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1,2-naphthoquinone + 2 NADH + 2 H+
?
1,4-naphthoquinone + 2 NADH + 2 H+
?
1-(2-pyridylazo)-2-naphthol + 2 NADH + 2 H+
pyridin-2-amine + 1-aminonaphthalen-2-ol + 2 NAD+
-
-
-
?
2-(4-dimethylaminophenyl)diazenylbenzoate + 2 NADH + 2 H+
anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD+
2-(4-dimethylaminophenylazo) benzoic acid + NADH + H+
N,N'-dimethyl-p-phenylenediamine + 2-aminobenzoic acid + NAD+
4'-(diethylamino)-azobenzene-2-carboxylic acid + 2 NADH + 2 H+
2-aminobenzoic acid + N,N-diethyl-p-phenylenediamine + 2 NAD+
i.e. ethyl red
-
-
?
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADH + 2 H+
2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NAD+
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADPH + 2 H+
2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NADP+
4-(dimethylamino)azobenzene + NADH + H+
N,N-dimethyl-1,4-phenylenediamine + aniline + NAD+
7-nitrocoumarin-3-carboxylic acid + 2 NADH + 2 H+
7-aminocoumarin-3-carboxylic acid + NAD+ + H2O
via 7-nitrosocoumarin-3-carboxylic acid and 7-hydroxylaminocoumarin-3-carboxylic acid intermediates
-
-
?
7-nitrocoumarin-3-carboxylic acid + NADH + H+
7-aminocoumarin-3-carboxylic acid + NAD+ + H2O
-
-
-
?
acid red 88 + 2 NADH + 2 H+
4-aminobenzene-1-sulfonic acid + 1-aminonaphthalen-2-ol + 2 NAD+
acid red 88 + NADH + H+
? + NAD+
amaranth + 2 NADH + 2 H+
4-aminonaphthalene-1-sulfonic acid + 4-amino-3-hydroxynaphthalene-2,7-disulfonic acid + 2 NAD+
amaranth + 2 NADPH + 2 H+
4-aminonaphthalene-1-sulfonic acid + 4-amino-3-hydroxynaphthalene-2,7-disulfonic acid + 2 NADP+
-
-
-
-
?
anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD+
2-(4-dimethylaminophenyl)diazenylbenzoate + 2 NADH + 2 H+
-
-
-
-
?
brilliant black + 2 NADH + 2 H+
?
Brilliant Black + NADH + H+
?
congo red + 2 NADH + 2 H+
? + 2 NAD+
-
-
-
?
Congo red + NADH + H+
? + NAD+
ethyl red + 2 NADH + 2 H+
anthranilate + N,N-diethyl-1,4-phenylenediamine + 2 NAD+
-
-
-
?
fast red E + 2 NADH + 2 H+
4-aminonaphthalene-1-sulfonic acid + 5-amino-6-hydroxynaphthalene-2-sulfonic acid + 2 NAD+
-
-
-
-
?
fast red E + 2 NADPH + 2 H+
4-aminonaphthalene-1-sulfonic acid + 5-amino-6-hydroxynaphthalene-2-sulfonic acid + 2 NADP+
-
-
-
-
?
menadione + 2 NADH + 2 H+
?
menadione + 2 NADH + 2 H+
? + 2 NAD+
-
-
-
?
methyl orange + 2 NADH + 2 H+
?
methyl orange + NADH + H+
?
methyl orange + NADH + H+
? + NAD+
methyl red + 2 NADH + 2 H+
?
Methyl Red + NADH + H+
2-aminobenzoic acid + N,N-dimethyl-1,4-phenylenediamine + NAD+
-
-
-
?
methyl red + NADH + H+
? + NAD+
orange G + 2 NADH + 2 H+
aniline + 8-amino-7-hydroxynaphthalene-1,3-disulfonic acid + 2 NAD+
-
-
-
-
?
orange G + 2 NADPH + 2 H+
aniline + 8-amino-7-hydroxynaphthalene-1,3-disulfonic acid + 2 NADP+
orange I + 2 NADH + 2 H+
4-aminobenzene-1-sulfonic acid + 4-aminonaphthalen-1-ol + 2 NAD+
Orange I + 2 NADH + 2 H+
?
orange II + 2 NADPH + 2 H+
4-aminobenzene-1-sulfonic acid + 1-aminonaphthalen-2-ol + 2 NADP+ + 2 NAD+
orange II + NADH + H+
? + NAD+
ponceau BS + 2 NADH + 2 H+
? + 2 NAD+
ponceau S + 2 NADH + 2 H+
? + 2 NAD+
-
-
-
?
Reactive black 5 + 2 NADH + 2 H+
n-hydroxy-benzenamine + dimethyl phthalate + phenylethyl alcohol + 4-methylphenol + 3-(methylthio)propanoic acid methyl ester + 2 NAD+
-
-
-
-
?
