HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.7.1.6 - azobenzene reductase
Word Map on EC 1.7.1.6
- 1.7.1.6
-
decolor
-
textile
- nitroreductase
- amaranth
- environmental protection
-
veratryl
- dehydrochlorinase
-
rubine
-
dechlorinase
- industry
-
2,6-dinitrotoluene
- degradation
- analysis
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.7.1.6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
azobenzene reductase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
-
-
-
-
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+
ping-pong mechanism
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
reduction
-
catalyzes the reductive cleavage of azo groups by a ping-pong mechanism
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9029-31-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain KF46, Orange II azoreductase induced by both Orange II and carboxy-Orange II
-
-
-
-
-
strain ATCC 19433, predominant member of the human gastrointestinal microflora
-
-
strain KF46, Orange II azoreductase induced by both Orange II and carboxy-Orange II
-
-
strain KF46F, DSM 13620, formerly Pseudomonas sp. KF46F
SwissProt
strain KF46F, DSM 13620, formerly Pseudomonas sp. KF46F
SwissProt
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
?
1-(2-pyridylazo)-2-naphthol + NADH + H+
? + NAD+
-
-
-
ir
1-(3'-carboxyphenylazo)-2-naphthol + NAD(P)H
3-amino-1-benzoic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
-
-
-
?
1-(3'-phosphophenylazo)-2-naphthol + NAD(P)H
3-amino-1-benzenephosphate + NAD(P)+ + 1-amino-2-hydroxynaphthalene
-
-
-
?
1-(3'-sulfophenylazo)-2-naphthol + NAD(P)H
3-amino-1-benzenesulfonic acid + NAD(P)+ + 1-amino-2-hydroxynaphthalene
-
-
-
?
1-(4'-carboxyphenylazo)-2-hydroxy-6-sulfonaphthalene + NAD(P)H
4-carboxyphenylamine + NAD(P)+ + 1-amino-2-hydroxy-6-sulfonaphthalene
-
-
-
?
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
-
substrate is carboxy-Orange II
-
-
?
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
-
-
-
?
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
-
-
-
?
1-(4'-sulfophenylazo)-2-hydroxy-6-sulfonaphthalene + NAD(P)H
4-sulfophenylamine + NAD(P)+ + 1-amino-2-hydroxy-6-sulfonaphthalene
-
-
-
?
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+
-
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
-
-
?
1-phenylazo-2-hydroxy-6-carboxynaphthalene + NAD(P)H
phenylamine + NAD(P)+ + 1-amino-2-hydroxy-6-carboxynaphthalene
-
-
-
?
1-phenylazo-2-hydroxy-6-sulfonaphthalene + NAD(P)H
phenylamine + NAD(P)+ + 1-amino-2-hydroxy-6-sulfonaphthalene
-
-
-
?
2'-carboxy-4-N,N-dimethylazobenzene + NAD(P)H
2-carboxy-1-phenylamine + N,N-dimethyl-1,4-phenylenediamine + NADP+
-
trivial name methyl red
-
?
2,2'-(1,8-dihydroxy-3,6-disulfonaphthalene-2,7-bis-azo)-bis(benzenearsonic acid) + NAD(P)H
?
-
reduced to an anion free radical by an outer membrane azoreductase
-
-
?
2-hydroxy-1,4-naphthoquinone + NADPH + H+
?
lawsone, quinone reductase activity
-
-
?
2-methyl-1,4-naphthoquinone + NADPH + H+
?
menadione, quinone reductase activity
-
-
?
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+
-
-
-
-
?
3-methyl-4-(2-chlorophenylhydrazone)-isoxazol-5-one + NAD(P)H
o-chloroaniline + ?
-
fungicide, trivial name drazoxolon, 90-80% activity with NADH
-
?
4'-dimethylaminoazobenzene-2-carboxylic acid + NADH + H+
2-aminobenzoic acid + N,N'-dimethyl-p-phenylenediamine + NAD+
-
methyl red
-
-
?
