Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
enzyme EF0404 shows both nitroreductase and azoreductase activity. The biochemical characteristics, such as substrate and cofactor specificity, of enzyme EF0404 resemble the properties of the known azoreductase AzoA. But its sequence matches with the nitroreductase group B, the same as enzyme EF0648
evolution
-
phylogeny of azoreductases, overview
evolution
-
phylogeny of azoreductases, overview
evolution
-
phylogeny of azoreductases, overview
evolution
-
phylogeny of azoreductases, overview
evolution
-
phylogeny of azoreductases, overview
evolution
phylogeny of azoreductases, overview
evolution
phylogeny of azoreductases, overview
evolution
the Bacillus subtilis YhdA enzyme belongs to the family of NADPH-dependent flavin mononucleotide oxide reductases and possesses azo-reductase activity. YhdA possesses structural homology with chromate reductases (cf. EC 1.6.5.2), amino acid homology to the two bona fide chromate reductases YieF and ChrR from Escherichia coli and Pseudomonas putida, respectively, with the signature sequence LFVTPEYNXXXXXXLKNAIDXXS, sequence comparisons, overview
metabolism
-
essential role of exclusively extracellular respiration in azo dye decolorization. Electrons from acetate oxidization by this strain are transferred by the respiratory chain to methyl orange. As Geobacter sulfurreducens strain PCA does not express known azo reductases, extracellular electron transfer is an alternative way to decolor methyl orange. Outermembrane cytochromes are reported to play a prominent role in electron acceptor in strain PCS. The outermembrane proteins, OmcB, OmcC, and OmcE, are identified as the key proteins in extracellular reduction by the electrochemically active bacterium
metabolism
-
essential role of exclusively extracellular respiration in azo dye decolorization. Electrons from acetate oxidization by this strain are transferred by the respiratory chain to methyl orange. As Geobacter sulfurreducens strain PCA does not express known azo reductases, extracellular electron transfer is an alternative way to decolor methyl orange. Outermembrane cytochromes are reported to play a prominent role in electron acceptor in strain PCS. The outermembrane proteins, OmcB, OmcC, and OmcE, are identified as the key proteins in extracellular reduction by the electrochemically active bacterium
-
physiological function
-
bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview
physiological function
-
bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview
physiological function
-
bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview
physiological function
-
bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview
physiological function
-
bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview
physiological function
bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview
physiological function
bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview
physiological function
enzyme EF0404 shows both nitroreductase and azoreductase activity. The biochemical characteristics, such as substrate and cofactor specificity, of enzyme EF0404 resemble the properties of the known azoreductase AzoA. But its sequence matches with the nitroreductase group, the same as enzyme EF0648
physiological function
-
molecular dynamics study of biodegradation of azo dyes via their interactions with AzrC azoreductase, molecular dynamics simulations, overview. The active site residues Phe105 (A), Phe125 (B), Phe172 (B), and Pro132 (B) have been found as the most important hydrophobic residues whereas Asn104 (A), Tyr127 (B), and Asn187 (A) have a key role in making hydrogen bonds
physiological function
-
Pseudomonas putida MET94 is a bacteria that degrades a wide range of structurally distinct azo dyes with high efficiency and the azoreductase PpAzoR plays a key role in this process
physiological function
-
the enzyme catalyzes extracellular bioreduction of methyl orange. Geobacter sulfurreducens strain PCA has a very high decolorization efficiency among the methyl orange reducing bacteria
physiological function
-
the enzyme degrades the azo dye naphthol blue black, the reaction product is less toxic than the substrate
physiological function
-
the enzyme is identified as a primary functional membrane-bound azoreductase used by members of the genus Shewanella to degrade azo dyes. Complete degradation of azo dyes by bacteria occurs in two sequential steps. In the first step, reductive cleavage of the azo bond takes place under anaerobic conditions, generating colorless aromatic amines, which are further degraded by aerobic processes. The reduction step is carried out mainly by azoreductase enzymes, which then cleave the azo bond by transferring electrons from reducing equivalents (NADH or NADPH) generated from the metabolism of organic compounds to the dye molecule
