caa a22 4500 60549844X CHVBK 20210128100546.0 cr unu---uuuuu 210128e20150801xx s 000 0 eng 10.1007/s00253-015-6699-6 doi (NATIONALLICENCE)springer-10.1007/s00253-015-6699-6 The substrate tolerance of alcohol oxidases [Elektronische Daten] [Mathias Pickl, Michael Fuchs, Silvia Glueck, Kurt Faber] Alcohols are a rich source of compounds from renewable sources, but they have to be activated in order to allow the modification of their carbon backbone. The latter can be achieved via oxidation to the corresponding aldehydes or ketones. As an alternative to (thermodynamically disfavoured) nicotinamide-dependent alcohol dehydrogenases, alcohol oxidases make use of molecular oxygen but their application is under-represented in synthetic biotransformations. In this review, the mechanism of copper-containing and flavoprotein alcohol oxidases is discussed in view of their ability to accept electronically activated or non-activated alcohols and their propensity towards over-oxidation of aldehydes yielding carboxylic acids. In order to facilitate the selection of the optimal enzyme for a given biocatalytic application, the substrate tolerance of alcohol oxidases is compiled and discussed: Substrates are classified into groups (non-activated prim- and sec-alcohols; activated allylic, cinnamic and benzylic alcohols; hydroxy acids; sugar alcohols; nucleotide alcohols; sterols) together with suitable alcohol oxidases, their microbial source, relative activities and (stereo)selectivities. The Author(s), 2015 Oxidation nationallicence Biocatalysis nationallicence Alcohol oxidase nationallicence Substrate tolerance nationallicence Flavoprotein nationallicence Cu-containing oxidase nationallicence Pickl Mathias Department of Chemistry, Organic & Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, A-8010, Graz, Austria aut Fuchs Michael Department of Chemistry, Organic & Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, A-8010, Graz, Austria aut Glueck Silvia Austrian Centre of Industrial Biotechnology (ACIB GmbH), Petersgasse 14, 8010 Graz, Austria aut Faber Kurt Department of Chemistry, Organic & Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, A-8010, Graz, Austria aut Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/16(2015-08-01), 6617-6642 0175-7598 99:16<6617 2015 99 253 https://doi.org/10.1007/s00253-015-6699-6 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-015-6699-6 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Pickl Mathias Department of Chemistry, Organic & Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, A-8010, Graz, Austria aut NATIONALLICENCE 700 1- Fuchs Michael Department of Chemistry, Organic & Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, A-8010, Graz, Austria aut NATIONALLICENCE 700 1- Glueck Silvia Austrian Centre of Industrial Biotechnology (ACIB GmbH), Petersgasse 14, 8010 Graz, Austria aut NATIONALLICENCE 700 1- Faber Kurt Department of Chemistry, Organic & Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, A-8010, Graz, Austria aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/16(2015-08-01), 6617-6642 0175-7598 99:16<6617 2015 99 253