NAD(P)<sup>+</sup>-dependent alcohol oxidoreductases oxidize 7-hydroxycannabidiol to a reactive formyl metabolite. [PDF]
Wu Q +4 more
europepmc +5 more sources
Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity [PDF]
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
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Novel NADP-linked alcohol–aldehyde/ketone oxidoreductase in thermophilic ethanologenic bacteria [PDF]
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
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Alcohol abuse is associated with enhanced pulmonary and systemic xanthine oxidoreductase activity [PDF]
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
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Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase [PDF]
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
Kamila Napora‐Wijata +5 more
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Steroid Oxidoreductase Activity of Alcohol Dehydrogenases from Horse, Rat, and Human Liver. [PDF]
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
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Nicotinoprotein [NAD(P)‐containing] alcohol/aldehyde oxidoreductases [PDF]
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
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Activities of Secreted Aryl Alcohol Quinone Oxidoreductases from Pycnoporus cinnabarinus Provide Insights into Fungal Degradation of Plant Biomass [PDF]
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
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Coupled oxidoreductase activity of horse liver alcohol dehydrogenase
Abstract Two assay procedures were used to study ethanol oxidation by crystalline horse liver alcohol dehydrogenase: (A) Acetaldehyde formed by ethanol oxidation (with and without lactaldehyde) was distilled into a semicarbazide solution and the absorbance of the acetaldehyde semicarbazone formed was measured at 224 nm.
Charles L. Woodley, Naba K. Gupta
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Substrate diffusion and oxidation in GMC oxidoreductases: an experimental and computational study on fungal aryl-alcohol oxidase [PDF]
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
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