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Enzyme Nomenclature
Information on EC 1.7.1.6 - azobenzene reductase
for references in articles please use BRENDA:EC1.7.1.6
Word Map on EC 1.7.1.6
- 1.7.1.6
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decolor
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textile
- environmental protection
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veratryl
- drug development
- amaranth
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voltammograms
- 2,6-dinitrotoluene
- dcip
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dechlorinase
- industry
- dehydrochlorinase
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ponceau
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rubine
- degradation
- analysis
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.7.1.6
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RECOMMENDED NAME
GeneOntology No.
azobenzene reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
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N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
ping-pong mechanism
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N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases
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N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases
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N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases
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N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases, mechanism for azoreduction by FMN-dependent azoreductases, overview. N5 of FMN accepts a hydride during oxidation of NAD(P)H and donates it upon reduction of the substrate
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N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases
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N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases
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N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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reduction
oxidation
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reduction
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reduction
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catalyzes the reductive cleavage of azo groups by a ping-pong mechanism
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SYSTEMATIC NAME
IUBMB Comments
N,N-dimethyl-1,4-phenylenediamine, aniline:NADP+ oxidoreductase
The reaction occurs in the reverse direction to that shown above. Other azo dyes, such as Methyl Red, Rocceline, Solar Orange and Sumifix Black B can also be reduced [2].
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CAS REGISTRY NUMBER
COMMENTARY
9029-31-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bacterium enrichment culture clone V9DM; from soil collected from banks of the Khari-cut canal (Vatva, Ahmedabad, Gujarat, India), contaminated by industrial wastes, V9 consortium
UniProt
Orange II azoreductase induced by both Orange II and carboxy-Orange II
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Shewanella oneidensis MR-1 / ATCC 700550
Xenophilus azovorans KF46F / DSM 13620
strain ATCC 19433, predominant member of the human gastrointestinal microflora
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
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
metabolism
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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
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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
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physiological function
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the enzyme degrades the azo dye naphthol blue black, the reaction product is less toxic than the substrate
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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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physiological function
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the enzyme catalyzes extracellular bioreduction of methyl orange. Geobacter sulfurreducens strain PCA has a very high decolorization efficiency among the methyl orange reducing bacteria
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physiological function
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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
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additional information
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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
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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
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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
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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
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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
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additional information
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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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dimethyl-4(p-carboxyphenylazo)-5-hydroxybenzene + NADPH
1,2-dimethyl-4-amino-5-hydroxybenzene + p-carboxyphenylamine + NADP+
1-(2'-methyl-4'-sulfophenylazo)2-naphthol + NAD(P)H
4-amino-2-methyl-1-benzenesulfonic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
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-
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?
1-(2-pyridylazo)-2-naphthol + NADH + H+
? + NAD+
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-
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ir
1-(3'-carboxyphenylazo)-2-naphthol + NAD(P)H
3-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
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?
1-(3'-phosphophenylazo)-2-naphthol + NAD(P)H
3-amino-1-benzenephosphate + NAD(P)+ + 1-amino-2-hydroxynaphthalene
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?
1-(3'-sulfophenylazo)-2-naphthol + NAD(P)H
3-amino-1-benzenesulfonic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
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?
1-(4'-carboxyphenylazo)-2-hydroxy-6-sulfonaphthalene + NAD(P)H
4-carboxyphenylamine + NAD(P)+ + 1-amino-2-hydroxy-6-sulfonaphthalene
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?
1-(4'-carboxyphenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
1-(4'-carboxyphenylazo)-2-naphthol + NADH
4-amino-1-benzoic acid + NAD+ + 1-amino-2-hydroxynaphthalene
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substrate is carboxy-Orange II
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?
1-(4'-carboxyphenylazo)-4-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-4-hydroxynaphthalene
1-(4'-nitrophenylazo)-2-hydroxy-6-sulfonaphthalene + NAD(P)H
4-nitrophenylamine + NAD(P)+ + 1-amino-2-hydroxy-6-sulfonaphthalene
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?
1-(4'-phosphophenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzenephosphate + NAD(P)+ + 1-amino-2-hydroxynaphthalene
1-(4'-sulfonaminophenylazo-)2-naphthol + NAD(P)H
4-amino-1-benzenesulfonamine + NAD(P)+ + 1-amino-2-hydroxynaphthalene
1-(4'-sulfophenylazo)-2-hydroxy-6-carboxynaphthalene + NAD(P)H
4-sulfophenylamine + NAD(P)+ + 1-amino-2-hydroxy-6-carboxynaphthalene
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?
