Relevant bibliographies by topics / Aldehyde oxidoreductase

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Academic literature on the topic 'Aldehyde oxidoreductase'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Aldehyde oxidoreductase"

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Bevers, Loes E., Emile Bol, Peter-Leon Hagedoorn, and Wilfred R. Hagen. "WOR5, a Novel Tungsten-Containing Aldehyde Oxidoreductase from Pyrococcus furiosus with a Broad Substrate Specificity." Journal of Bacteriology 187, no. 20 (October 15, 2005): 7056–61. http://dx.doi.org/10.1128/jb.187.20.7056-7061.2005.

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ABSTRACT WOR5 is the fifth and last member of the family of tungsten-containing oxidoreductases purified from the hyperthermophilic archaeon Pyrococcus furiosus. It is a homodimeric protein (subunit, 65 kDa) that contains one [4Fe-4S] cluster and one tungstobispterin cofactor per subunit. It has a broad substrate specificity with a high affinity for several substituted and nonsubstituted aliphatic and aromatic aldehydes with various chain lengths. The highest catalytic efficiency of WOR5 is found for the oxidation of hexanal (V max = 15.6 U/mg, Km = 0.18 mM at 60°C). Hexanal-incubated enzyme exhibits S = 1/2 electron paramagnetic resonance signals from [4Fe-4S]1+ (g values of 2.08, 1.93, and 1.87) and W5+ (g values of 1.977, 1.906, and 1.855). Cyclic voltammetry of ferredoxin and WOR5 on an activated glassy carbon electrode shows a catalytic wave upon addition of hexanal, suggesting that ferredoxin can be a physiological redox partner. The combination of WOR5, formaldehyde oxidoreductase, and aldehyde oxidoreductase forms an efficient catalyst for the oxidation of a broad range of aldehydes in P. furiosus.
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GARATTINI, Enrico, Ralf MENDEL, Maria João ROMÃO, Richard WRIGHT, and Mineko TERAO. "Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology." Biochemical Journal 372, no. 1 (May 15, 2003): 15–32. http://dx.doi.org/10.1042/bj20030121.

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The molybdo–flavoenzymes are structurally related proteins that require a molybdopterin cofactor and FAD for their catalytic activity. In mammals, four enzymes are known: xanthine oxidoreductase, aldehyde oxidase and two recently described mouse proteins known as aldehyde oxidase homologue 1 and aldehyde oxidase homologue 2. The present review article summarizes current knowledge on the structure, enzymology, genetics, regulation and pathophysiology of mammalian molybdo–flavoenzymes. Molybdo–flavoenzymes are structurally complex oxidoreductases with an equally complex mechanism of catalysis. Our knowledge has greatly increased due to the recent crystallization of two xanthine oxidoreductases and the determination of the amino acid sequences of many members of the family. The evolution of molybdo–flavoenzymes can now be traced, given the availability of the structures of the corresponding genes in many organisms. The genes coding for molybdo–flavoenzymes are expressed in a cell-specific fashion and are controlled by endogenous and exogenous stimuli. The recent cloning of the genes involved in the biosynthesis of the molybdenum cofactor has increased our knowledge on the assembly of the apo-forms of molybdo–flavoproteins into the corresponding holo-forms. Xanthine oxidoreductase is the key enzyme in the catabolism of purines, although recent data suggest that the physiological function of this enzyme is more complex than previously assumed. The enzyme has been implicated in such diverse pathological situations as organ ischaemia, inflammation and infection. At present, very little is known about the pathophysiological relevance of aldehyde oxidase, aldehyde oxidase homologue 1 and aldehyde oxidase homologue 2, which do not as yet have an accepted endogenous substrate.
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Chen, Jun, and Shulin Yang. "Catalytic mechanism of UDP-glucose dehydrogenase." Biochemical Society Transactions 47, no. 3 (June 12, 2019): 945–55. http://dx.doi.org/10.1042/bst20190257.

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AbstractUDP-glucose dehydrogenase (UGDH), an oxidoreductase, catalyzes the NAD+-dependent four-electron oxidation of UDP-glucose to UDP-glucuronic acid. The catalytic mechanism of UGDH remains controversial despite extensive investigation and is classified into two types according to whether an aldehyde intermediate is generated in the first oxidation step. The first type, which involves the presence of this putative aldehyde, is inconsistent with some experimental findings. In contrast, the second type, which indicates that the first oxidation step bypasses the aldehyde via an NAD+-dependent bimolecular nucleophilic substitution (SN2) reaction, is consistent with the experimental phenomena, including those that cannot be explained by the first type. This NAD+-dependent SN2 mechanism is thus more reasonable and likely applicable to other oxidoreductases that catalyze four-electron oxidation reactions.
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Rauh, David, Andrea Graentzdoerffer, Katrin Granderath, Jan R. Andreesen, and Andreas Pich. "Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum." European Journal of Biochemistry 271, no. 1 (December 19, 2003): 212–19. http://dx.doi.org/10.1111/j.1432-1033.2004.03922.x.

