Print Email Facebook Twitter Purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity Title Purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity Author Jin, J. Straathof, A.J.J. Pinkse, M.W.H. Hanefeld, U. Faculty Applied Sciences Department BT/Biotechnology Date 2010-12-01 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 ?,?-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. Subject Michael addition?,?-unsaturated carbonyl compoundshydratasealcohol dehydrogenasemolybdenum-containing hydroxylase To reference this document use: http://resolver.tudelft.nl/uuid:0d08c109-cad9-4b0b-b89a-b52131a02ddb DOI https://doi.org/10.1007/s00253-010-2996-2 Publisher Springer ISSN 0175-7598 Source Applied Microbiology and Biotechnology, 89 (6), 2011 Part of collection Institutional Repository Document type journal article Rights (c) 2010 The Author(s). This article is published with open access at Springerlink.com Files PDF Jin_2011.pdf 379.64 KB Close viewer /islandora/object/uuid:0d08c109-cad9-4b0b-b89a-b52131a02ddb/datastream/OBJ/view