Reactive Orange + NADH + H+
?
-
substrate for immobilized enzyme (catalyst meso-cellular foam-A) only
-
-
?
sunset yellow + 2 NADH + 2 H+
?
-
-
-
-
?
tartrazine + 2 NADH + 2 H+
?
additional information
?
-
1,2-naphthoquinone + 2 NADH + 2 H+
?
-
-
-
?
1,2-naphthoquinone + 2 NADH + 2 H+
?
-
-
-
?
1,4-naphthoquinone + 2 NADH + 2 H+
?
-
-
-
?
1,4-naphthoquinone + 2 NADH + 2 H+
?
-
-
-
?
2-(4-dimethylaminophenyl)diazenylbenzoate + 2 NADH + 2 H+
anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD+
i.e. azo dye methyl red
-
-
?
2-(4-dimethylaminophenyl)diazenylbenzoate + 2 NADH + 2 H+
anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD+
i.e. azo dye methyl red, via a diazene intermediate
-
-
?
2-(4-dimethylaminophenylazo) benzoic acid + NADH + H+
N,N'-dimethyl-p-phenylenediamine + 2-aminobenzoic acid + NAD+
i.e. methyl red
-
-
?
2-(4-dimethylaminophenylazo) benzoic acid + NADH + H+
N,N'-dimethyl-p-phenylenediamine + 2-aminobenzoic acid + NAD+
i.e. methyl red
-
-
?
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADH + 2 H+
2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NAD+
i.e. methyl red
-
-
?
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADH + 2 H+
2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NAD+
-
i.e. methyl red
-
-
?
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADH + 2 H+
2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NAD+
i.e. methyl red
-
-
?
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADH + 2 H+
2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NAD+
-
i.e. methyl red
-
-
?
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADH + 2 H+
2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NAD+
i.e. methyl red
-
-
?
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADH + 2 H+
2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NAD+
i.e. methyl red
-
-
?
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADH + 2 H+
2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NAD+
i.e. methyl red
-
-
?
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADPH + 2 H+
2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NADP+
-
i.e. methyl red
-
-
?
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADPH + 2 H+
2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NADP+
i.e. methyl red
-
-
?
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADPH + 2 H+
2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NADP+
i.e. methyl red
-
-
?
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADPH + 2 H+
2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NADP+
-
i.e. methyl red
-
-
?
4-(dimethylamino)azobenzene + NADH + H+
N,N-dimethyl-1,4-phenylenediamine + aniline + NAD+
-
-
-
?
4-(dimethylamino)azobenzene + NADH + H+
N,N-dimethyl-1,4-phenylenediamine + aniline + NAD+
i.e. methyl yellow
-
-
?
4-(dimethylamino)azobenzene + NADH + H+
N,N-dimethyl-1,4-phenylenediamine + aniline + NAD+
-
-
-
?
4-(dimethylamino)azobenzene + NADH + H+
N,N-dimethyl-1,4-phenylenediamine + aniline + NAD+
i.e. methyl yellow
-
-
?
acid red 88 + 2 NADH + 2 H+
4-aminobenzene-1-sulfonic acid + 1-aminonaphthalen-2-ol + 2 NAD+
-
-
-
?
acid red 88 + 2 NADH + 2 H+
4-aminobenzene-1-sulfonic acid + 1-aminonaphthalen-2-ol + 2 NAD+
-
-
-
?
acid red 88 + NADH + H+
? + NAD+
-
-
-
r
acid red 88 + NADH + H+
? + NAD+
-
-
-
r
Allura Red + NADH + H+
?
-
substrate for immobilized enzyme (catalyst meso-cellular foam-A) only
-
-
?
Allura Red + NADH + H+
?
-
substrate for immobilized enzyme (catalyst meso-cellular foam-A) only
-
-
?
amaranth + 2 NADH + 2 H+
4-aminonaphthalene-1-sulfonic acid + 4-amino-3-hydroxynaphthalene-2,7-disulfonic acid + 2 NAD+
-
-
-
-
?
amaranth + 2 NADH + 2 H+
4-aminonaphthalene-1-sulfonic acid + 4-amino-3-hydroxynaphthalene-2,7-disulfonic acid + 2 NAD+
-
-
-
?
amaranth + 2 NADH + 2 H+
4-aminonaphthalene-1-sulfonic acid + 4-amino-3-hydroxynaphthalene-2,7-disulfonic acid + 2 NAD+
-
-
-
?
amaranth + 2 NADH + 2 H+
4-aminonaphthalene-1-sulfonic acid + 4-amino-3-hydroxynaphthalene-2,7-disulfonic acid + 2 NAD+
-
-
-
-
?