4-(4-aminophenylazo)benzenesulfonic acid + NADPH + H+
?
about 25% specific activity compared to balsalazide
-
-
?
4-(dimethylamino)azobenzene + 2 NADPH
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ + 2 H+
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
?
-
reduces also Acid Orange 6, 8 and 12, Acid Red 88 and 151, NADH is more effective
-
-
?
anthraquinone-2,6-disulfonate + NADPH + H+
?
quinone reductase activity
-
-
?
anthraquinone-2-sulfonate + NADPH + H+
?
quinone reductase activity
-
-
?
direct blue 15 + FAD + NADH + H+
? + NAD+
-
highest activity in presence of both NADH and FAD
-
-
?
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
-
-
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
-
-
-
?
methyl red + NADH + H+
o-aminobenzoic acid + N,N'-dimethyl-p-phenylenediamine + NAD+
-
-
-
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
-
in the presence of menadione as electron carrier
-
?
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+
-
-
-
-
?
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
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)-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-[(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
?
Bacillus sp. SF
-
-
-
-
?
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 + 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
-
-
?
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
?
-
Bacillus sp. SF
-
Basic violet 3, Basic Red 9, Acid Blue 74, Acid blue 225, and Disperse red 86 are not metabolized
-
-
-
additional information
?
-
Bacillus sp. SF
-
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
?
-
-
important for the conversion of azo dyes in the gastrointestinal tract
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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+
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
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
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
NADH
-
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
-
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
-
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
-
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
-
effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
-
additional information
-
effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
-
additional information
-
effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
-
additional information
-
effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
-
additional information
-
effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
-
additional information
-
effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
-
additional information
-
effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
-
additional information
-
effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
-
additional information
-
effect of different cofactors on azoreductase activity of intestinal anaerobic bacteria
-
additional information
-
apparent non-identity of cytochrome c reductase and flavin-dependent azoreductase activity
-
additional information
-
P-450 type cytochromes are responsible for azoreductase activity
-
additional information
AzoB belongs to the flavin-free azoreductase group
-
additional information
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
activation, optimum concentration 25 mM giving 126% of initial activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ferric chloride
-
1 mM leads to 80% inhibition, 2.5 mM leads to 98% inhibition
dicoumarol
-
0.0001 mM, 50% inhibition of methyl red reduction, 0.0004 mM, 90% inhibition, competitive vs. NADPH noncompetitve vs. methyl red
additional information
-
not inhibited by N-ethylmaleimide, p-chloromercuribenzoate and monoiodoacetic acid
-
additional information
-
0.08% SDS together with 0.0022 mM KCN causes 50% inhibition
-
additional information
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-methylhydroquinone
-
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
-
catechol
-
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
-
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
-
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
Direct blue 15
-
pH not specified in the publication, temperature not specified in the publication
0.00018
FAD
-
