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Biotechnology and Applied Biochemistry Dec 2023Oxidoreductases are enzymes with distinctive characteristics that favor their use in different areas, such as agriculture, environmental management, medicine, and... (Review)
Review
Oxidoreductases are enzymes with distinctive characteristics that favor their use in different areas, such as agriculture, environmental management, medicine, and analytical chemistry. Among these enzymes, oxidases, dehydrogenases, peroxidases, and oxygenases are very interesting. Because their substrate diversity, they can be used in different biocatalytic processes by homogeneous and heterogeneous catalysis. Immobilization of these enzymes has favored their use in the solution of different biotechnological problems, with a notable increase in the study and optimization of this technology in the last years. In this review, the main structural and catalytical features of oxidoreductases, their substrate specificity, immobilization, and usage in biocatalytic processes, such as bioconversion, bioremediation, and biosensors obtainment, are presented.
Topics: Oxidoreductases; Peroxidases; Enzymes, Immobilized; Biodegradation, Environmental; Biotechnology
PubMed: 37753743
DOI: 10.1002/bab.2513 -
Molecules (Basel, Switzerland) May 2023A 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... (Review)
Review
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 -I felt like I was travelling back in time (and space), bringing together the people that have contributed most to this area of research. I sincerely hope that I can give my collaborators the credit they deserve. This study is not presented as a chronologic narrative but as a grouping of topics, the development of which occurred over many years.
Topics: Humans; Aldehyde Oxidoreductases; Desulfovibrio gigas; Desulfovibrio; Molybdenum; Aldehyde Dehydrogenase
PubMed: 37241969
DOI: 10.3390/molecules28104229 -
Analytical Sciences : the International... Oct 2008Due to their unique characteristics ionic liquids (ILs) have been extensively used as solvents in enzymatic procedures, proving to be advantageous alternatives to... (Review)
Review
Due to their unique characteristics ionic liquids (ILs) have been extensively used as solvents in enzymatic procedures, proving to be advantageous alternatives to conventional organic solvents. The studies of enzyme behavior in ILs have increased exponentially in the last years and oxidoreductases particularly have recently started to be studied. The association of oxidoreductases with IL is very promising due to the large field of application of these enzymes. The materials are very interesting not only from the analytical point of view but also in the biocatalytic perspective. In this review, we discuss the behavior of oxidoreductases in the presence of ILs, the mechanisms involved in this association and the immobilization of oxidoreductases in composite materials with IL. The performance of proteins with peroxidase activity in ILs is also reviewed. Future trends and perspectives related with the development of biocatalytic studies involving oxidoreductases and ILs are also considered.
Topics: Animals; Enzymes, Immobilized; Humans; Ionic Liquids; Oxidoreductases; Peroxidase
PubMed: 18845879
DOI: 10.2116/analsci.24.1231 -
Advances in Protein Chemistry 1996
Review
Topics: Amino Acid Sequence; Archaea; Bacterial Proteins; Fermentation; Hot Temperature; Molecular Sequence Data; Oxidoreductases; Phylogeny
PubMed: 8791625
DOI: 10.1016/s0065-3233(08)60362-9 -
Archives of Toxicology Aug 2022This is an overview of the metabolic reactions of drugs, natural products, physiological compounds, and other (general) chemicals catalyzed by flavin monooxygenase... (Review)
Review
This is an overview of the metabolic reactions of drugs, natural products, physiological compounds, and other (general) chemicals catalyzed by flavin monooxygenase (FMO), monoamine oxidase (MAO), NAD(P)H quinone oxidoreductase (NQO), and molybdenum hydroxylase enzymes (aldehyde oxidase (AOX) and xanthine oxidoreductase (XOR)), including roles as substrates, inducers, and inhibitors of the enzymes. The metabolism and bioactivation of selected examples of each group (i.e., drugs, "general chemicals," natural products, and physiological compounds) are discussed. We identified a higher fraction of bioactivation reactions for FMO enzymes compared to other enzymes, predominately involving drugs and general chemicals. With MAO enzymes, physiological compounds predominate as substrates, and some products lead to unwanted side effects or illness. AOX and XOR enzymes are molybdenum hydroxylases that catalyze the oxidation of various heteroaromatic rings and aldehydes and the reduction of a number of different functional groups. While neither of these two enzymes contributes substantially to the metabolism of currently marketed drugs, AOX has become a frequently encountered route of metabolism among drug discovery programs in the past 10-15 years. XOR has even less of a role in the metabolism of clinical drugs and preclinical drug candidates than AOX, likely due to narrower substrate specificity.
Topics: Aldehyde Oxidase; Biological Products; Humans; Molybdenum; Monoamine Oxidase; Oxidoreductases
PubMed: 35648190
DOI: 10.1007/s00204-022-03304-3 -
Current Opinion in Structural Biology Dec 20162-Oxoacid:ferredoxin oxidoreductases (OFORs) are essential enzymes in microbial one-carbon metabolism. They use thiamine pyrophosphate to reversibly cleave carbon-carbon... (Review)
Review
2-Oxoacid:ferredoxin oxidoreductases (OFORs) are essential enzymes in microbial one-carbon metabolism. They use thiamine pyrophosphate to reversibly cleave carbon-carbon bonds, generating low potential (∼-500mV) electrons. Crystallographic analysis of a recently discovered OFOR, an oxalate oxidoreductase (OOR), has provided a second view of OFOR architecture and active site composition. Using these recent structural data along with the previously determined structures of pyruvate:ferredoxin oxidoreductase, structure-function relationships in this superfamily have been expanded and re-evaluated. Additionally, structural motifs have been defined that better serve to distinguish one OFOR subfamily from another and potentially uncover novel OFORs.