1-(4'-sulfophenylazo)-2-hydroxy-6-sulfonaphthalene + NAD(P)H
4-sulfophenylamine + NAD(P)+ + 1-amino-2-hydroxy-6-sulfonaphthalene
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?
1-(4-sulfo-1-naphthylazo)-2-naphthol-3,6-disulfonic acid + NADPH
alpha-naphthylamine-4-sulfonic acid + beta-naphthol-3,6-disulfonic acid + NADP+
1-methyl-1-([1-[(Z)-(methyl[4-[(E)-2-[6'-[(E)-[4-[methyl([4-[(1-methylpyrrolidinium-1-yl)methyl]-1H-1,2,3-triazol-1-yl]methyl)amino]phenyl]diazenyl]-3-oxo-3H-spiro[2-benzofuran-1,9'-xanthen]-3'-yl]ethenyl]phenyl]iminio)methyl]-1H-1,2,3-triazol-4-yl]methyl)pyrrolidinium + FMN + NADH + H+
? + NAD+
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pro-fluorophore, based on fluorescent rhodamine 110. Upon reduction of the two diazo bonds, substrate shows a green fluorescence suitable for the detection of azoreductases
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?
1-phenylazo-2-hydroxy-6-carboxynaphthalene + NAD(P)H
phenylamine + NAD(P)+ + 1-amino-2-hydroxy-6-carboxynaphthalene
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?
1-phenylazo-2-hydroxy-6-sulfonaphthalene + NAD(P)H
phenylamine + NAD(P)+ + 1-amino-2-hydroxy-6-sulfonaphthalene
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?
2'-carboxy-4-N,N-dimethylazobenzene + NAD(P)H
2-carboxy-1-phenylamine + N,N-dimethyl-1,4-phenylenediamine + NADP+
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trivial name methyl red
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?
2,2'-(1,8-dihydroxy-3,6-disulfonaphthalene-2,7-bis-azo)-bis(benzenearsonic acid) + NAD(P)H
?
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reduced to an anion free radical by an outer membrane azoreductase
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?
2-hydroxy-1,4-naphthoquinone + NADPH + H+
?
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lawsone, quinone reductase activity
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?
2-methyl-1,4-naphthoquinone + NADPH + H+
?
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menadione, quinone reductase activity
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?
2-[4-(dimethylamino)phenylazo]benzoic acid + NADH
2-aminobenzoic acid + N,N-dimethyl-1,4-phenylenediamine + NAD+
2-[4-(dimethylamino)phenylazo]benzoic acid + NADPH
N,N-dimethyl-p-phenylenediamine + 2-aminobenzoic acid + NADP+
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?
3-methyl-4-(2-chlorophenylhydrazone)-isoxazol-5-one + NAD(P)H
o-chloroaniline + ?
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fungicide, trivial name drazoxolon, 90-80% activity with NADH
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?
4'-dimethylaminoazobenzene-2-carboxylic acid + NADH + H+
2-aminobenzoic acid + N,N'-dimethyl-p-phenylenediamine + NAD+
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methyl red
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?
4-(4-aminophenylazo)benzenesulfonic acid + NADPH + H+
?
about 25% specific activity compared to balsalazide
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?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
4-(dimethylamino)azobenzene + NADPH + H+
N,N-dimethyl-1,4-phenylenediamine + aniline + NADP+
4-dimethylaminoazobenzene-2'-carboxylic acid + NADH + H+
anthranilate + N,N'-dimethylaminoaniline + NAD+
4-dimethylaminoazobenzene-2'-carboxylic acid + NADPH + H+
anthranilate + N,N'-dimethylamino-aniline + NAD+
i.e. methyl red
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?
4-[(2-hydroxy-1-naphthalenyl)azo]benzene sulfonic acid + NAD(P)H
4-amino-1-benzenesulfonic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
4-[(4-hydroxy-1-naphthalenyl)azo]benzene sulfonic acid + NAD(P)H
4-amino-benzenesulfonic acid + 1-amino-4-hydroxynaphthalene + NADP+
acid Orange 7 + NAD(P)H
?
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reduces also Acid Orange 6, 8 and 12, Acid Red 88 and 151, NADH is more effective
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?
anthraquinone-2,6-disulfonate + NADPH + H+
?
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quinone reductase activity
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?
anthraquinone-2-sulfonate + NADPH + H+
?