amaranth + 2 NADH + 2 H+
4-aminonaphthalene-1-sulfonic acid + 4-amino-3-hydroxynaphthalene-2,7-disulfonic acid + 2 NAD+
-
-
-
-
?
amaranth + 2 NADH + 2 H+
4-aminonaphthalene-1-sulfonic acid + 4-amino-3-hydroxynaphthalene-2,7-disulfonic acid + 2 NAD+
-
-
-
?
amaranth + 2 NADH + 2 H+
4-aminonaphthalene-1-sulfonic acid + 4-amino-3-hydroxynaphthalene-2,7-disulfonic acid + 2 NAD+
-
-
-
?
amaranth + 2 NADH + 2 H+
4-aminonaphthalene-1-sulfonic acid + 4-amino-3-hydroxynaphthalene-2,7-disulfonic acid + 2 NAD+
-
-
-
-
?
amaranth + 2 NADH + 2 H+
4-aminonaphthalene-1-sulfonic acid + 4-amino-3-hydroxynaphthalene-2,7-disulfonic acid + 2 NAD+
-
-
-
-
?
brilliant black + 2 NADH + 2 H+
?
-
-
-
-
?
brilliant black + 2 NADH + 2 H+
?
-
-
-
-
?
brilliant black + 2 NADH + 2 H+
?
-
-
-
-
?
Brilliant Black + NADH + H+
?
-
low activity
-
-
?
Brilliant Black + NADH + H+
?
-
low activity
-
-
?
Congo red + NADH + H+
? + NAD+
-
-
-
r
Congo red + NADH + H+
? + NAD+
-
-
-
r
menadione + 2 NADH + 2 H+
?
-
-
-
?
menadione + 2 NADH + 2 H+
?
-
-
-
?
methyl orange + 2 NADH + 2 H+
?
-
-
-
?
methyl orange + 2 NADH + 2 H+
?
-
-
-
?
methyl orange + NADH + H+
?
-
substrate for immobilized enzyme (catalyst meso-cellular foam-A) only
-
-
?
methyl orange + NADH + H+
?
-
substrate for immobilized enzyme (catalyst meso-cellular foam-A) only
-
-
?
methyl orange + NADH + H+
? + NAD+
-
-
-
r
methyl orange + NADH + H+
? + NAD+
-
-
-
r
methyl red + 2 NADH + 2 H+
?
-
-
-
?
methyl red + 2 NADH + 2 H+
?
-
-
-
?
methyl red + NADH + H+
?
-
substrate for immobilized enzyme (catalyst meso-cellular foam-A) only
-
-
?
methyl red + NADH + H+
?
-
substrate for immobilized enzyme (catalyst meso-cellular foam-A) only
-
-
?
methyl red + NADH + H+
? + NAD+
-
-
-
r
methyl red + NADH + H+
? + NAD+
-
-
-
r
orange G + 2 NADPH + 2 H+
aniline + 8-amino-7-hydroxynaphthalene-1,3-disulfonic acid + 2 NADP+
-
-
-
?
orange G + 2 NADPH + 2 H+
aniline + 8-amino-7-hydroxynaphthalene-1,3-disulfonic acid + 2 NADP+
-
-
-
?
orange G + 2 NADPH + 2 H+
aniline + 8-amino-7-hydroxynaphthalene-1,3-disulfonic acid + 2 NADP+
-
-
-
-
?
orange I + 2 NADH + 2 H+
4-aminobenzene-1-sulfonic acid + 4-aminonaphthalen-1-ol + 2 NAD+
-
-
-
?
orange I + 2 NADH + 2 H+
4-aminobenzene-1-sulfonic acid + 4-aminonaphthalen-1-ol + 2 NAD+
-
-
-
?
Orange I + 2 NADH + 2 H+
?
-
-
-
?
Orange I + 2 NADH + 2 H+
?
-
-
-
?
orange II + 2 NADPH + 2 H+
4-aminobenzene-1-sulfonic acid + 1-aminonaphthalen-2-ol + 2 NADP+ + 2 NAD+
-
-
-
?
orange II + 2 NADPH + 2 H+
4-aminobenzene-1-sulfonic acid + 1-aminonaphthalen-2-ol + 2 NADP+ + 2 NAD+
-
-
-
?
orange II + NADH + H+
? + NAD+
-
-
-
r
orange II + NADH + H+
? + NAD+
-
-
-
r
ponceau BS + 2 NADH + 2 H+
? + 2 NAD+
-
-
-
?
ponceau BS + 2 NADH + 2 H+
? + 2 NAD+
-
-
-
?
tartrazine + 2 NADH + 2 H+
?
-
-
-
-
?
tartrazine + 2 NADH + 2 H+
?
-
-
-
-
?
tartrazine + 2 NADH + 2 H+
?
-
-
-
-
?
additional information
?
