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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