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quinone reductase activity
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?
balsalazide + NADPH + H+
? + NADP+
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tautomeric forms of balsalazide occur in solution, reaction mechanism, overview
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?
direct blue 15 + FAD + NADH + H+
? + NAD+
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highest activity in presence of both NADH and FAD
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?
direct blue 15 + NAD(P)H
3,3'-dimethoxybenzidine + 1-hydroxy-2,8-diamino-3,6-naphthalenedisulfonic acid + NAD(P)+
ethyl red + NADH + H+
? + NAD+
best substrate, 182% of the activity with methyl red at 30°C
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-
ir
methyl red + NADH
2-aminobenzoic acid + N,N-dimethyl-1,4-phenylenediamine + NAD+
-
-
-
-
?
methyl red + NADH + H+
N,N-dimethyl-p-phenylenediamine and 2-aminobenzoic acid + NAD+
F0PC48;
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-
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?
methyl red + NADH + H+
o-aminobenzoic acid + N,N'-dimethyl-p-phenylenediamine + NAD+
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ir
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+
4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
NADPH + 9,10-phenanthrenequinone
NADP+ + 9,10-phenanthrenequinol
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NADPH + oxidized cytochrome c
NADP+ + reduced cytochrome c
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in the presence of menadione as electron carrier
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?
naphthol blue black + NADH + H+
? + NAD+
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78% conversion, analysis by UV-visible and FITR spectroscopy, HPLC, and GC-MS
-
-
?
Navitan fast blue S5R + NADH
metanilic acid + 1,4-diamino naphtalene + peri acid + NAD+
-
-
-
-
?
olsalazine + NADPH + H+
?
less than 10% specific activity compared to balsalazide
-
-
?
orange II + NADH + H+
sulfanilic acid + 1-amino-2-naphthol + NAD+
-
-
-
-
?
reactive violet 5 + NADH + H+
? + NAD+
-
-
-
?
reactive violet 5 + NADPH + H+
? + NADP+
-
-
-
?
sulfasalazine + NADPH + H+
?
about 20% specific activity compared to balsalazide
-
-
?
1,2-dimethyl-4(p-carboxyphenylazo)-5-hydroxybenzene + NADPH
1,2-dimethyl-4-amino-5-hydroxybenzene + p-carboxyphenylamine + NADP+
-
-
-
?
1,2-dimethyl-4(p-carboxyphenylazo)-5-hydroxybenzene + NADPH
1,2-dimethyl-4-amino-5-hydroxybenzene + p-carboxyphenylamine + NADP+
-
-
-
?
1,2-dimethyl-4(p-carboxyphenylazo)-5-hydroxybenzene + NADPH
1,2-dimethyl-4-amino-5-hydroxybenzene + p-carboxyphenylamine + NADP+
-
-
-
?
1,2-dimethyl-4(p-carboxyphenylazo)-5-hydroxybenzene + NADPH
1,2-dimethyl-4-amino-5-hydroxybenzene + p-carboxyphenylamine + NADP+
-
-
-
?
1,2-dimethyl-4(p-carboxyphenylazo)-5-hydroxybenzene + NADPH
1,2-dimethyl-4-amino-5-hydroxybenzene + p-carboxyphenylamine + NADP+
-
-
-
?
1-(4'-carboxyphenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
-
-
-
?
1-(4'-carboxyphenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
-
-
-
?
1-(4'-carboxyphenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
substrate is carboxy-Orange II
-
-
?
1-(4'-carboxyphenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
substrate is carboxy-Orange II
-
-
?
1-(4'-carboxyphenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
substrate can be utilized as sole carbon and energy source
-
-
?
1-(4'-carboxyphenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
substrate is carboxy-Orange II
-
-
?
1-(4'-carboxyphenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
Xenophilus azovorans KF46F / DSM 13620
substrate can be utilized as sole carbon and energy source
-
-
?
1-(4'-carboxyphenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
Xenophilus azovorans KF46F / DSM 13620
substrate is carboxy-Orange II
-
-
?
1-(4'-carboxyphenylazo)-4-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-4-hydroxynaphthalene
substrate can be utilized as sole carbon and energy source
-
-
?
1-(4'-carboxyphenylazo)-4-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-4-hydroxynaphthalene
substrate is carboxy-Orange I
-
-
?
1-(4'-carboxyphenylazo)-4-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-4-hydroxynaphthalene
substrate can be utilized as sole carbon and energy source
-
-
?
1-(4'-carboxyphenylazo)-4-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-4-hydroxynaphthalene
substrate is carboxy-Orange I
-
-
?
1-(4'-carboxyphenylazo)-4-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-4-hydroxynaphthalene
-
-
-
-
-
1-(4'-carboxyphenylazo)-4-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-4-hydroxynaphthalene
-
-
-
-
-
1-(4'-phosphophenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzenephosphate + NAD(P)+ + 1-amino-2-hydroxynaphthalene
-
-
-
?