-
the enzyme shows a negligible ability to use molecular oxygen as an electron acceptor
-
-
-
additional information
?
-
the enzyme shows a negligible ability to use molecular oxygen as an electron acceptor
-
-
-
additional information
?
-
active site structure analysis and substrate specificity, Azo compound binding structure, overview
-
-
?
additional information
?
-
AzoR utilizes NADH but not NADPH as an electron donor and binds FMN as a flavin cofactor
-
-
?
additional information
?
-
no activity with Ponceau SX. Recombinant AcpD reaction follows a ping-pong mechanism requiring 2 mol of NADH to reduce 1 mol of methyl red into 2-aminobenzoic acid and N,N'-dimethyl-p-phenylenediamine. On the other hand, the gene product cannot convert holo-acyl carrier protein into the apo form under either in vitro or in vivo conditions. These data indicate that the acpD gene product is not acyl carrier protein phosphodiesterase but an azoreductase
-
-
?
additional information
?
-
-
enzyme additionally acts as nitroreductase and selectively reduces the nitro group of 2-nitrophenol, 4-nitrobenzoic acid, 2-nitro-benzaldehyde and 3-nitrophenol
-
-
?
additional information
?
-
-
free enzyme has no activity with azobenzene, 4-phenylazophenol, Allura Red, Amido Black, Reactive Orange, Para Red, Chlorazol Black and Methyl Orange
-
-
-
additional information
?
-
-
free enzyme has no activity with azobenzene, 4-phenylazophenol, Allura Red, Amido Black, Reactive Orange, Para Red, Chlorazol Black and Methyl Orange
-
-
-
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0.061 - 0.062
1,2-naphthoquinone
0.064 - 0.097
1,4-Naphthoquinone
0.0179
2-(4-dimethylaminophenyl)diazenylbenzoate
recombinant enzyme, pH 7.4, 30°C
0.002 - 0.034
4'-(dimethylamino)-azobenzene-2-carboxylic acid
0.034
Amaranth
-
pH 7.4, 37°C
0.01155 - 0.09315
Methyl red
additional information
additional information
-
0.061
1,2-naphthoquinone
wild type enzyme, at pH 8.5 and 25°C
0.062
1,2-naphthoquinone
mutant enzyme W60A, at pH 8.5 and 25°C
0.064
1,4-Naphthoquinone
mutant enzyme W60A, at pH 8.5 and 25°C
0.097
1,4-Naphthoquinone
wild type enzyme, at pH 8.5 and 25°C
0.002
4'-(dimethylamino)-azobenzene-2-carboxylic acid
cofactor roseoflavin mononucleotide, pH 7.4, 30°C
0.011
4'-(dimethylamino)-azobenzene-2-carboxylic acid
-
pH 7.2, 25°C
0.011
4'-(dimethylamino)-azobenzene-2-carboxylic acid
mutant R21G/N121A, pH 7.1, temperature not specified in the publication
0.016
4'-(dimethylamino)-azobenzene-2-carboxylic acid
mutant R21G/N121Q, pH 7.1, temperature not specified in the publication
0.018
4'-(dimethylamino)-azobenzene-2-carboxylic acid
pH 7.4, 30°C
0.02
4'-(dimethylamino)-azobenzene-2-carboxylic acid
mutant R21K, pH 7.1, temperature not specified in the publication
0.024
4'-(dimethylamino)-azobenzene-2-carboxylic acid
pH 7.1, 23°C
0.024
4'-(dimethylamino)-azobenzene-2-carboxylic acid
wild-type, pH 7.1, temperature not specified in the publication
0.0247
4'-(dimethylamino)-azobenzene-2-carboxylic acid
mutant W105F, pH 7.1, 23°C
0.0251
4'-(dimethylamino)-azobenzene-2-carboxylic acid
mutant W105H, pH 7.1, 23°C
0.0254
4'-(dimethylamino)-azobenzene-2-carboxylic acid
wild-type, pH 7.1, 23°C
0.027
4'-(dimethylamino)-azobenzene-2-carboxylic acid
cofactor FMN, pH 7.4, 30°C
0.0276
4'-(dimethylamino)-azobenzene-2-carboxylic acid
mutant W105Y, pH 7.1, 23°C
0.0282
4'-(dimethylamino)-azobenzene-2-carboxylic acid
mutant W105Q, pH 7.1, 23°C
0.029
4'-(dimethylamino)-azobenzene-2-carboxylic acid
mutant N121Q, pH 7.1, temperature not specified in the publication
0.031
4'-(dimethylamino)-azobenzene-2-carboxylic acid
mutant R21K/N121A, pH 7.1, temperature not specified in the publication
0.034
4'-(dimethylamino)-azobenzene-2-carboxylic acid
mutant R21K/N121Q, pH 7.1, temperature not specified in the publication
0.025
menadione
mutant enzyme W60A, at pH 8.5 and 25°C
0.069
menadione
wild type enzyme, at pH 8.5 and 25°C
0.01155
Methyl red
wild type enzyme, at pH 7.4 and 30°C
0.01603
Methyl red
mutant enzyme F117A, at pH 7.4 and 30°C
0.01928
Methyl red
mutant enzyme Y119A, at pH 7.4 and 30°C
0.0296
Methyl red
mutant enzyme R59A, at pH 7.4 and 30°C
0.04809
Methyl red
mutant enzyme R139A, at pH 7.4 and 30°C
0.06872
Methyl red
mutant enzyme H143A, at pH 7.4 and 30°C
0.07676
Methyl red
mutant enzyme S16A, at pH 7.4 and 30°C
