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 +5 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 +5 more sources
Iron-Containing Alcohol Dehydrogenase from Hyperthermophiles [PDF]
BioTechIron-containing alcohol dehydrogenases (Fe-ADHs) from hyperthermophiles represent a distinct class of oxidoreductases characterized by exceptional thermostability, catalytic versatility, and unique metal-dependent properties.
Ching Tse, Kesen Ma
doaj +2 more sources
NAD(P)<sup>+</sup>-dependent alcohol oxidoreductases oxidize 7-hydroxycannabidiol to a reactive formyl metabolite. [PDF]
Arch ToxicolCannabidiol (CBD) undergoes oxidation to 7-hydroxy-CBD in the liver via cytochrome P450 enzymes. 7-Hydroxy-CBD can be further oxidized to 7-carboxy-CBD, the principal circulating metabolite in humans. An aldehyde intermediate, 7-formyl-CBD, is hypothesized to be the precursor of 7-carboxy-CBD; however, the formation of 7-formyl-CBD and the enzymes ...
Wu Q +4 more
europepmc +3 more sources
Engineering a newly identified alcohol dehydrogenase from Sphingobium Sp. for efficient utilization of nicotinamide cofactors biomimetics [PDF]
Bioresources and BioprocessingNicotinamide cofactor biomimetics (NCBs) serve as low-cost alternatives to the expensive NAD(P)+/NAD(P)H, holding significant potential for applications in oxidoreductases. In this study, an alcohol dehydrogenase (SpADH2) from Sphingobium sp.
Yichun Zhu +5 more
doaj +2 more sources
Biofuel Cells Based on Oxidoreductases and Electroactive Nanomaterials: Development and Characterization [PDF]
BiosensorsAmperometric biosensors (ABSs) and enzymatic biofuel cells (BFCs) share several fundamental principles in their functionality, despite serving different primary purposes.
Olha Demkiv +5 more
doaj +2 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. A novel alcohol dehydrogenase from Comamonas testosteroni (CtADH) was identified in silico, recombinantly ...
Daniel Bakonyi +2 more
exaly +4 more sources
Adaptive evolution of electron transfer pathways in Thermoanaerobacterium saccharolyticum [PDF]
Journal of BacteriologyThermoanaerobacterium saccharolyticum is an anaerobic, thermophilic bacterium that has been proposed for use in consolidated bioprocessing in coculture with cellulolytic bacteria such as Clostridium thermocellum for ethanol production. Although the mixed
João H. T. M. Fabri +5 more
doaj +2 more sources
Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity [PDF]
Chemistry – A European Journal, 2020 AbstractThe l‐lysine‐ϵ‐dehydrogenase (LysEDH) from Geobacillus stearothermophilus naturally catalyzes the oxidative deamination of the ϵ‐amino group of l‐lysine. 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 ...
Vasilis Tseliou +4 more
openaire +4 more sources
Display of Bombyx mori alcohol dehydrogenases on the Bacillus subtilis spore surface to enhance enzymatic activity under adverse conditions. [PDF]
PLoS ONE, 2011 Alcohol dehydrogenases (ADHs) are oxidoreductases catalyzing the reversible oxidation of alcohols to corresponding aldehydes or ketones accompanied by nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP) as ...
Nan Wang +6 more
doaj +1 more source