1-(4'-phosphophenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzenephosphate + NAD(P)+ + 1-amino-2-hydroxynaphthalene
-
-
-
?
1-(4'-sulfonaminophenylazo-)2-naphthol + NAD(P)H
4-amino-1-benzenesulfonamine + NAD(P)+ + 1-amino-2-hydroxynaphthalene
-
-
-
?
1-(4'-sulfonaminophenylazo-)2-naphthol + NAD(P)H
4-amino-1-benzenesulfonamine + NAD(P)+ + 1-amino-2-hydroxynaphthalene
-
-
-
?
1-(4-sulfo-1-naphthylazo)-2-naphthol-3,6-disulfonic acid + NADPH
alpha-naphthylamine-4-sulfonic acid + beta-naphthol-3,6-disulfonic acid + NADP+
-
-
-
?
1-(4-sulfo-1-naphthylazo)-2-naphthol-3,6-disulfonic acid + NADPH
alpha-naphthylamine-4-sulfonic acid + beta-naphthol-3,6-disulfonic acid + NADP+
-
-
-
?
1-(4-sulfo-1-naphthylazo)-2-naphthol-3,6-disulfonic acid + NADPH
alpha-naphthylamine-4-sulfonic acid + beta-naphthol-3,6-disulfonic acid + NADP+
-
activity in liver microsomes, reduces also the dyes Red 2G, Red 10B, Carmoisine and Ponceau 4R
-
?
1-(4-sulfo-1-naphthylazo)-2-naphthol-3,6-disulfonic acid + NADPH
alpha-naphthylamine-4-sulfonic acid + beta-naphthol-3,6-disulfonic acid + NADP+
-
trivial name amaranth, activity in liver microsomes
-
?
2-[4-(dimethylamino)phenylazo]benzoic acid + NADH
2-aminobenzoic acid + N,N-dimethyl-1,4-phenylenediamine + NAD+
-
substrate is Methyl red
-
-
?
2-[4-(dimethylamino)phenylazo]benzoic acid + NADH
2-aminobenzoic acid + N,N-dimethyl-1,4-phenylenediamine + NAD+
-
substrate is Methyl red
-
-
?
2-[4-(dimethylamino)phenylazo]benzoic acid + NADH
2-aminobenzoic acid + N,N-dimethyl-1,4-phenylenediamine + NAD+
substrate is Methyl red
-
-
?
2-[4-(dimethylamino)phenylazo]benzoic acid + NADH
2-aminobenzoic acid + N,N-dimethyl-1,4-phenylenediamine + NAD+
substrate is Methyl red
-
-
?
4-(4-nitrophenylazo)-1-naphthol + NAD(P)H
?
substrate is Magneson II, 13% of the activity with carboxy-Orange I
-
-
?
4-(4-nitrophenylazo)-1-naphthol + NAD(P)H
?
substrate is Magneson II, 13% of the activity with carboxy-Orange I
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
Orange I azoreductase: absolute requirement for a hydroxyl group in 4'-position of the naphthol ring of the substrate molecule
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
Orange II azoreductase: requirement for substrates with a 2-naphthol moiety
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
Orange II azoreductase: requirement for substrates with a 2-naphthol moiety
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
key enzyme of azo dye degradation, selective agent during experimental evolution in continuous cultures
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
Orange I azoreductase: absolute requirement for a hydroxyl group in 4'-position of the naphthol ring of the substrate molecule
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
Orange II azoreductase: requirement for substrates with a 2-naphthol moiety
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
key enzyme of azo dye degradation, selective agent during experimental evolution in continuous cultures
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
Orange II azoreductase: requirement for substrates with a 2-naphthol moiety
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
specific for reduction of methyl red
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
electron transport protein
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
-
-
?
4-(dimethylamino)azobenzene + NADPH + H+
N,N-dimethyl-1,4-phenylenediamine + aniline + NADP+
-
-
-
-
?
4-(dimethylamino)azobenzene + NADPH + H+
N,N-dimethyl-1,4-phenylenediamine + aniline + NADP+
-
-
-
-
?
4-([4-(dimethylamino)phenyl]diazenyl)benzene-1-sulfonate + NADPH + H+
? + NADP+
-
i.e. methyl orange
-
-
?
4-([4-(dimethylamino)phenyl]diazenyl)benzene-1-sulfonate + NADPH + H+
? + NADP+
-
i.e. methyl orange
-
-
?