0.09315
Methyl red
mutant enzyme N96A, at pH 7.4 and 30°C
0.0107
NADH
recombinant enzyme, pH 6.0, 25°C
0.016
NADH
-
pH 7.4, 37°C
0.02714
NADH
mutant enzyme F117A, at pH 7.4 and 30°C
0.0316
NADH
recombinant enzyme, pH 7.4, 30°C
0.04338
NADH
mutant enzyme H143A, at pH 7.4 and 30°C
0.08
NADH
mutant R21G/N121A, pH 7.1, temperature not specified in the publication
0.082
NADH
-
pH 7.2, 25°C
0.115
NADH
mutant R21K/N121Q, pH 7.1, temperature not specified in the publication
0.122
NADH
mutant R21K, pH 7.1, temperature not specified in the publication
0.143
NADH
wild-type, pH 7.1, temperature not specified in the publication
0.158
NADH
wild-type, pH 7.1, 23°C
0.166
NADH
mutant W105Y, pH 7.1, 23°C
0.169
NADH
mutant W105Q, pH 7.1, 23°C
0.171
NADH
mutant W105H, pH 7.1, 23°C
0.175
NADH
mutant W105F, pH 7.1, 23°C
0.18777
NADH
wild type enzyme, at pH 7.4 and 30°C
0.19
NADH
mutant R21G/N121Q, pH 7.1, temperature not specified in the publication
0.2241
NADH
mutant enzyme R139A, at pH 7.4 and 30°C
0.26
NADH
cofactor FMN, pH 7.4, 30°C
0.267
NADH
mutant R21K/N121Q, pH 7.1, temperature not specified in the publication
0.269
NADH
cofactor roseoflavin mononucleotide, pH 7.4, 30°C
0.3158
NADH
mutant enzyme N96A, at pH 7.4 and 30°C
0.3433
NADH
mutant enzyme R59A, at pH 7.4 and 30°C
0.371
NADH
mutant N121Q, pH 7.1, temperature not specified in the publication
0.5307
NADH
mutant enzyme S16A, at pH 7.4 and 30°C
0.6551
NADH
mutant enzyme Y119A, at pH 7.4 and 30°C
0.115
Orange I
wild type enzyme, at pH 8.5 and 25°C
0.157
Orange I
mutant enzyme W60A, at pH 8.5 and 25°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
steady-state kinetic analysis
-
additional information
additional information
nonlinear Michaelis-Menten kinetics
-
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0.626
-
cofactor NADPH, pH 7.0, 25°C
11.4
substrate orange I, pH 7.4, 30°C
137
substrate amaranth, pH 7.1, 23°C
139
substrate orange II, pH 7.1, 23°C
141.25
purified recombinant enzyme, pH 4.0, 25°C
167
substrate ponceau S, pH 7.1, 23°C
18
-
substrate orange G, cofactor NADH, pH 7.4, 37°C
181
substrate 4'-(dimethylamino)-azobenzene-2-carboxylic acid, pH 7.1, 23°C
188.6
purified recombinant enzyme, pH 7.4, 30°C, methyl red with FMN
22
-
substrate amaranth, cofactor NADPH, pH 7.4, 37°C
24.1
substrate 1-(2-pyridylazo)-2-naphthol,pH 7.4, 30°C
25
-
substrate amaranth, cofactor FADH2, pH 7.4, 37°C
25.8
30°C, pH 7.4, substrate 4'-(dimethylamino)-azobenzene-2-carboxylic acid
26
-
substrate amaranth, cofactor FMNH2, pH 7.4, 37°C
26.6
substrate 4'-(dimethylamino)-azobenzene-2-carboxylic acid, pH 7.4, 30°C
362.6
purified recombinant enzyme, pH 7.4, 30°C, menadione with FMN
441
purified recombinant enzyme, pH 7.4, 30°C, ethyl red with FMN
63
-
substrate fast red E, cofactor NADH, pH 7.4, 37°C
7.3
substrate acid red 88, pH 7.4, 30°C
74
-
substrate amaranth, cofactor NADH, pH 7.4, 37°C
98.9
purified recombinant enzyme, pH 7.4, 30°C, methyl red with FAD
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in complex with FMN, sitting drop vapor diffusion method, using 0.17 M ammonium sulfate and 25.2% (w/v) PEG 4000
purified recombinant His-tagged wild-type enzyme in complex with FMN/N-cyclohexyl-2-aminoethanesulfonate (CHES) and Y151F enzyme mutant in complex with FMN, sitting drop vapor diffusion method, mixing of 0.002 ml of 42 mg/ml protein solution with an equal volume of reservoir solution containing 40% PEG 600 and 100 mM CHES, pH 9.5 for the wild-type, and 36% PEG 600 and 100 mM phosphate-citrate buffer, pH 4.2 for the mutant, equilibration against 0.1 m reservoir resolution, 20°C, X-ray diffraction structure determination and analysis at 1.97 and 1.95 A resolution respectively, molecular replacement method. Diffraction-quality crystals for the Y127F mutant cannot be obtained
docking simulations. The isoalloxazine ring of FAD localizes at the same site and plays the same role as that of FMN in AzrA
in complex with FMN, to 2.07 A resolution. The AzoA monomer shows a typical NAD(P)-binding Rossmann fold with a highly conserved FMN binding pocket. A salt bridge between Arg18 and Asp184 restricts the size of the flavin binding pocket such that only FMN can bind