pH not specified in the publication, temperature not specified in the publication
0.057
2-[4-(dimethylamino)phenylazo]benzoic acid
-
in 25 mM potassium phosphate buffer (pH 7.1), 0.25 mM 2-[4-(dimethylamino)phenylazo]benzoic acid and 0.1 mM NADPH
0.28
2-[4-(dimethylamino)phenylazo]benzoic acid
GST-fusion protein, pH 8.0, 40°C
0.42
2-[4-(dimethylamino)phenylazo]benzoic acid
native protein, pH 8.0, 40°C
0.0986
balsalazide
wild type enzyme, using NADPH as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
0.1029
balsalazide
mutant enzyme Y131F, using NADPH as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
0.055
balsalzide
-
isoform AzoR2, pH 8.0, temperature not specified in the publication
0.34
balsalzide
-
isoform AzoR3, pH 8.0, temperature not specified in the publication
2.447
balsalzide
-
isoform AzoR1, pH 8.0, temperature not specified in the publication
0.0445
Methyl red
mutant enzyme Y131F, using NADPH as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
0.0927
Methyl red
wild type enzyme, using NADPH as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
0.26
Methyl red
-
isoform AzoR1, pH 8.0, temperature not specified in the publication
0.3
Methyl red
-
isoform AzoR2, pH 8.0, temperature not specified in the publication
0.983
Methyl red
-
isoform AzoR3, pH 8.0, temperature not specified in the publication
0.0081
NADH
-
pH not specified in the publication, temperature not specified in the publication
0.298
NADH
-
isoform AzoR1, pH 8.0, temperature not specified in the publication
0.525
NADH
-
isoform AzoR1, pH 8.0, temperature not specified in the publication
0.538
NADH
wild type enzyme, using methyl red as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
0.965
NADH
mutant enzyme Y131F, using methyl red as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
0.074
NADPH
-
in 25 mM potassium phosphate buffer (pH 7.1), 0.25 mM azo dye and 0.1 mM NADPH
0.535
NADPH
mutant enzyme Y131F, using methyl red as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
1.197
NADPH
wild type enzyme, using methyl red as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
10.26
NADPH
-
isoform AzoR1, pH 8.0, temperature not specified in the publication
0.22
sulfasalazine
-
isoform AzoR3, pH 8.0, temperature not specified in the publication
0.38
sulfasalazine
-
isoform AzoR2, pH 8.0, temperature not specified in the publication
1.118
sulfasalazine
-
isoform AzoR1, pH 8.0, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24.1
balsalazide
Pseudomonas aeruginosa
Q9I5F3
mutant enzyme Y131F, using NADPH as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
36.8
balsalazide
Pseudomonas aeruginosa
Q9I5F3
wild type enzyme, using NADPH as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
0.2
balsalzide
Pseudomonas aeruginosa
-
isoform AzoR3, pH 8.0, temperature not specified in the publication
0.7
balsalzide
Pseudomonas aeruginosa
-
isoform AzoR2, pH 8.0, temperature not specified in the publication
20
balsalzide
Pseudomonas aeruginosa
-
isoform AzoR1, pH 8.0, temperature not specified in the publication
1
Methyl red
Pseudomonas aeruginosa
-
isoform AzoR2, pH 8.0, temperature not specified in the publication
4.8
Methyl red
Pseudomonas aeruginosa
-
isoform AzoR1, pH 8.0, temperature not specified in the publication
11.6
Methyl red
Pseudomonas aeruginosa
-
isoform AzoR3, pH 8.0, temperature not specified in the publication
12.7
Methyl red
Pseudomonas aeruginosa
Q9I5F3
wild type enzyme, using NADPH as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
19.1
Methyl red
Pseudomonas aeruginosa
Q9I5F3
mutant enzyme Y131F, using NADPH as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
10
NADH
Pseudomonas aeruginosa
Q9I5F3
wild type enzyme, using methyl red as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
25.2
NADH
Pseudomonas aeruginosa
Q9I5F3
mutant enzyme Y131F, using methyl red as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
33.6
NADPH
Pseudomonas aeruginosa
Q9I5F3
wild type enzyme, using methyl red as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
35.5
NADPH
Pseudomonas aeruginosa
Q9I5F3
mutant enzyme Y131F, using methyl red as cosubstrate, in 20 mM Tris–HCl pH 8.0, temperature not specified in the publication
0.5
sulfasalazine
Pseudomonas aeruginosa
-
isoform AzoR3, pH 8.0, temperature not specified in the publication
0.8
sulfasalazine
Pseudomonas aeruginosa
-