4-dimethylaminoazobenzene-2'-carboxylic acid + NADH + H+
anthranilate + N,N'-dimethylaminoaniline + NAD+
-
i.e. methyl red
-
-
?
4-dimethylaminoazobenzene-2'-carboxylic acid + NADH + H+
anthranilate + N,N'-dimethylaminoaniline + NAD+
-
i.e. methyl red
-
-
?
4-dimethylaminoazobenzene-2'-carboxylic acid + NADH + H+
anthranilate + N,N'-dimethylaminoaniline + NAD+
Shewanella oneidensis MR-1 / ATCC 700550
-
i.e. methyl red
-
-
?
4-[(2-hydroxy-1-naphthalenyl)azo]benzene sulfonic acid + NAD(P)H
4-amino-1-benzenesulfonic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
-
NADH is more effective
-
?
4-[(2-hydroxy-1-naphthalenyl)azo]benzene sulfonic acid + NAD(P)H
4-amino-1-benzenesulfonic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
-
trivial name Orange II
-
?
4-[(2-hydroxy-1-naphthalenyl)azo]benzene sulfonic acid + NAD(P)H
4-amino-1-benzenesulfonic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
-
trivial name Orange II
-
?
4-[(4-hydroxy-1-naphthalenyl)azo]benzene sulfonic acid + NAD(P)H
4-amino-benzenesulfonic acid + 1-amino-4-hydroxynaphthalene + NADP+
-
trivial name Orange I
-
?
4-[(4-hydroxy-1-naphthalenyl)azo]benzene sulfonic acid + NAD(P)H
4-amino-benzenesulfonic acid + 1-amino-4-hydroxynaphthalene + NADP+
-
trivial name Orange I
-
?
acid red 88 + NADH + H+
? + NAD+
10% of hte activity with methyl red at 30°C
-
-
ir
di-sodium-(R)-benzyl-azo-2,7-dihydroxy-3,6-disulfonyl-naphthaline + NADH
?
-
-
-
-
?
di-sodium-(R)-benzyl-azo-2,7-dihydroxy-3,6-disulfonyl-naphthaline + NADH
?
-
-
-
-
?
direct blue 15 + NAD(P)H
3,3'-dimethoxybenzidine + 1-hydroxy-2,8-diamino-3,6-naphthalenedisulfonic acid + NAD(P)+
-
-
-
?
direct blue 15 + NAD(P)H
3,3'-dimethoxybenzidine + 1-hydroxy-2,8-diamino-3,6-naphthalenedisulfonic acid + NAD(P)+
-
-
-
?
direct blue 15 + NAD(P)H
3,3'-dimethoxybenzidine + 1-hydroxy-2,8-diamino-3,6-naphthalenedisulfonic acid + NAD(P)+
-
-
-
?
direct blue 15 + NAD(P)H
3,3'-dimethoxybenzidine + 1-hydroxy-2,8-diamino-3,6-naphthalenedisulfonic acid + NAD(P)+
-
-
-
?
direct blue 15 + NAD(P)H
3,3'-dimethoxybenzidine + 1-hydroxy-2,8-diamino-3,6-naphthalenedisulfonic acid + NAD(P)+
-
-
-
?
direct blue 15 + NAD(P)H
3,3'-dimethoxybenzidine + 1-hydroxy-2,8-diamino-3,6-naphthalenedisulfonic acid + NAD(P)+
-
-
-
?
direct blue 15 + NAD(P)H
3,3'-dimethoxybenzidine + 1-hydroxy-2,8-diamino-3,6-naphthalenedisulfonic acid + NAD(P)+
-
-
-
?
direct blue 15 + NAD(P)H
3,3'-dimethoxybenzidine + 1-hydroxy-2,8-diamino-3,6-naphthalenedisulfonic acid + NAD(P)+
-
-
-
?
direct red 28 + NADH + H+
benzidine + 4-aminobiphenyl + NAD+
-
-
-
?
direct red 28 + NADH + H+
benzidine + 4-aminobiphenyl + NAD+
-
-
-
?
methyl red + NADH + H+
?
the enzyme exhibits lower activity with NADH compared to NADPH
-
-
?
methyl red + NADH + H+
anthranilate + N,N'-dimethylaminoaniline + NAD+
i.e. 4-dimethylaminoazobenzene-2'-carboxylic acid
-
-
?
methyl red + NADH + H+
anthranilate + N,N'-dimethylaminoaniline + NAD+
Shewanella oneidensis MR-1 / ATCC 700550
i.e. 4-dimethylaminoazobenzene-2'-carboxylic acid
-
-
?
methyl red + NADH + H+
anthranilate + N,N'-dimethylaminoaniline + NAD+
i.e. 4-dimethylaminoazobenzene-2'-carboxylic acid
-
-
?
methyl red + NADH + H+
anthranilate + N,N'-dimethylaminoaniline + NAD+
i.e. 4-dimethylaminoazobenzene-2'-carboxylic acid
-
-
?
methyl red + NADPH + H+
?
about 50% specific activity compared to balsalazide
-
-
?
