Characterization of human oxidoreductases involved in aldehyde odorant metabolism. [PDF]
AbstractOxidoreductases 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. Among them, some were additionally shown to be involved in chemosensory perception, acting in signal ...
Boichot V+12 more
europepmc +9 more sources
Biosynthetic Strategies of Berberine Bridge Enzyme-like Flavoprotein Oxidases toward Structural Diversification in Natural Product Biosynthesis. [PDF]
Berberine bridge enzyme-like oxidases are often involved in natural product biosynthesis and are seen as essential enzymes for the generation of intricate pharmacophores.
Tjallinks G, Mattevi A, Fraaije MW.
europepmc +3 more sources
Direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase [PDF]
This work reports on the direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase (DgAOR), a molybdenum enzyme of the xanthine oxidase family that contains three redox‐active cofactors: two [2Fe‐2S] centers and a molybdopterin cytosine dinucleotide cofactor.
José J. G. Moura+5 more
openaire +3 more sources
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
openaire +2 more sources
Supersulfide biology and translational medicine for disease control
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
Tungsten‐containing aldehyde oxidoreductase of Eubacterium acidaminophilum [PDF]
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.
Jan R. Andreesen+4 more
openaire +3 more sources
The oxygen-independent metabolism of cyclic monoterpenes in Castellaniella defragrans 65Phen [PDF]
BACKGROUND: The facultatively anaerobic betaproteobacterium Castellaniella defragrans 65Phen utilizes acyclic, monocyclic and bicyclic monoterpenes as sole carbon source under oxic as well as anoxic conditions.
Becher, D.+7 more
core +2 more sources
Comparative genomics and mutagenesis analyses of choline metabolism in the marine Roseobacter clade [PDF]
Choline is ubiquitous in marine eukaryotes and appears to be widely distributed in surface marine waters; however, its metabolism by marine bacteria is poorly understood.
Andresen P.A.+6 more
core +1 more source
Immunochemical characterization of aldo-keto reductases from human tissues [PDF]
Aldose reductase, aldehyde reductase and carbonyl reductase constitute a family of monomeric NADPH-dependent oxidoreductases with similar physical and chemical properties.
Wermuth, Bendicht, Wirth, Hans-Peter
core +1 more source
Multiple implications of an active site phenylalanine in the catalysis of aryl-alcohol oxidase [PDF]
Aryl-alcohol oxidase (AAO) has demonstrated to be an enzyme with a bright future ahead due to its biotechnological potential in deracemisation of chiral compounds, production of bioplastic precursors and other reactions of interest.
Amengual-Rigo, Pep+6 more
core +6 more sources