Results 1 to 10 of about 195,873 (193)

Characterization of human oxidoreductases involved in aldehyde odorant metabolism [PDF]

open access: goldScientific Reports, 2023
Oxidoreductases are major enzymes of xenobiotic metabolism. Consequently, they are essential in the chemoprotection of the human body. Many xenobiotic metabolism enzymes have been shown to be involved in chemosensory tissue protection.
Valentin Boichot   +12 more
doaj   +9 more sources

Nicotinoprotein [NAD(P)‐containing] alcohol/aldehyde oxidoreductases [PDF]

open access: bronzeEuropean 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

A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire [PDF]

open access: goldScience Advances, 2023
Aldehyde oxidoreductases (AOR) are tungsten enzymes catalysing the oxidation of many different aldehydes to the corresponding carboxylic acids. In contrast to other known AORs, the enzyme from the denitrifying betaproteobacterium Aromatoleum aromaticum ...
Agnieszka Winiarska   +8 more
semanticscholar   +9 more sources

Minimal aromatic aldehyde reduction (MARE) yeast platform for engineering vanillin production [PDF]

open access: yesBiotechnology for Biofuels and Bioproducts
Background Vanillin represents one of the most widely used flavoring agents in the world. However, microbial synthesis of vanillin is hindered by the host native metabolism that could rapidly degrade vanillin to the byproducts.
Qiwen Mo, Jifeng Yuan
doaj   +3 more sources

Electrocatalytic Aldehyde Oxidation by a Tungsten Dependent Aldehyde Oxidoreductase from Aromatoleum Aromaticum [PDF]

open access: hybridChemistry – A European Journal, 2023
AbstractIn contrast to their molybdenum dependent relatives, tungsten enzymes operate at significantly lower redox potentials, and in some cases they can carry out reversible redox transformations of their substrates and products. Still, the electrochemical properties of W enzymes have received much less attention than their Mo relatives.
Palraj Kalimuthu   +6 more
openalex   +3 more sources

The History of Desulfovibrio gigas Aldehyde Oxidoreductase—A Personal View [PDF]

open access: goldMolecules, 2023
A story going back almost 40 years is presented in this manuscript. This is a different and more challenging way of reporting my research and I hope it will be useful to and target a wide-ranging audience. When preparing the manuscript and collecting references on the subject of this paper—aldehyde oxidoreductase from Desulfovibrio gigas—I felt like I ...
José J. G. Moura
openalex   +4 more sources

Tungsten‐containing aldehyde oxidoreductase of Eubacterium acidaminophilum [PDF]

open access: bronzeEuropean Journal of Biochemistry, 2003
Aldehyde oxidoreductase of Eubacterium acidaminophilum was purified to homogeneity under strict anaerobic conditions using a four‐step procedure. The purified enzyme was present as a monomer with an apparent molecular mass of 67 kDa and contained 6.0 ± 0.1 iron, 1.1 ± 0.2 tungsten, about 0.6 mol pterin cofactor and zinc, but no molybdenum.
David Rauh   +4 more
openalex   +3 more sources

Continuous-wave electron paramagnetic resonance (CW-EPR) for studying structure-function relationships in a Cu-containing nitrite reductase and a Mo-containing aldehyde oxidoreductase

open access: goldJournal of Magnetic Resonance Open, 2023
Transition metal ion-containing oxidoreductases, which carry out long-distance electron transfer reactions, are a large family of metalloproteins that are widely distributed in nature.
Pablo J. González   +3 more
doaj   +2 more sources

Identification of crucial amino acids in mouse aldehyde oxidase 3 that determine substrate specificity.

open access: yesPLoS ONE, 2013
In order to elucidate factors that determine substrate specificity and activity of mammalian molybdo-flavoproteins we performed site directed mutagenesis of mouse aldehyde oxidase 3 (mAOX3).
Martin Mahro   +6 more
doaj   +2 more sources

Molybdenum Incorporation in Tungsten Aldehyde Oxidoreductase Enzymes from Pyrococcus furiosus [PDF]

open access: greenJournal of Bacteriology, 2010
ABSTRACT The hyperthermophilic archaeon Pyrococcus furiosus expresses five aldehyde oxidoreductase (AOR) enzymes, all containing a tungsto-bispterin cofactor. The growth of this organism is fully dependent on the presence of tungsten in the growth medium.
Ana‐Maria Sevcenco   +7 more
openalex   +6 more sources

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