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+
4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+
4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
-
-
-
?
Orange I + NADH
?
both NADH and NADPH can be used as an electron donor for its activity with 4-(4-hydroxy-1-naphthylazo)benzenesulfonic acid (Orange I) as substrate
-
-
?
Orange I + NADH
?
both NADH and NADPH can be used as an electron donor for its activity with 4-(4-hydroxy-1-naphthylazo)benzenesulfonic acid (Orange I) as substrate
-
-
?
Orange I + NADPH
?
both NADH and NADPH can be used as an electron donor for its activity with 4-(4-hydroxy-1-naphthylazo)benzenesulfonic acid (Orange I) as substrate
-
-
?
Orange I + NADPH
?
both NADH and NADPH can be used as an electron donor for its activity with 4-(4-hydroxy-1-naphthylazo)benzenesulfonic acid (Orange I) as substrate
-
-
?
oxidized methyl red + NADH + H+
reduced methyl red + NAD+
-
-
-
-
?
oxidized methyl red + NADH + H+
reduced methyl red + NAD+
-
-
-
-
?
additional information
?
-
-
Basic violet 3, Basic Red 9, Acid Blue 74, Acid blue 225, and Disperse red 86 are not metabolized
-
-
-
additional information
?
-
-
several derivatives of di-sodium-(R)-benzyl-azo-2,7-dihydroxy-3,6-disulfonyl-naphthaline tested as substrates are found to be metabolized
-
-
-
additional information
?
-
ammoniumazo-1, citrus yellow, orange G, Ponceau BS, and ruby red are inert to reduction with BTI1
-
-
-
additional information
?
-
-
Basic violet 3, Basic Red 9, Acid Blue 74, Acid blue 225, and Disperse red 86 are not metabolized
-
-
-
additional information
?
-
-
several derivatives of di-sodium-(R)-benzyl-azo-2,7-dihydroxy-3,6-disulfonyl-naphthaline tested as substrates are found to be metabolized
-
-
-
additional information
?
-
-
enzyme AzrC interacts with azo dyes orange G, acid red 88, Sudan I, orange I, and methyl red. The hydrophobic azo dyes like acid red 88 binds more tightly to the AzrC protein
-
-
-
additional information
?
-
-
in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates
-
-
-
additional information
?
-
-
in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates
-
-
-
additional information
?
-
-
important for the conversion of azo dyes in the gastrointestinal tract
-
-
-
additional information
?
-
-
in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates
-
-
-
additional information
?
-
the enzyme can also catalyze the nitroreduction of 7-nitrocoumarin-3-carboxylic acid in a FMN-dependent manner
-
-
-
additional information
?
-
no substrates: ponceau S, tartrazine, amaranth
-
-
-
additional information
?
-
-
no substrates: ponceau S, tartrazine, amaranth
-
-
-
additional information
?
-
-
no substrates: ponceau S, tartrazine, amaranth
-
-
-
additional information
?
-
-
the enzyme from strain L2 decolorizes a wide spectrum of azo dyes with a constantly high activity, overview
-
-
-
additional information
?
-
-
the enzyme from strain L2 decolorizes a wide spectrum of azo dyes with a constantly high activity, overview
-
-
-
additional information
?
-
-
enzyme additionally shows quinone reductase activity. When NAD(P)H is used as an electron donor, the purified enzyme can reduce menadione effectively with a quinone reductase activity of approximately 3.4 U ml-1
-
-
-
additional information
?
-
-
in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates
-
-
-
additional information
?
-
-
enzyme additionally shows quinone reductase activity. When NAD(P)H is used as an electron donor, the purified enzyme can reduce menadione effectively with a quinone reductase activity of approximately 3.4 U ml-1
-
-
-
additional information
?
-
Methyl Red, Amaranth, Ponceau BS, Ponceau S, Orange II, Orange G, Megneson II, 1-(4-nitrophenylazo)-2-naphthol, and 4-(4-nitrophenylazo)-resorcinol are not reduced by AzoB
-
-
-
additional information
?