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Badalyan, Artavazd, Meina Neumann-Schaal, Silke Leimkühler, and Ulla Wollenberger. "A Biosensor for Aromatic Aldehydes Comprising the Mediator Dependent PaoABC-Aldehyde Oxidoreductase." Electroanalysis 25, no. 1 (October 10, 2012): 101–8. http://dx.doi.org/10.1002/elan.201200362.

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Correia dos Santos, Margarida M., Patrícia M. P. Sousa, M. Lurdes S. Gonçalves, M. João Romão, Isabel Moura, and José J. G. Moura. "Direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase." European Journal of Biochemistry 271, no. 7 (March 23, 2004): 1329–38. http://dx.doi.org/10.1111/j.1432-1033.2004.04041.x.

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Andrade, Susana L. A., Carlos D. Brondino, Maria J. Feio, Isabel Moura, and José J. G. Moura. "Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491." European Journal of Biochemistry 267, no. 7 (April 2000): 2054–61. http://dx.doi.org/10.1046/j.1432-1327.2000.01209.x.

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Rivas, Maria Gabriela, Pablo Javier Gonzalez, Felix Martin Ferroni, Alberto Claudio Rizzi, and Carlos Brondino. "Studying Electron Transfer Pathways in Oxidoreductases." Science Reviews - from the end of the world 1, no. 2 (March 16, 2020): 6–23. http://dx.doi.org/10.52712/sciencereviews.v1i2.15.

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Oxidoreductases containing transition metal ions are widespread in nature and are essential for living organisms. The copper-containing nitrite reductase (NirK) and the molybdenum-containing aldehyde oxidoreductase (Aor) are typical examples of oxidoreductases. Metal ions in these enzymes are present either as mononuclear centers or organized into clusters and accomplish two main roles. One of them is to be the active site where the substrate is converted into product, and the other one is to serve as electron transfer center. Both enzymes transiently bind the substrate and an external electron donor/acceptor in NirK/Aor, respectively, at distinct protein points for them to exchange the electrons involved in the redox reaction. Electron exchange occurs through a specific intra-protein chemical pathway that connects the different enzyme metal cofactors. Based on the two oxidoreductases presented here, we describe how the different actors involved in the intra-protein electron transfer process can be characterized and studied employing molecular biology, spectroscopic, electrochemical, and structural techniques.
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Golwala, Neel H., Christopher Hodenette, Subramanyam N. Murthy, Bobby D. Nossaman, and Philip J. Kadowitz. "Vascular responses to nitrite are mediated by xanthine oxidoreductase and mitochondrial aldehyde dehydrogenase in the ratThis article is one of a selection of papers published in a special issue on Advances in Cardiovascular Research." Canadian Journal of Physiology and Pharmacology 87, no. 12 (December 2009): 1095–101. http://dx.doi.org/10.1139/y09-101.

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Sodium nitrite has been shown to have vasodilator activity in experimental animals and in human subjects. However, the mechanism by which nitrite anion is converted to vasoactive nitric oxide (NO) is uncertain. It has been hypothesized that deoxyhemoglobin, xanthine oxidoreductase, mitochondrial aldehyde dehydrogenase, and other heme proteins can reduce nitrite to NO, but studies in the literature have not identified the mechanism in the intact rat, and several studies report no effect of inhibitors of xanthine oxidoreductase. In the present study, the effects of the xanthine oxidoreductase inhibitor allopurinol and the mitochondrial aldehyde dehydrogenase inhibitor cyanamide on decreases in mean systemic arterial pressure in response to i.v. sodium nitrite administration were investigated in the rat. The decreases in mean systemic arterial pressure in response to i.v. administration of sodium nitrite were inhibited in a selective manner after administration of allopurinol in a dose of 25 mg/kg i.v. A second 25 mg/kg i.v. dose had no additional inhibitory effect on the response to sodium nitrite. The decreases in mean systemic arterial pressure in response to sodium nitrite were attenuated by cyanamide and a second 25 mg/kg i.v. dose had no additional inhibitory effect. In l-NAME-treated animals, allopurinol attenuated responses to sodium nitrite and a subsequent administration of cyanamide had no additional effect. When the order of administration of the inhibitors was reversed, responses to sodium nitrite were attenuated by administration of cyanamide and a subsequent administration of allopurinol had no additional inhibitory effect. The results of these studies suggest that nitrite can be reduced to vasoactive NO in the systemic vascular bed of the rat by xanthine oxidoreductase and mitochondrial aldehyde dehydrogenase and that the 2 pathways of nitrite activation act in a parallel manner.
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Chan, M., S. Mukund, A. Kletzin, M. Adams, and D. Rees. "Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase." Science 267, no. 5203 (March 10, 1995): 1463–69. http://dx.doi.org/10.1126/science.7878465.

