Results 1 to 10 of about 6,092 (169)
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. We also evaluated the enzyme activity (oxidoreductases) for enantioselective oxidation reactions, by using derivatives of (RS)
Thaís P. Garcia +4 more
doaj +6 more sources
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. The purified enzyme was characterized in vitro. The substrate scope for YlADH2 mediated oxidation and
Margit Winkler +5 more
doaj +7 more sources
Alcohol abuse is associated with enhanced pulmonary and systemic xanthine oxidoreductase activity [PDF]
American Journal of Physiology-Lung Cellular and Molecular Physiology, 2017 Acute respiratory distress syndrome (ARDS) is a common and devastating disorder. Alcohol use disorders (AUDs) increase ARDS risk and worsen outcomes through mechanisms that may include enhancement of pulmonary oxidative stress. Alcohol consumption increases activity of the enzyme xanthine oxidoreductase (XOR) that contributes to production of both ...
Mehdi A. Fini +4 more
openaire +3 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 +6 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
R J Lamed, J G Zeikus
openaire +4 more sources
Steroid Oxidoreductase Activity of Alcohol Dehydrogenases from Horse, Rat, and Human Liver. [PDF]
Acta Chemica Scandinavica, 1975 Alcohol dehydrogenase from horse (isoenzyme SS and ES, but not EE), rat and human liver were found to catalyze the NAD-dependent oxidation of 3beta-hydroxy groups in 5alpha- and 5beta-steroids of the C19, C21, and C24 series. The enzymes from horse and rat liver were more active on 5beta-than on 5alpha-steroids. This difference was most marked with the
Tomas Cronholm +5 more
openaire +4 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 +5 more
openaire +6 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
openaire +5 more sources
Engineering in Life Sciences, 2006 AbstractBiocatalytic processes are useful methods for the production of chiral intermediates. As an example, alcohol dehydrogenases are applied for the production of chiral alcohols by asymmetric reduction of prochiral ketones. From this class of enzymes alcohol dehydrogenase from Lactobacillus brevis will be described with respect to its industrial ...
T. Daußmann +2 more
openaire +3 more sources
Supersulfide biology and translational medicine for disease control
British Journal of Pharmacology, EarlyView., 2023 Abstract For decades, the major focus of redox biology has been oxygen, the most abundant element on Earth. Molecular oxygen functions as the final electron acceptor in the mitochondrial respiratory chain, contributing to energy production in aerobic organisms. In addition, oxygen‐derived reactive oxygen species including hydrogen peroxide and nitrogen
Uladzimir Barayeu +5 more
wiley +1 more source