isoform AzoR2, pH 8.0, temperature not specified in the publication
2.6
sulfasalazine
Pseudomonas aeruginosa
-
isoform AzoR1, pH 8.0, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0019
Methyl red
Enterococcus faecalis
-
in 50 mM potassium phosphate buffer pH 7.0 at 25°C
989
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.003
0.0035
-
activity in caecal suspension with amaranth; activity in liver microsomes with amaranth
0.004
-
activity in liver microsomes with carmoisine; activity in liver microsomes with Fast Red E
0.65
extract from host strain with Methyl red and NADH as substrates, pH 8.0, 40°C
1.1
purified recombinant enzyme with Red dye III and NADH as substrates, pH 8.0, 40°C
2.8
purified enzyme, pH 7.1 with 1-(4'-carboxyphenylazo)-4-naphthol and NADH as substrates
2.9
crude extract, using Orange I as the substrate with NADH as proton donor, pH 6.8, 45°C
8.5
extract from Escherichia coli containing recombinant enzyme with Methyl red and NADH as substrates, pH 8.0, 40°C
10.1
purified enzyme, using Orange I as the substrate with NADH as proton donor, pH 6.8, 45°C
10.8
purified enzyme, pH 7.1 with 1-(4'-carboxyphenylazo)-2-naphthol and NADH as substrates
12.6
purified recombinant enzyme with Red dye II and NADH as substrates, pH 8.0, 40°C
15.4
-
cofactor FAD, pH not specified in the publication, temperature not specified in the publication
20.3
purified recombinant enzyme with Red dye I and NADH as substrates, pH 8.0, 40°C
20.7
substrate Ponceau BS, cofactor NADH; substrate ponceau BS, cosubstrate NADH, pH 7.0, 25°C
26
-
pH not specified in the publication, temperature not specified in the publication
26.9
-
cofactor FMN, pH not specified in the publication, temperature not specified in the publication
63.9
-
purified enzyme, pH 7.1, 23°C, with Methyl red and NADH as substrates
78.9
purified recombinant enzyme with Methyl red and NADH as substrates, pH 8.0, 40°C
626
-
after 209fold purification, using methyl red and NADPH as substrates, in 50 mM potassium phosphate buffer pH 7.0 at 25°C
2868
5095
substrate methyl red, cofactor NADH; substrate methyl red, cosubstrate NADH, pH 7.0, 25°C
additional information
0.003
-
crude extract, using methyl red and NADPH as substrates, in 50 mM potassium phosphate buffer pH 7.0 at 25°C
additional information
substrate 1-(2-pyridylazo)-2-naphthol, relative activity 0.64%, methyl red 100%; substrate 1-(2-pyridylazo)-2-naphthol, relative activity 23.2%, methyl red 100%; substrate acid red 88, relative activity 0.12%, methyl red 100%; substrate acid red 88, relative activity 12.2%, methyl red 100%; substrate ethyl red, relative activity 113%, methyl red 100%; substrate ethyl red, relative activity 146%, methyl red 100%; substrate methyl orange, relative activity 0.21%, methyl red 100%; substrate methyl orange, relative activity 0.93%, methyl red 100%; substrate methyl red, relative activity 100%; substrate methyl red, relative activity 100%; substrate new cossin, relative activity 0.1%, methyl red 100%; substrate orange II, relative activity 0.01%, methyl red 100%; substrate orange II, relative activity 0.29%, methyl red 100%; substrate orange I, relative activity 0.03%, methyl red 100%; substrate orange I, relative activity 1.26%, methyl red 100%; substrate sunset yellow FCF, relative activity 0.16%, methyl red 100%
additional information
substrate 1-(2-pyridylazo)-2-naphthol, relative activity 0.64%, methyl red 100%; substrate 1-(2-pyridylazo)-2-naphthol, relative activity 23.2%, methyl red 100%; substrate acid red 88, relative activity 0.12%, methyl red 100%; substrate acid red 88, relative activity 12.2%, methyl red 100%; substrate ethyl red, relative activity 113%, methyl red 100%; substrate ethyl red, relative activity 146%, methyl red 100%; substrate methyl orange, relative activity 0.21%, methyl red 100%; substrate methyl orange, relative activity 0.93%, methyl red 100%; substrate methyl red, relative activity 100%; substrate methyl red, relative activity 100%; substrate new cossin, relative activity 0.1%, methyl red 100%; substrate orange II, relative activity 0.01%, methyl red 100%; substrate orange II, relative activity 0.29%, methyl red 100%; substrate orange I, relative activity 0.03%, methyl red 100%; substrate orange I, relative activity 1.26%, methyl red 100%; substrate sunset yellow FCF, relative activity 0.16%, methyl red 100%