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Dissertations / Theses on the topic "Aldehyde oxidoreductase"

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Aburas, Omaro A. Emhmed. "Investigation of aldehyde oxidase and xanthine oxidoreductase in rainbow trout (Oncorhynchus mykiss)." Thesis, University of Huddersfield, 2014. http://eprints.hud.ac.uk/id/eprint/23543/.

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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 detoxication enzymes. To date there has been scant study of the properties, substrate and inhibitor specificities of MFEs in non-mammalian vertebrate organisms. This investigation focuses on MFEs in rainbow trout (Oncorhynchus mykiss) as it belongs to a class of fish that host a single AOX (AOXβ) and one XOR. In this study the substrate specificity of rainbow trout liver AOX and XOR was investigated using HPLC and spectrophotometric assays. AOX in hepatic cytosol was found to be able to catalyse the oxidation of azanaphthalenes belonging to a group of compounds that are environmental pollutants such as phenanthridine, phthalazine and cinchonine. In addition, xenobiotic aromatic aldehydes (vanillin and dimethylaminocinnamaldehyde) and drugs such as allopurinol and pyrazinamide were substrates. Several endogenous vitamins including pyridoxal (vitamin B6), all-trans retinal (vitamin A) and N1-methylnicotinamide were also biotransformed by the rainbow trout AOX. In contrast to liver no AOX activity was detectable in kidney and gill tissue. XOR activity in rainbow trout liver was measurable with the endogenous purine xanthine, purine drug metabolites (1-methylxanthine and 6-thioxanthine) and N-heterocyclic drugs (allopurinol and pyrazinamide). Unlike mammalian XOR that can utilise both NAD+ and O2 as electron acceptors, trout XOR was exclusively NAD+-dependent with no activity being detected with O2. Eadie-Hofstee plots were using to determine the Km and Vmax of rainbow trout AOX and XOR with different substrates and it was found the Vmax of the rainbow trout enzymes were generally lower and Km generally higher than mammalian AOX and XOR. Inhibitors of mammalian AOX were tested to determine if they could interact with the piscine AOX. Environmental pollutants (17α-ethinyl estradiol and phenanthridine), an endogenous steroid (estradiol) and drugs (chlorpromazine and menadione) were found to be effective inhibitors and were classed as competitive, non-competitive and uncompetitive respectively using Lineweaver-Burk plots. The drug metabolite, oxipurinol, was a non-competitive inhibitor of rainbow trout XOR. In order to further characterise trout AOX protein purification was carried out. In contrast to mammalian AOX, the piscine enzyme was not thermotolerant at 55°C nor was it inhibited by benzamidine, thus heat treatment and affinity chromatography could not be used as a purification steps. Trout AOX was purified 210-fold using ammonium sulphate fractionation, together with ion exchange and gel filtration chromatography. The native molecular mass of the piscine AOX was 295 kDa, which is similar to mammalian AOXs. In conclusion this study yields new insight into groups of anthropogenic environmental pollutants, drugs and vitamins that are substrates and inhibitors of an ancestral vertebrate AOX. The toxicological relevance of these findings is discussed.
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Norin, Annika. "Medium chain dehydrogenases/reductases : alcohol dehydrogenases of novel types /." Stockholm, 2003. http://diss.kib.ki.se/2003/91-7349-675-8/.

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3

"Response of sodium nitrite in the vascular bed of the rat mediated by xanthine oxidoreductase and aldehyde dehydrogenase 2." Tulane University, 2011.