purified oxidized or reduced AzoR, free or in complex with inhibitor dicoumarol, hanging drop vapor diffusion method, mixing of equal volumes of 8 mg/ml protein in 10 mM Tris-HCl, pH 8.0, 100 mM NAD+ and 0.1 mM FMN with reservoir solution containing 200 mM NaOAc, 200 mM sodium cacodylate, pH 6.7, 15% w/v PEG 8000, and 3% v/v dimethyl sulfoxide, equilibration over reservoir solution, at 25 °C, 2 weeks, X-ray diffraction structure determination and analysis at 1.4-2.3 A resolution, molecular replacement using the 1.8 Å resolution structure of oxidized AzoR as a search model, modelling
purified recombinant enzyme, sitting drop vapour-diffusion method, mixing 0.015 ml of 23 mg/ml protein in 10 mM Tris-HCl, pH 8.0, and 1 mM FMN, with an equal volume of reservoir solution containing 200 mM MgCl2, 30% v/v 2-propanol, and 100 mM HEPES, pH 7.5, equilibration over 0.5 ml reservoir solution, one week, 15°C, method optimization, crystal soaking in heavy metal solution with K2PtCl4, X-ray diffraction structure determination and analysis at 1.8-2.5 A resolution. FMN is tightly bound to the protein moiety, and this interaction is essential for the crystallization of AzoR
to 1.6 A resolution, space group F222, with unit-cell parameters a = 72.1, b = 95.5, c = 146.1 A
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Y127F
site-directed mutagenesis, Diffraction-quality crystals for the Y127F mutant cannot be obtained
Y151F
site-directed mutagenesis, structure comparison with the wild-type enzyme
Y127F
-
site-directed mutagenesis, Diffraction-quality crystals for the Y127F mutant cannot be obtained
-
Y151F
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
-
N121Q
115% of wild-type activity
R21G/N121A
136% of wild-type activity
R21G/N121Q
171% of wild-type activity
R21K
80% of wild-type activity
R21K/N121A
41% of wild-type activity
R21K/N121Q
40% of wild-type activity
W105A
complete loss of both affinity for FMN and enzyme activity
W105F
31fold decrease in vmax value, Km value similar to wild-type
W105G
complete loss of both affinity for FMN and enzyme activity
W105H
8fold decrease in vmax value, Km value similar to wild-type
W105Q
68fold decrease in vmax value, Km value similar to wild-type
W105Y
22% reduction in vmax value
N121Q
-
115% of wild-type activity
-
R21G/N121A
-
136% of wild-type activity
-
R21G/N121Q
-
171% of wild-type activity
-
R21K
-
80% of wild-type activity
-
R21K/N121A
-
41% of wild-type activity
-
W105A
-
complete loss of both affinity for FMN and enzyme activity
-
W105F
-
31fold decrease in vmax value, Km value similar to wild-type
-
W105H
-
8fold decrease in vmax value, Km value similar to wild-type
-
W105Q
-
68fold decrease in vmax value, Km value similar to wild-type
-
W105Y
-
22% reduction in vmax value
-
F162A
site-directed mutagenesis
R59A
site-directed mutagenesis, the mutation enhances the Vmax value for p-methyl red 27fold with a 3.8fold increase of the Km value, residue Arg59 decides the substrate specificity of AzoR
R59G
-
mutation influences the formation of dilution-induced intermediates. Mutant R59G contains only two types of FMN, emitting at 530 nm and 600 nm
Y120A
site-directed mutagenesis
F117A
the mutant shows 208% activity with Methyl Red and 176% activity with NADH compared to the wild type enzyme
H143A
the mutant shows 19% activity with Methyl Red and 76% activity with NADH compared to the wild type enzyme
N96A
the mutant shows 9% activity with Methyl Red and 37% activity with NADH compared to the wild type enzyme
R139A
the mutant shows 63% activity with Methyl Red and 78% activity with NADH compared to the wild type enzyme
R59A
the mutant shows 70% activity with Methyl Red and 83% activity with NADH compared to the wild type enzyme
S16A
the mutant shows 29% activity with Methyl Red and 49% activity with NADH compared to the wild type enzyme
Y119A
the mutant shows 59% activity with Methyl Red and 44% activity with NADH compared to the wild type enzyme
additional information
deletion of the azoR gene in Escherichia coli strain MG1655 has no strong influence on the 7NCCA reduction of the cells even though the pure enzyme displays a clear nitroreductase activity with this compound
W60D
the mutant retains more than 10% of wild type activity
W60D
-
the mutant retains more than 10% of wild type activity
-
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Ito, K.; Nakanishi, M.; Lee, W.-C.; Sasaki, H.; Zenno,S.; Saigo, K.; Kitade, Y.; Tanokura, M.
