Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase [PDF]
Biomolecules, 2013 Enzymes of the non-conventional yeast Yarrowia lipolytica seem to be tailor-made for the conversion of lipophilic substrates. Herein, we cloned and overexpressed the Zn-dependent alcohol dehydrogenase ADH2 from Yarrowia lipolytica in Escherichia coli ...
Margit Winkler +5 more
doaj +6 more sources
Screening of Microorganisms Producing Cold-Active Oxidoreductases to Be Applied in Enantioselective Alcohol Oxidation. An Antarctic Survey [PDF]
Marine Drugs, 2011 Several microorganisms were isolated from soil/sediment samples of Antarctic Peninsula. The enrichment technique using (RS)-1-(phenyl)ethanol as a carbon source allowed us to isolate 232 psychrophile/psychrotroph microorganisms.
Leandro H. Andrade +4 more
doaj +6 more sources
NAD(P)<sup>+</sup>-dependent alcohol oxidoreductases oxidize 7-hydroxycannabidiol to a reactive formyl metabolite. [PDF]
Arch ToxicolWu Q +4 more
europepmc +6 more sources
Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity [PDF]
Chemistry – A European Journal, 2020 The l‐lysine‐ϵ‐dehydrogenase (LysEDH) from Geobacillus stearothermophilus naturally catalyzes the oxidative deamination of the ϵ‐amino group of l‐lysine.
Vasilis Tseliou +4 more
semanticscholar +6 more sources
Activities of Secreted Aryl Alcohol Quinone Oxidoreductases from Pycnoporus cinnabarinus Provide Insights into Fungal Degradation of Plant Biomass [PDF]
Applied and Environmental Microbiology, 2016 ABSTRACT Auxiliary activities family 3 subfamily 2 (AA3_2) from the CAZy database comprises various functions related to ligninolytic enzymes, such as fungal aryl alcohol oxidases (AAO) and glucose oxidases, both of which are flavoenzymes.
Yann Mathieu +6 more
semanticscholar +7 more sources
Nicotinoprotein [NAD(P)‐containing] alcohol/aldehyde oxidoreductases [PDF]
European Journal of Biochemistry, 1993 Extracts of Gram‐positive bacteria like Rhodococcus rhodochrous, Rhodococcus erythropolis and Amycolatopsis methanolica, but not those of several Gram‐negative ones, showed dehydrogenase activity for ethanol as well as for methanol when 4‐nitroso‐N, N‐dimethylaniline (NDMA) was used as electron acceptor.
Peter W. Van Ophem +2 more
semanticscholar +5 more sources
Substrate diffusion and oxidation in GMC oxidoreductases: an experimental and computational study on fungal aryl-alcohol oxidase [PDF]
Biochemical Journal, 2011 AAO (aryl-alcohol oxidase) provides H2O2 in fungal degradation of lignin, a process of high biotechnological interest. The crystal structure of AAO does not show open access to the active site, where different aromatic alcohols are oxidized. In the present study we investigated substrate diffusion and oxidation in AAO compared with the structurally ...
Aitor Hernández‐Ortega +5 more
semanticscholar +6 more sources
Expanding the Application Range of Microbial Oxidoreductases by an Alcohol Dehydrogenase from Comamonas testosteroni with a Broad Substrate Spectrum and pH Profile [PDF]
Catalysts, 2020 Alcohol dehydrogenases catalyse the conversion of a large variety of ketone substrates to the corresponding chiral products. Due to their high regio- and stereospecificity, they are key components in a wide range of industrial applications.
Daniel Bakonyi +5 more
openalex +2 more sources
Novel NADP-linked alcohol–aldehyde/ketone oxidoreductase in thermophilic ethanologenic bacteria [PDF]
Biochemical Journal, 1981 An NADP-specific alcohol--aldehyde/ketone oxidoreductase was detected in cell extracts of Thermoanaerobium brockii and Clostridium thermohydrosulfuricum, but not in Thermobacteroides acetoethylicus or Clostridium thermocellum. The enzyme was purified from Ta. brockii by differential procedures that included heat treatment and an affinity-chromatography
Raphael Lamed, J. G. Zeikus
openalex +4 more sources
Biotechnology for Biofuels, 2019 Background The glucose–methanol–choline (GMC) superfamily is a large and functionally diverse family of oxidoreductases that share a common structural fold.
Leander Sützl +4 more
doaj +2 more sources