-
Methyl Red, Amaranth, Ponceau BS, Ponceau S, Orange II, Orange G, Megneson II, 1-(4-nitrophenylazo)-2-naphthol, and 4-(4-nitrophenylazo)-resorcinol are not reduced by AzoB
-
-
-
additional information
?
-
-
no activity with Amaranth, Tropaeolin, Orange II, Ponceau S, Ponceau BS, and Orange G
-
-
-
additional information
?
-
no activity with Amaranth, Tropaeolin, Orange II, Ponceau S, Ponceau BS, and Orange G
-
-
-
additional information
?
-
-
in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates
-
-
-
additional information
?
-
-
in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates
-
-
-
additional information
?
-
-
the bifunctional enzyme shows activity with quinone substrates, anthraquinone-2-sulfonic acid, 1,4-benzoquinone, 1,2-dihydroxybenzene (catechol), 2-hydroxy-1,4-naphthoquinone (Lawsone), and 1,2-naphthoquinone-4-sulfonate, and NADPH as cofactor, cf. EC 1.6.5.10
-
-
-
additional information
?
-
-
in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates
-
-
-
additional information
?
-
-
generation of a coupled enzyme system constructed with azoreductase and glucose 1-dehydrogenase for removal of methyl red, method evaluation, overview. Artificial neural network modelling of the integrated enzyme system
-
-
-
additional information
?
-
Shewanella oneidensis MR-1 / ATCC 700550
-
generation of a coupled enzyme system constructed with azoreductase and glucose 1-dehydrogenase for removal of methyl red, method evaluation, overview. Artificial neural network modelling of the integrated enzyme system
-
-
-
additional information
?
-
-
wide substrate specificity of the enzyme. No activity with reactive blue 4
-
-
-
additional information
?
-
substrate specificity: the catalytic efficiency of AzrS follows the descending order of methyl red, methyl orange, and congo red. The enzyme has a wide substrate range of azo dyes
-
-
-
additional information
?
-
substrate specificity: the catalytic efficiency of AzrS follows the descending order of methyl red, methyl orange, and congo red. The enzyme has a wide substrate range of azo dyes
-
-
-
additional information
?
-
-
does not react with NADH as electron donor
-
-
-
additional information
?
-
-
ammoniumazo-1, citrus yellow, orange G, Ponceau BS, and ruby red are inert to reduction with BTI1
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(4'-carboxyphenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
1-(4'-carboxyphenylazo)-4-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-4-hydroxynaphthalene
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
4-(dimethylamino)azobenzene + NADPH + H+
N,N-dimethyl-1,4-phenylenediamine + aniline + NADP+
additional information
?
-
-
important for the conversion of azo dyes in the gastrointestinal tract
-
-
-
1-(4'-carboxyphenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
Q8KU07
substrate can be utilized as sole carbon and energy source
-
-
?
1-(4'-carboxyphenylazo)-2-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
Xenophilus azovorans KF46F / DSM 13620
Q8KU07
substrate can be utilized as sole carbon and energy source
-
-
?
1-(4'-carboxyphenylazo)-4-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-4-hydroxynaphthalene
Q6YAN1
substrate can be utilized as sole carbon and energy source
-
-
?
1-(4'-carboxyphenylazo)-4-naphthol + NAD(P)H
4-amino-1-benzoic acid + NAD(P)+ + 1-amino-4-hydroxynaphthalene
Q6YAN1
substrate can be utilized as sole carbon and energy source
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
key enzyme of azo dye degradation, selective agent during experimental evolution in continuous cultures
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
-
key enzyme of azo dye degradation, selective agent during experimental evolution in continuous cultures
-
?
4-(dimethylamino)azobenzene + NADPH + H+
N,N-dimethyl-1,4-phenylenediamine + aniline + NADP+
-
-
-
-
?