Crystallization and preliminary X-ray analysis of AzoR (azoreductase) from Escherichia coli
Acta Crystallogr. Sect. F
61
399-402
2005
Escherichia coli (P41407)
-
brenda
Nakanishi, M.; Yatome, C.; Ishida, N.; Kitade, Y.
Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase
J. Biol. Chem.
276
46394-46399
2001
Escherichia coli (P41407)
-
brenda
Ito, K.; Nakanishi, M.; Lee, W.-C.; Zhi, Y.; Sasaki, H.; Zenno, S.; Saigo, K.; Kitade, Y.; Tanokura, M.
Expansion of substrate specificity and catalytic mechanism of azoreductase by X-ray crystallography and site-directed mutagenesis
J. Biol. Chem.
283
13889-13896
2008
Escherichia coli (P41407)
-
brenda
Qi, J.; Schloemann, M.; Tischler, D.
Biochemical characterization of an azoreductase from Rhodococcus opacus 1CP possessing methyl red degradation ability
J. Mol. Catal. B
130
9-17
2016
Rhodococcus opacus (A0A1B1KJ01), Rhodococcus opacus 1CP (A0A1B1KJ01)
-
brenda
Mercier, C.; Chalansonnet, V.; Orenga, S.; Gilbert, C.
Characteristics of major Escherichia coli reductases involved in aerobic nitro and azo reduction
J.Appl. Microbiol.
115
1012-1022
2013
Escherichia coli (P41407)
-
brenda
Correia, B.; Chen, Z.; Mendes, S.; Martins, L.; Bento, I.
Crystallization and preliminary X-ray diffraction analysis of the azoreductase PpAzoR from Pseudomonas putida MET94
Acta Crystallogr. Sect. F
67
121-123
2011
Pseudomonas putida (Q88IY3), Pseudomonas putida DSM 6125 (Q88IY3)
brenda
Ooi, T.; Shibata, T.; Sato, R.; Ohno, H.; Kinoshita, S.; Thuoc, T.; Taguchi, S.
An azoreductase, aerobic NADH-dependent flavoprotein discovered from Bacillus sp. Functional expression and enzymatic characterization
Appl. Microbiol. Biotechnol.
75
377-386
2007
Bacillus sp. B29 (Q0WXX2)
brenda
Matsumoto, K.; Mukai, Y.; Ogata, D.; Shozui, F.; Nduko, J.M.; Taguchi, S.; Ooi, T.
Characterization of thermostable FMN-dependent NADH azoreductase from the moderate thermophile Geobacillus stearothermophilus
Appl. Microbiol. Biotechnol.
86
1431-1438
2010
Geobacillus stearothermophilus (Q9X4K2)
brenda
Liu, Z.; Chen, H.; Shaw, N.; Hopper, S.; Chen, L.; Chen, S.; Cerniglia, C.; Wang, B.
Crystal structure of an aerobic FMN-dependent azoreductase (AzoA) from Enterococcus faecalis
Arch. Biochem. Biophys.
463
68-77
2007
Enterococcus faecalis (Q831B2)
brenda
Sun, J.; Kweon, O.; Jin, J.; He, G.; Li, X.; Cerniglia, C.; Chen, H.
Mutation network-based understanding of pleiotropic and epistatic mutational behavior of Enterococcus faecalis FMN-dependent azoreductase
Biochem. Biophys. Rep.