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The purpose of the research presented is to develop a better understanding of the mechanism by which nitrite is converted to nitric oxide. In the present study, the role xanthine oxidoreductase (XOR) and mitochondrial aldehyde dehydrogenase (mALDH2) plays in the mediation of vasodilator responses to sodium nitrite, the role nitrite plays in nitroglycerin induced vasodilation, the effect chronic treatment with sodium nitrite on monocrotaline induced pulmonary hypertension, and the response to peroxynitrite, a nitrite metabolite, was investigated using right heart catheterization techniques to measure pulmonary arterial pressure and the thermodilution technique to measure cardiac output In the first set of experiments, iv injections of sodium nitrite produced dose related decreases in systemic and pulmonary arterial pressures and increases in cardiac output. The decreases in pulmonary arterial pressure were enhanced when baseline tone was increased by U46619, hypoxia and treatment with L-NAME. Pulmonary and systemic vasodilator responses to sodium nitrite were attenuated by treatment with the XOR inhibitor allopurinol or the mALDH2 inhibitor cyanamide and these agents did not alter responses to the NO donors sodium nitroprusside or DEA/NO. The decreases in pulmonary arterial pressure under elevated tone conditions were similar when the rats breathed room air or a 10% O2 and 90% N2 gas mixture. In experiments in which systemic vasodilator responses were evaluated combination treatment with allopurinol and cyanamide did not produce a greater reduction in the response to sodium nitrite than did treatment with either agent alone In the experiments investigating the role nitrite plays in nitroglycerin induced vasodilation, intravenous injections of GTN and sodium nitrite decreased pulmonary and systemic arterial pressures and increased cardiac output. The decreases in pulmonary arterial pressure under baseline and elevated tone conditions and decreases in systemic arterial pressure in response to GTN and sodium nitrite were attenuated by cyanamide, an ALDH2 inhibitor, whereas responses to the NO donor, sodium nitroprusside (SNP), were not altered. The decreases in pulmonary and systemic arterial pressure in response to GTN and SNP were not altered by allopurinol, an inhibitor of xanthine oxidoreductase (XOR), whereas responses to sodium nitrite were attenuated. GTN was approximately 1000 fold more potent than sodium nitrite in decreasing pulmonary and systemic arterial pressures. These results suggest that ALDH2 plays an important role in the bioactivation of GTN and nitrite in the pulmonary and systemic vascular beds but that the reduction of nitrite to vasoactive NO does not play an important role in mediating vasodilator responses to GTN in the intact chest rat In experiments in which the responses to peroxynitrite (PN) were investigated, the results show that injections of PN in doses of 10 -- 100 mmol/kg iv produced dose-related decreases in the pulmonary and systemic arterial pressure in the intact rat and that these responses were enhanced when tone was increased. The vasodilator responses were rapid in onset, short in duration, and reproducible. In addition, injections of 2 mmol/kg of L-PEN did not alter vasodilator responses of PN in the pulmonary and systemic vascular beds of the intact rat These data provide evidence in support of the hypothesis that XOR and mALDH2 can play a role in the bioactivation of nitrite in the rat, that pulmonary vasodilator responses to nitrite are not modulated by ventilatory hypoxia, and that monocrotaline induced pulmonary hypertension can be alleviated by chronic administration of sodium nitrite. These data also provide evidence that nitrite may not play a major role in NTG bioactivation and that peroxynitrite, a product of interaction of NO and superoxide, has potent vasodilator activity in the pulmonary and systemic vascular beds of the intact rat. These data suggest that multiple pathways are involved in the bioactivation of nitrite in the cardiovascular system of the rat and that sodium nitrite may be useful as a treatment for pulmonary hypertension. (Abstract shortened by UMI.)
acase@tulane.edu
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Roy, Roopali. "Tungsten-containing aldehyde oxidoreductases : a novel family of enzymes from hyperthermophilic archaea." 2001. http://purl.galileo.usg.edu/uga%5Fetd/roy%5Froopali%5F200112%5Fphd.

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Thesis (Ph. D.)--University of Georgia, 2001.
Includes articles published in Methods in enzymology, and Journal of becteriology, and articles submitted to Journal of bacteriology, and Journal of biological chemistry. Directed by M.W.W. Adams. Includes bibliographical references (leaves 232-234).
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Books on the topic "Aldehyde oxidoreductase"

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International Workshop on the Enzymology and Molecular Biology of the Carbonyl Metabolism (5th 1990 West Lafayette, Ind.). Enzymology and molecular biology of carbonyl metabolism 3. New York: Plenum Press, 1991.

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International Workshop on the Enzymology and Molecular Biology of the Carbonyl Metabolism. Enzymology and molecular biology of carbonyl metabolism 3. New York: Plennum Press, 1991.

