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Information on EC 1.7.1.6 - azobenzene reductase and Organism(s) Bacillus subtilis and UniProt Accession O07529
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1.7.1.6 azobenzene reductaseIUBMB Comments
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 .
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Word Map
- 1.7.1.6
-
decolor
-
textile
- laccase
-
veratryl
- environmental protection
-
remazol
- drug development
-
dechlorinase
- dcip
-
rubine
- 2,6-dinitrotoluene
-
ponceau
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voltammograms
- industry
- laterosporus
- dehydrochlorinase
- degradation
- analysis
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
azo reductase, azo-reductase, paazor1, orange ii azoreductase, azor1, ef0404, azobenzene reductase, aerobic azoreductase, orange i azoreductase, azo 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
azo dye reductase
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azo reductase
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azo-dye reductase
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azoreductase
dibromopropylaminophenylazobenzoic azoreductase
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dimethylaminobenzene reductase
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methyl red azoreductase
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N,N-dimethyl-4-phenylazoaniline azoreductase
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NAD(P)H:1-(4'-sulfophenylazo)-2-naphthol oxidoreductase
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NADPH2-dependent azoreductase
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NC-reductase
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new Coccine (NC)-reductase
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nicotinamide adenine dinucleotide (phosphate) azoreductase
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Orange II azoreductase
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p-aminoazobenzene reductase
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p-dimethylaminoazobenzene azoreductase
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reductase, azobenzene
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azoreductase
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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+
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
redox reaction
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oxidation
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reduction
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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].
CAS REGISTRY NUMBER
COMMENTARY
9029-31-6
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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
Cibacron Marine dye + NADPH + H+
? + NADP+
reductive degradation
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r
Methyl Red + NADPH + H+
2-aminobenzoic acid + N,N-dimethyl-1,4-phenylenediamine + NADP+
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?
additional information
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YhdA is characterized as an enzyme with azoreductase activity. The pure recombinant His10-YhdA protein efficiently catalyzes the reduction of Cr(VI) employing NADPH as a cofactor. The oxidoreductase possess the ability to reduce Cr(VI) to Cr(III), avoiding the intermediates Cr(V) and Cr(IV). The purified recombinant His10-YhdA protein displays a strong NADP(H)-dependent chromate reductase activity, overview
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additional information
?
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YhdA is characterized as an enzyme with azoreductase activity. The pure recombinant His10-YhdA protein efficiently catalyzes the reduction of Cr(VI) employing NADPH as a cofactor. The oxidoreductase possess the ability to reduce Cr(VI) to Cr(III), avoiding the intermediates Cr(V) and Cr(IV). The purified recombinant His10-YhdA protein displays a strong NADP(H)-dependent chromate reductase activity, overview
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additional information
?
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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
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?
NATURAL SUBSTRATE
NATURAL 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
Cibacron Marine dye + NADPH + H+
? + NADP+
reductive degradation
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
YhdA uses NADPH as the electron donor to reduce the active-site FMN
additional information
YhdA uses NADPH as the electron donor to reduce the active-site FMN. No activity with NADH
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additional information
-
YhdA uses NADPH as the electron donor to reduce the active-site FMN. No activity with NADH
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
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azoreductases are primarily cytosolic enzymes, but have been shown to be secreted during exposure of bacteria to azo dyes
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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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
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
binding site analysis when enzyme is complexed with FMN. Amino acids Thr9, Arg11, Arg15, Thr16, Ser76, Val104, Ala105 and Gly106 are involved in hydrophilic interactions with the ligand, whereas the residues Glu73, Tyr74, His75 andAla105 exhibit hydrophobic interactions, too. Residue Gly110 has no interactiions with the ligand
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene yhdA, recombinant overexpression of His10-tagged enzyme in Escherichia coli strain Rosetta (DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
anthropogenic activity has converted chromium (Cr), an element found in rocks, soils, plants, and animals, into a dangerous environmental pollutant. The activity of the pure oxidoreductase YhdA can be used for efficient bioremediation of Cr(VI)
drug development
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azoreductases from enteric bacteria are targets in the development of drugs for the treatment of colon related disorders
additional information
additional information
health protection, the activity of the pure oxidoreductase YhdA can be used for efficient bioremediation of Cr(VI), it counteracts the cytotoxic and genotoxic effects of oxygen radicals induced by intracellular factors and those generated during reduction of hexavalent chromium. Oxidoreductases that possess the ability to reduce Cr(VI) to Cr(III), avoiding the intermediates Cr(V) and Cr(IV), are of significant biotechnological value
additional information
-
health protection, the activity of the pure oxidoreductase YhdA can be used for efficient bioremediation of Cr(VI), it counteracts the cytotoxic and genotoxic effects of oxygen radicals induced by intracellular factors and those generated during reduction of hexavalent chromium. Oxidoreductases that possess the ability to reduce Cr(VI) to Cr(III), avoiding the intermediates Cr(V) and Cr(IV), are of significant biotechnological value
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, H.