4-(dimethylamino)azobenzene + NADPH + H+
N,N-dimethyl-1,4-phenylenediamine + aniline + NADP+
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
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about 60% of the activity in presence of FMN. FAD binds to the apo-form and the bound FAD is stably retained in the enzyme molecule without degradation to FMN. The isoalloxazine ring of FAD localizes at the same site and plays the same role as that of FMN in the enzyme
FMN
enzyme sequence consists of different sites such as FMN-dependent NADH-azoreductase site azoR, residues 2-204, flavodoxin-like fold, residues 2-205, NADPH-dependent FMN reductase, residues 2-205, cAMP and cGMP-dependent protein kinase phosphorylation site
FMN
enzyme-bound prosthetic group, FMN-dependence for azoreductase activity
FMN
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a flavin-dependent azoreductase, FMN is anchored by a series of sequence-independent hydrogen bonds to a structural motif referred to as the FMN binding cradle. One molecule of flavin is bound within each active site and is required for activity
NADH
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180fold preference for NADH over NADPH as an electron donor to reduce methyl red
NADH
when NADPH serves as the electron donor, the activity of the enzyme is 63% higher than that when NADH is used
NADH
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AzoA shows more than 180fold preference for NADH over NADPH as an electron donor to reduce methyl red
NADH
enzyme sequence consists of different sites such as FMN-dependent NADH-azoreductase site azoR, residues 2-204, flavodoxin-like fold, residues 2-205, NADPH-dependent FMN reductase, residues 2-205, cAMP and cGMP-dependent protein kinase phosphorylation site
NADPH
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180fold preference for NADH over NADPH as an electron donor to reduce methyl red
NADPH
when NADPH serves as the electron donor, the activity of the enzyme is 63% higher than that when NADH is used
NADPH
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AzoA shows more than 180fold preference for NADH over NADPH as an electron donor to reduce methyl red
NADPH
enzyme sequence consists of different sites such as FMN-dependent NADH-azoreductase site azoR, residues 2-204, flavodoxin-like fold, residues 2-205, NADPH-dependent FMN reductase, residues 2-205, cAMP and cGMP-dependent protein kinase phosphorylation site
additional information
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effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
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additional information
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effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
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additional information
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effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
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additional information
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effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
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additional information
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effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
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additional information
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effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
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additional information
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effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
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additional information
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effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
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additional information
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effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
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additional information
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apparent non-identity of cytochrome c reductase and flavin-dependent azoreductase activity
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additional information
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P-450 type cytochromes are responsible for azoreductase activity
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additional information
AzoB belongs to the flavin-free azoreductase group
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additional information
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the flavin mononucleotide analogue roseoflavin mononucleotide binds to the AzoR apoenzyme with an even higher affinity compared to that of the natural cofactor FMN. Roseoflavin mononucleotide binding does not affect the overall topology of the enzyme and also does not interfere with dimerization of AzoR. The AzoR-roseoflavin mononucleotide holoenzyme complex shows 30% of AzoR-FMN activity in a standard assay
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additional information
the enzyme can use both cofactors, NADH and NADPH, it shows a preference towards NADH for the azoreductase activity, but a preference towards NADPH for the nitroreductase activity
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additional information
AzrS shows activity with both NADH and NADPH. The maximum relative activity of AzrS with 0.875 mM NADPH or NADH is 28.1% and 100%, respectively, indicating that AzrS shows a preference for NADH rather than NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe3+
Mg2+
Zn2+
Mg2+
activation, optimum concentration 25 mM giving 126% of initial activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ferric chloride
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1 mM leads to 80% inhibition, 2.5 mM leads to 98% inhibition
dicoumarol
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0.0001 mM, 50% inhibition of methyl red reduction, 0.0004 mM, 90% inhibition, competitive vs. NADPH noncompetitve vs. methyl red
additional information
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not inhibited by N-ethylmaleimide, p-chloromercuribenzoate and monoiodoacetic acid
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additional information
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0.08% SDS together with 0.0022 mM KCN causes 50% inhibition
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additional information
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changes in salinity from 0 to 2% do not affect the activity of the enzyme very much. After a 1-h incubation, more than 80% relative activity is indicated at 0-5% salt concentrations
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-methylhydroquinone
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0.5 mM, increase in expression of azoR mRNA relative to the expression at zero time before stress is applied, at 10 min 46.0, at 20 min 129.1
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catechol
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6 mM, increase in expression of azoR mRNA relative to the expression at zero time before stress is applied, at 10 min 15.6, at 20 min 31.9
Diamide
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1 mM, increase in expression of azoR mRNA relative to the expression at zero time before stress is applied, at 10 min 11.4, at 20 min 8.1
H2O2
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1 mM, increase in expression of azoR mRNA relative to the expression at zero time before stress is applied, at 10 min 0.9, at 20 min 0.6, 10 mM, 10 min 3.0, 20 min 1.9
menadione
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0.3 mM, increase in expression of azoR mRNA relative to the expression at zero time before stress is applied, at 10 min 25.5, at 20 min 13.3
additional information
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the enzyme is stimulated on the addition of flavin or quinone compounds. 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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
Direct blue 15
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pH not specified in the publication, temperature not specified in the publication
0.00018
FAD
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pH not specified in the publication, temperature not specified in the publication