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6
6.2
6.5
8.5
-
substrate 2-methyl-1,4-naphthoquinone, quinone reductase activity
additional information
-
the reduction rate is both dye and pH specific
6
for activity of the enzyme with Orange I, in 50 mM Sorensen's phosphate buffer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
35
35 - 40
40
41
45
50
70
50
-
substrate 2-methyl-1,4-naphthoquinone, quinone reductase activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
20 - 50
-
20 C: about 25% activity with carboxy-Orange II, about 30% activity with Orange II, 50 C: about 95% activity with carboxy-Orange II, about 80% activity with Orange II
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
activity higher in crude outer mitochondrial membrane fraction than in mitoplast and intact mitochondria
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
14000
19000
20000
23000
27000
28000
29000
30000
46000
85000
20000
gel filtration, differences in molecular weights are supposed to be due to an extraordinary behavior of the enzyme in gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
tetramer
homodimer
2 * 22900, determined by gel filtration; 2 * 23000, determined by gel filtration
monomer
-
1 * 29000, subunit mass by SDS-PAGE, native mass by gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
modeling of structure. Binding mode shows that the benzoic acid moiety of substrate methyl red and the nicotinamide ring of NADH are not parallel to the flavin isoalloxazine ring, but lay against it at angles of about 45 and 35 degrees, respectively. The adenine ribose moiety of NADH is surrounded by loop l2 on chain B and alpha3 on chain A in a typical Rossmann fold
-
hanging drop vapour diffusion method using 10 mM Tris-HCl (pH 8.0), 1 mM FMN, and an equal volume of reservoir solution containing 200 mM NaCl, 100 mM CAPS2 (pH 10.5), 20% (w/v) polyethylene glycol 8000, 20% (v/v) 1,4-dioxane, and 4 mM menadione
-
the structures of oxidized and reduced AzoR, and in complex with the inhibitor 3,3'-methylene-bis(4-hydroxycoumarin) are determined at resolutions from 1.4 to 2.3 A
-
homology modeling and multiple sequence alignment shows conserved regions at different stretches from amino acid residues 1-11, 40-57, 82-120 and 161-177
mutant enzyme Y131F in the presence of methyl red, sitting drop vapor diffusion method, using 0.1 M sodium acetate pH 4.5, 1.0 M diammonium hydrogen phosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
42 - 55
whilst wild type AzoR1 loses 50% of its activity after incubation for 10 min at 55°C, mutant enzyme Y131F loses 50% of its activity after exposure to 42°C for 10 min, both enzymes are inactive after 10 min at 80°C
60
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation by oxygen
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cell extracts of Enterococcus faecalis are prepared, AzoA is purified by hydrophobic, anion exchange and affinity chromatography
-
crude cell extracts are applied on a DEAE cellulose column, subsequently to an ammonium sulfate precipitation the enzyme solution is applied on a Butyl Toyopearl 650M column, finally a Sephacryl S200 column is used; crude cell extracts are applied on a DEAE cellulose column, subsequently to an ammonium sulfate precipitation the enzyme solution is applied on a Phenyl Toyopearl 650M column, finally a Sephacryl S200 column is used
crude protein extracts from Bacillus velezensis are prepared
HiPrep 16/10 Q XL anion-exchange column chromatography and HiLoad 26/60 Superdex 200 gel fltration
-
His-tagged proteins are purified by gravity-flow chromatography using nickel-nitrilotriacetic acid-agarose
-
octyl Sepharose column chromatography, DEAE Bio-gel agarose column chromatography, and Affi-gel Blue gel filtration
-
phenyl Sepharose column chromatography and HiPrep SP XL column chromatography
recombinant enzyme
the GST-AzoR protein is purified by glutathione Sepharose 4B, the GST tag is removed by digestion with thrombin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS using a phage T7-promotor system
expressed in Escherichia coli BL21(DE3)pLysS using a phage T7-promotor system, no in vivo activity in recombinant strains due to missing azo dye uptake system
expression in Escherichia coli