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Henry, Weiner, Flynn T. Geoffrey, and International Workshop on the Enzymology and Molecular Biology of the Carbonyl Metabolism (1988 : Gifu-shi, Japan), eds. Enzymology and molecular biology of carbonyl metabolism 2: Aldehyde dehydrogenase, alcohol dehydrogenase, and aldo-keto reductase : proceedings of the fourth international workshop, held in Gifu, Japan, July 4-8, 1988. New York: Liss, 1989.

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Henry, Weiner, Flynn T. Geoffrey, and International Workshop on Carbonyl Metabolism (4th : 1988 : Gifu Japan), eds. Enzymology and molecular biology of carbonyl metabolism 2: Aldehyde dehydrogenase, alcohol dehydrogenase, and carbonyl reductase. New York: Liss, 1989.

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Henry, Weiner, Flynn T. Geoffrey, and International Workshop on Carbonyl Metabolism (3rd : 1986 : Espoo, Finland), eds. Enzymology and molecular biology of carbonyl metabolism: Aldehyde dehydrogenase, aldo-keto reductase, and alcohol dehydrogenase : proceedings of an international workshop held in Espoo, Finland, June 14-16, 1986. New York: A.R. Liss, 1987.

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Enzymology and Molecular Biology of Carbonyl Metabolism 6. Springer, 2011.

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Weiner, Henry. Enzymology and Molecular Biology of Carbonyl Metabolism 6. Springer, 2013.

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Henry, Weiner, and International Workshop on the Enzymology and Molecular Biology of the Carbonyl Metabolism (8th : 1996 : Deadwood, S.D.), eds. Enzymology and molecular biology of carbonyl metabolism 6. New York: Plenum Press, 1997.

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Henry, Weiner, Crabb David W, Flynn T. Geoffrey, and International Workshop on Enzymology and Molecular Biology of Carbonyl Metabolism (6th : 1992 : Dublin, Ireland), eds. Enzymology and molecular biology of carbonyl metabolism 4. New York: Plenum Press, 1993.

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Enzymology and Molecular Biology of Carbonyl Metabolism 4. Springer, 2011.

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Book chapters on the topic "Aldehyde oxidoreductase"

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Kozminski, Kirk D., and Michael A. Zientek. "Differentiation of Cytochrome P450-Mediated from Non-CYP-Mediated Metabolism: Aldehyde Oxidase and Xanthine Oxidoreductase." In Methods in Pharmacology and Toxicology, 277–89. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1542-3_17.

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Piersma, Sander R., Simon de Vries, and Johannis A. Duine. "Nicotinoprotein Alcohol/Aldehyde Oxidoreductases." In Advances in Experimental Medicine and Biology, 425–34. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5871-2_48.

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van Ophem, Peter W., and Johannis A. Duine. "Microbial Alcohol, Aldehyde and Formate Ester Oxidoreductases." In Advances in Experimental Medicine and Biology, 605–20. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2904-0_63.

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Geerlof, A., J. B. A. Tol, J. A. Jongejan, and J. A. Duine. "Microbial Alcohol/Aldehyde Oxidoreductases in Enantioselective Conversions." In Microbial Reagents in Organic Synthesis, 411–20. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2444-7_33.

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Götz, Katharina, Lutz Hilterhaus, and Andreas Liese. "Industrial Application of Oxidoreductase Catalyzed Reduction of Ketones and Aldehydes." In Enzyme Catalysis in Organic Synthesis, 1205–23. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2012. http://dx.doi.org/10.1002/9783527639861.ch29.

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"Aldehyde ferredoxin oxidoreductase." In Class 1 · Oxidoreductases, 188–202. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-85188-2_30.

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Roy, Roopali, and Michael Adams. "Tungsten-Dependent Aldehyde Oxidoreductase." In Metal Ions in Biological Systems. CRC Press, 2002. http://dx.doi.org/10.1201/9780203909331.ch19.

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Beedham, C. "Xanthine Oxidoreductase and Aldehyde Oxidase*." In Comprehensive Toxicology, 185–205. Elsevier, 2010. http://dx.doi.org/10.1016/b978-0-08-046884-6.00410-3.

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Garattini, E., and M. Terao. "Xanthine Oxidoreductase and Aldehyde Oxidases." In Comprehensive Toxicology, 208–32. Elsevier, 2018. http://dx.doi.org/10.1016/b978-0-12-801238-3.99184-0.

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"Tungsten-Dependent Aldehyde Oxidoreductase: A New Family of Enzymes Containing the Pterin Cofactor." In Metals Ions in Biological System, 529–48. CRC Press, 2002. http://dx.doi.org/10.1201/9780203909331-28.

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