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We previously engineered this enzyme to create amine dehydrogenase (AmDH) variants that possess a new hydrophobic cavity in their active site such that aromatic ketones can bind and be converted into \u03b1\u2010chiral amines with excellent enantioselectivity. We also recently observed that LysEDH was capable of reducing aromatic aldehydes into primary alcohols. Herein, we harnessed the promiscuous alcohol dehydrogenase (ADH) activity of LysEDH to create new variants that exhibited enhanced catalytic activity for the reduction of substituted benzaldehydes and arylaliphatic aldehydes to primary alcohols. Notably, these novel engineered dehydrogenases also catalyzed the reductive amination of a variety of aldehydes and ketones with excellent enantioselectivity, thus exhibiting a dual AmDH\/ADH activity. We envisioned that the catalytic bi\u2010functionality of these enzymes could be applied for the direct conversion of alcohols into amines. As a proof\u2010of\u2010principle, we performed an unprecedented one\u2010pot \u201chydrogen\u2010borrowing\u201d cascade to convert benzyl alcohol to benzylamine using a single enzyme. Conducting the same biocatalytic cascade in the presence of cofactor recycling enzymes (i.e., NADH\u2010oxidase and formate dehydrogenase) increased the reaction yields. In summary, this work provides the first examples of enzymes showing \u201calcohol aminase\u201d activity.<\/jats:p>","DOI":"10.1002\/chem.202003140","type":"journal-article","created":{"date-parts":[[2020,10,19]],"date-time":"2020-10-19T13:42:43Z","timestamp":1603114963000},"page":"3315-3325","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity"],"prefix":"10.1002","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5923-9735","authenticated-orcid":false,"given":"Vasilis","family":"Tseliou","sequence":"first","affiliation":[{"name":"Van't Hoff Institute for Molecular Sciences, HIMS-Biocat University of Amsterdam  Science Park 904 1098 XH Amsterdam The 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