Results 11 to 20 of about 6,446 (181)
Direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase [PDF]
European Journal of Biochemistry, 2004 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.
Margarida M. Correia dos Santos +5 more
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Tungsten‐containing aldehyde oxidoreductase of Eubacterium acidaminophilum [PDF]
European 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
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Reduction of Carboxylic Acids by Nocardia Aldehyde Oxidoreductase Requires a Phosphopantetheinylated Enzyme [PDF]
Journal of Biological Chemistry, 2006 Aldehyde oxidoreductase (carboxylic acid reductase (Car)) catalyzes the magnesium-, ATP-, and NADPH-dependent reduction of carboxylic acids to their corresponding aldehydes. Heterologous expression of the car gene in Escherichia coli afforded purified recombinant enzyme with a specific activity nearly 50-fold lower than that of purified native Nocardia
Padmesh Venkitasubramanian +2 more
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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
Raphael Lamed, J. G. Zeikus
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NMR Identification of an Acyl-adenylate Intermediate in the Aryl-aldehyde Oxidoreductase Catalyzed Reaction [PDF]
Journal of Biological Chemistry, 1998 A new one-pot synthesis was designed to prepare benzoyl-AMP under anhydrous conditions in N,N-dimethylformamide. Reaction of benzoic acid with N,N'-carbonyldiimidazole and subsequently with 5'-adenosyl monophosphate gave the mixed anhydride in 76% isolated yield. The structure of benzoyl-AMP was confirmed by mass spectroscopy and 1H-, 31P-, and 13C-NMR.
Tao Li, John P. N. Rosazza
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A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire [PDF]
Science Advances, 2023 Abstract 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 (AOR
Agnieszka Winiarska +8 more
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Evidence for enzyme‐substrate intermediates in the aryl‐aldehyde: NADP oxidoreductase catalysed reduction of salicylate [PDF]
FEBS Letters, 1969 Georg G. Gross
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Investigation of aldehyde oxidase and xanthine oxidoreductase in rainbow trout (Oncorhynchus mykiss) [PDF]
, 2014 Molybdo-flavoenzymes (MFEs), aldehyde oxidase (AOX) and xanthine oxidoreductase (XOR) are involved in the oxidation of N-heterocyclic compounds and aldehydes, many of which are environmental pollutants, drugs and vitamins. This biotransformation generally generates more polar compounds that are more easily excreted, thus MFEs have been classed as ...
Omaro A. Emhmed Aburas
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Combinatorial application of two aldehyde oxidoreductases on isobutanol production in the presence of furfural [PDF]
Journal of Industrial Microbiology and Biotechnology, 2015 Abstract Furfural is a toxic by-product formulated from pretreatment processes of lignocellulosic biomass. In order to utilize the lignocellulosic biomass on isobutanol production, inhibitory effect of the furfural on isobutanol production was investigated and combinatorial application of two oxidoreductases, FucO and YqhD, was suggested
Hyeongmin Seo +11 more
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Chemistry – 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
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