expression in Escherichia coli; into the pCR2.1-TOPO vector and subsequently into pET15b for expression in Escherichia coli NovaBlue DE3 cells
into the vector pET-11a for expression in Escherichia coli BL21-Gold DE3 pLysS cells
-
into the vector pET32a for recombinant expression in Escherichia coli DH5alpha cells
-
into the vector pGEM-T and subsequently into pET3a for expression in Escherichia coli BL21DE3 cells; into the vector pGEM-T and subsequently into pET3a for expression in Escherichia coli BL21DE3 cells
into the vector pGEX 4T-1 for transformation into Escherichia coli JM109 cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in presence of balsalazide, expression of isoform AzoR1 increases by about 50%; in presence of methyl red or balsalzide, expression of isoform AzoR2 increases 3.5- and 2.5fold, respectively
-
in presence of methyl red, expression of isoform AzoR1 increases more than 50%
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W105A
-
mutant, complete loss of both affinity for FMN and enzyme activity
W105G
-
mutant, complete loss of both affinity for FMN and enzyme activity
W105Y
-
mutant, substitution does not significantly decrease the Vmax of the enzyme, 22% reduction
F162A
-
Phe-162 is chosen because it is predicted to participate in the substrate binding on top of the isoalloxazine ring, as observed in the AzoR-inhibitor structure
R59A
-
the results indicate that Arg-59 decides the substrate specificity of AzoR
Y120A
-
Tyr-120 is chosen because it is predicted to participate in the substrate binding on top of the isoalloxazine ring, as observed in the AzoR-inhibitor structure
Y131F
the mutant shows increased specific activity with methyl red and reduced specific activity with balsalazide compared to the wild type enzyme
H75N
-
mutation decreases the binding of methyl red and nitrofurazone and has no effect on the bining of NADPH
K109A
-
K109 might only be involved in the binding of the 2'-phosphate group of NADPH and have no effect on the binding of NADH
K109H
-
K109 might only be involved in the binding of the 2'-phosphate group of NADPH and have no effect on the binding of NADH
Y74W
-
mutation decreases the binding of methyl red and nitrofurazone and has no effect on the bining of NADPH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
pro-fluorophore 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 shows a green fluorescence upon reduction of the two diazo bonds suitable for the detection of azoreductases
degradation
environmental protection
industry
degradation
-
the optimum medium contains dye at 200 mg per l, 1.14 mM NADH, glucose at 2.07 g per l, and peptone at 6.44 g per l for the decolorization of Orange II up to 87% in 48 hr
degradation
F0PC48
expression of enzyme gene AzoA in Escherichia coli induces a higher rate of dye reduction with increases of 2fold for methyl red, 4fold for ponceau BS and 2.6fold for orange II compared to noninduced cells, respectively
environmental protection
potential for the treatment of azo dye contaminated wastewater
environmental protection
potential for the treatment of azo dye contaminated wastewater
environmental protection
-
potential for the treatment of azo dye contaminated wastewater
environmental protection
-
potential for the treatment of azo dye contaminated wastewater
environmental protection
potential for the treatment of azo dye contaminated wastewater
environmental protection
-
potential for the treatment of azo dye contaminated wastewater
-
environmental protection
-
potential for the treatment of azo dye contaminated wastewater
-
environmental protection
-
potential for the treatment of azo dye contaminated wastewater
-
industry
culture of Bacillus velezensis seems to be a suitable candidate for further study for both decolourization and detoxification of azo dyes, resulting in their safe disposal
industry
azoreductases are favorable for the development of biodegradation process for azo dyes; azoreductases are favorable for the development of biodegradation process for azo dyes
industry
-
industrial use of the enzyme in the biodegradation process of azo compounds
industry
-
culture of Bacillus velezensis seems to be a suitable candidate for further study for both decolourization and detoxification of azo dyes, resulting in their safe disposal
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.7.1.6)
html completed
Information