physiological function
-
the rate limiting first step of the biodegradation pathway of recalcitrant azo dyes is their decolorization, which involves the reductive cleavage of the azo bond catalysed by the enzyme azoreductase. The enzyme from strain L2 decolorizes a wide spectrum of azo dyes
physiological function
the bacterial flavin mononucleotide/NADPH-dependent oxidoreductase YhdA, widely distributed among Gram-positive bacilli, confers protection to cells from the cytotoxic effects of Cr(VI) and prevents the hypermutagenesis exhibited by a MutT/MutM/MutY-deficient strain. Additionally, a purified recombinant His10-YhdA protein displays a strong NADPH-dependent chromate reductase activity. In bacterial cells, YhdA counteracts the cytotoxic and genotoxic effects of intracellular and extracellular inducers of oxygen radicals, including those caused by hexavalent chromium. The enzyme upon overexpression confers protection on Bacillus subtilis from the cytotoxic effects promoted by Cr(VI) and counteracts the mutagenic effects of the reactive oxygen species (ROS)-promoted lesion 8-oxoguanine (8-OxoG). YhdA prevents the formation of mutations in Bacillus subtilis, mainly those that are increased in the absence of systems that repair 8-OxoG lesions
physiological function
-
Pseudomonas putida MET94 is a bacteria that degrades a wide range of structurally distinct azo dyes with high efficiency and the azoreductase PpAzoR plays a key role in this process
-
physiological function
-
the enzyme catalyzes extracellular bioreduction of methyl orange. Geobacter sulfurreducens strain PCA has a very high decolorization efficiency among the methyl orange reducing bacteria
-
physiological function
-
the rate limiting first step of the biodegradation pathway of recalcitrant azo dyes is their decolorization, which involves the reductive cleavage of the azo bond catalysed by the enzyme azoreductase. The enzyme from strain L2 decolorizes a wide spectrum of azo dyes
-
additional information
-
active site structure of ecAzoR, overview. The active sites of the enzyme are situated at the dimer interface and are formed by residues from both monomers. One molecule of flavin is bound within each active site and is required for activity
additional information
-
deletion of genes omcB, omcC, and omcE encoding outer membrane proteins of Geobacter sulfurrescens modestly inhibit the decolorization activity by 16%, 42%, and 35%, respectively
additional information
homologous modeling and molecular docking of AzrS for protein-ligand interactions analysis, using the the azoreductase structure from Escherichia coli strain JM109, PDB ID 1v4b. Methyl red and methyl orange formed the hydrogen bonds with His143, Gly140, Gly141 and Asn176
additional information
interaction analysis and molecular docking of substrates and enzyme for analysis of binding mode and binding stability between azoreductase and azo dyes, overview
additional information
-
the azoreductase of the Shewanella sp. strain IFN4 reduces the azo dyes extracellularly while being attached with the plasma membrane. Electrons generated by cellular metabolism must be transported outside the cell in order to reduce substrate. Electrons are transferred from the menaquinone pool in the cytoplasmic membrane to the bacterial cell surface through a series of proteins. Shewanella sp. secretes redox-active flavin compounds able to transfer electrons between the cell surface and substrate in a cyclic fashion, a process termed electron shuttling. In the absence of redox-active flavin compounds transfer of electrons to the substrate is a slow process. Therefore, supplementation of the azoreductase assay with redox active substances (riboflavin, anthraquinone-2,6-disulfonic acid, and anthraquinone-2-sulfonic acid) increases the specific activity of membrane-bound azoreductase as the shuttling of electrons to azo substrate is promoted
additional information
-
deletion of genes omcB, omcC, and omcE encoding outer membrane proteins of Geobacter sulfurrescens modestly inhibit the decolorization activity by 16%, 42%, and 35%, respectively
-
additional information
-
homologous modeling and molecular docking of AzrS for protein-ligand interactions analysis, using the the azoreductase structure from Escherichia coli strain JM109, PDB ID 1v4b. Methyl red and methyl orange formed the hydrogen bonds with His143, Gly140, Gly141 and Asn176
-