Recent advances in azo dye degrading enzyme research
Curr. Protein Pept. Sci.
7
101-111
2006
Acidaminococcus fermentans, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) OY-2, Bacillus sp. (in: Bacteria) SF, Bacillus subtilis, Bacteroides thetaiotaomicron, Bifidobacterium adolescentis, Blautia obeum, Cereibacter sphaeroides, Citrobacter sp., Clostridium perfringens, Coprococcus catus, Enterocloster clostridioformis, Enterococcus faecalis, Escherichia coli, Fusobacterium sp., Holdemanella biformis, Kocuria rosea, Kocuria varians, Micrococcus luteus, Pantoea agglomerans, Pigmentiphaga kullae, Pigmentiphaga kullae K24, Proteus vulgaris, Shigella dysenteriae, Staphylococcus aureus, Staphylococcus epidermidis, Xenophilus azovorans, Xenophilus azovorans KF46
Bafana, A.; Chakrabarti, T.
Lateral gene transfer in phylogeny of azoreductase enzyme
Comput. Biol. Chem.
32
191-197
2008
Bacillus sp. (in: Bacteria) (Q9FAW5), Bacillus sp. (in: Bacteria) OY1-2 (Q9FAW5), Bacillus subtilis (O07529), Bacillus subtilis 168 (O07529), Cereibacter sphaeroides (Q8GKS3), Cereibacter sphaeroides AS1.1737 (Q8GKS3), Enterococcus faecalis (Q831B2), Escherichia coli (Q8X9S9), Geobacillus stearothermophilus (Q8RR37), Pigmentiphaga kullae (Q6YAN1), Pigmentiphaga kullae K24 (Q6YAN1), Staphylococcus aureus (Q50H63), Xenophilus azovorans (Q8KU07), Xenophilus azovorans KF46F / DSM 13620 (Q8KU07)
Shobana, S.; Berla Thangam, E.; Kasmir Raja, S.
Evolutionary trace analysis of azoreductase at the ligand binding site and enhancing the active site through site directed mutagenesis
J. Proteomics Bioinform.
5
222-225
2012
Bacillus subtilis (O07529)
-
Ryan, A.
Azoreductases in drug metabolism
Br. J. Pharmacol.
174
2161-2173
2017
Bacillus sp. B29 (C0STY1), Bacillus subtilis, Cereibacter sphaeroides, Enterococcus faecalis, Escherichia coli, Pseudomonas aeruginosa (Q9I5F3), Pseudomonas putida
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Valenzuela-Garcia, L.I.; Zapata, B.L.; Ramirez-Ramirez, N.; Huchin-Mian, J.P.; Robleto, E.A.; Ayala-Garcia, V.M.; Pedraza-Reyes, M.
Novel biochemical properties and physiological role of the flavin mononucleotide oxidoreductase YhdA from Bacillus subtilis
Appl. Environ. Microbiol.
86
e1688-20
2020
Bacillus subtilis (O07529), Bacillus subtilis
Suzuki, H.
Remarkable diversification of bacterial azoreductases primary sequences, structures, substrates, physiological roles, and biotechnological applications
Appl. Microbiol. Biotechnol.
103
3965-3978
2019
Bacillus sp. OY1-2, Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis ATCC 6633, Bacillus subtilis ISW1214, Cereibacter sphaeroides, Cereibacter sphaeroides AS1.1737, Geobacillus stearothermophilus, Geobacillus stearothermophilus IFO 13737
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