Topics: Coenzymes; Humans; Keto Acids; Oxidoreductases; Phylogeny
PubMed: 27315560
DOI: 10.1016/j.sbi.2016.05.011 -
Molecules (Basel, Switzerland) Jun 2019In the last decade, new types of solvents called deep eutectic solvents (DES) have been synthesized and commercialized. Among their main advantages, they can be... (Review)
Review
In the last decade, new types of solvents called deep eutectic solvents (DES) have been synthesized and commercialized. Among their main advantages, they can be eco-friendly and are easy to synthesize at different molar ratios depending on the desired solvent properties. This review aims to show the different uses of DES in some relevant biocatalytic redox reactions. Here we analyze oxidoreductase-mediated transformations that are performed in the presence of DES and compare them with the ones that avoided those solvents. DES were found to present advantages such as the increase in the product yield and enantiomeric excess in many reactions.
Topics: Animals; Aquatic Organisms; Bacteria; Biocatalysis; Biotechnology; Catalase; Humans; Oxidation-Reduction; Oxidoreductases; Plants; Solvents
PubMed: 31212686
DOI: 10.3390/molecules24112190 -
Journal of Biological Inorganic... Dec 2022Five tungstopterin-containing oxidoreductases were characterized from the hyperthermophile Pyrococcus furiosus. Each enzyme catalyzes the reversible conversion of one or...
Five tungstopterin-containing oxidoreductases were characterized from the hyperthermophile Pyrococcus furiosus. Each enzyme catalyzes the reversible conversion of one or more aldehydes to the corresponding carboxylic acid, but they have different specificities. The physiological functions of only two of these enzymes are known: one, termed GAPOR, is a glycolytic enzyme that oxidizes glyceraldehyde-3-phosphate, while the other, termed AOR, oxidizes multiple aldehydes generated during peptide fermentation. Two of the enzymes have known structures (AOR and FOR). Herein, we focus on WOR5, the fifth tungstopterin enzyme to be discovered in P. furiosus. Expression of WOR5 was previously shown to be increased during cold shock (growth at 72 ℃), although the physiological substrate is not known. To gain insight into WOR5 function, we sought to determine both its structure and identify its intracellular substrate. Crystallization experiments were performed with a concentrated cytoplasmic extract of P. furiosus grown at 72 ℃ and the structure of WOR5 was deduced from the crystals that were obtained. In contrast to a previous report, WOR5 is heterodimeric containing an additional polyferredoxin-like subunit with four [4Fe-4S] clusters. The active site structure of WOR5 is substantially different from that of AOR and FOR and the significant electron density observed adjacent to the tungsten cofactor of WOR5 was modeled as an aliphatic sulfonate. Biochemical assays and product analysis confirmed that WOR5 is an aliphatic sulfonate ferredoxin oxidoreductase (ASOR). A catalytic mechanism for ASOR is proposed based on the structural information and the potential role of ASOR in the cold-shock response is discussed.
Topics: Tungsten; Oxidoreductases; Aldehyde Oxidoreductases; Pyrococcus furiosus; Aldehydes
PubMed: 36269456
DOI: 10.1007/s00775-022-01965-0 -
Experimental Biology and Medicine... Mar 2015The WW domain-containing oxidoreductase (WWOX) encodes a tumor suppressor that is frequently altered in cancer. WWOX binds several proteins and thus is postulated to be... (Review)
Review
The WW domain-containing oxidoreductase (WWOX) encodes a tumor suppressor that is frequently altered in cancer. WWOX binds several proteins and thus is postulated to be involved in a variety of cellular processes. Interestingly, Wwox-knockout mice develop normally in utero but succumb to hypoglycemia and other metabolic defects early in life resulting in their death by 3-4 weeks of age. Cumulative evidence has linked WWOX with cellular metabolism including steroid metabolism, high-density lipoprotein cholesterol (HDL-C) metabolism, bone metabolism and, more recently, glucose metabolism. In this review, we discuss these evolving functions for WWOX and how its deletion affects cellular metabolism and neoplastic progression.
Topics: Animals; Bone and Bones; Cells; Cholesterol, HDL; Disease Models, Animal; Disease Progression; Glucose; Humans; Mice; Mice, Knockout; Neoplasms; Oxidoreductases; Steroids; Tumor Suppressor Proteins; WW Domain-Containing Oxidoreductase
PubMed: 25491415
DOI: 10.1177/1535370214561956 -
Chemical Reviews Jun 2003
Review
Topics: Bacteria; Catalysis; Electron Transport; Free Radicals; Ketone Oxidoreductases; Models, Molecular; Molecular Structure; Pyruvate Synthase
PubMed: 12797832
DOI: 10.1021/cr020423e