12
240-244
2017
Enterococcus faecalis (Q831B2), Enterococcus faecalis ATCC 700802 (Q831B2)
brenda
Langer, S.; Nakanishi, S.; Mathes, T.; Knaus, T.; Binter, A.; Macheroux, P.; Mase, T.; Miyakawa, T.; Tanokura, M.; Mack, M.
The flavoenzyme azobenzene reductase AzoR from Escherichia coli binds roseoflavin mononucleotide (RoFMN) with high affinity and is less active in its RoFMN form
Biochemistry
52
4288-4295
2013
Escherichia coli (P41407)
brenda
Misal, S.A.; Lingojwar, D.P.; Lokhande, M.N.; Lokhande, P.D.; Gawai, K.R.
Enzymatic transformation of nitro-aromatic compounds by a flavin-free NADH azoreductase from Lysinibacillus sphaericus
Biotechnol. Lett.
36
127-131
2014
Lysinibacillus sphaericus
brenda
Feng, J.; Han, T.; Zhang, M.; Zhou, Y.; Wu, Q.
Application of 2D fluorescence correlation method to investigate the dilution-induced heterogeneous distribution of the bound FMN in azoreductase
Chin. Chem. Lett.
26
210-214
2015
Escherichia coli
-
brenda
Punj, S.; John, G.
Purification and identification of an FMN-dependent NAD(P)H azoreductase from Enterococcus faecalis
Curr. Issues Mol. Biol.
11
59-66
2009
Enterococcus faecalis, Enterococcus faecalis ATCC 27274
brenda
Ooi, T.; Ogata, D.; Matsumoto, K.; Nakamura, G.; Yu, J.; Yao, M.; Kitamura, M.; Taguchi, S.
Flavin-binding of azoreductase Direct evidences for dual-binding property of apo-azoreductase with FMN and FAD
J. Mol. Catal. B
74
204-208
2012
Bacillus sp. (in: Bacteria) (Q0WXX2), Bacillus sp. (in: Bacteria) B29 (Q0WXX2)
-
brenda
Chen, H.; Xu, H.; Kweon, O.; Chen, S.; Cerniglia, C.
Functional role of Trp-105 of Enterococcus faecalis azoreductase (AzoA) as resolved by structural and mutational analysis
Microbiology
154
2659-2667
2008
Enterococcus faecalis (Q831B2), Enterococcus faecalis ATCC 700802 (Q831B2)
brenda
Chen, H.; Wang, R.; Cerniglia, C.
Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis
Protein Expr. Purif.
34
302-310
2004
Enterococcus faecalis (Q831B2), Enterococcus faecalis ATCC 19433 (Q831B2)
brenda
Romero, E.; Savino, S.; Fraaije, M.W.; Loncar, N.
Mechanistic and crystallographic studies of azoreductase AzoA from Bacillus wakoensis A01
ACS Chem. Biol.
15
504-512
2020
Alkalihalobacillus wakoensis (A0A455X8R2), Alkalihalobacillus wakoensis A01 (A0A455X8R2)
brenda
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
e01688-20
2020
Bacillus smithii (A0A0H4NXC5), Bacillus smithii DSM 4216 (A0A0H4NXC5)
brenda
Verma, K.; Kundu, D.; Kundu, L.M.; Singh, A.K.; Dubey, V.K.
Folding and stability of recombinant azoreductase enzyme from Chromobacterium violaceum
Enzyme Microb. Technol.
131
109433
2019
Chromobacterium violaceum (Q7NWH3), Chromobacterium violaceum ATCC 12472 (Q7NWH3)
brenda
Qi, J.; Anke, M.; Szymanska, K.; Tischler, D.
Immobilization of Rhodococcus opacus 1CP azoreductase to obtain azo dye degrading biocatalysts operative at acidic pH
Int. Biodeter. Biodegrad.
118
89-94
2017
Rhodococcus opacus, Rhodococcus opacus 1CP
-
brenda
Cao, X.; Di, M.; Wang, J.
Expansion of the active site of the azoreductase from Shewanella oneidensis MR-1
J. Mol. Graph. Model.
78
213-220
2017
Shewanella oneidensis (Q8E990)
brenda
Zahran, S.; Ali-Tammam, M.; Hashem, A.; Aziz, R.; Ali, A.
Azoreductase activity of dye-decolorizing bacteria isolated from the human gut microbiota
Sci. Rep.
9
5508
2019
Bacillus cereus, Escherichia coli, Enterococcus faecalis, Enterococcus avium
brenda
Fazeliyan, E.; Sadeghi, M.; Forouzandeh, S.; Doosti, A.; Mohammadi Moghadam, F.; Sedehi, M.; Emadi, Z.; Sadeghi, R.
Decolorization mechanism, identification of an FMN-dependent NADH-azoreductase from a moderately halotolerant Staphylococcus sp. MEH038S, and toxicity assessment of biotransformed metabolites
Water Environ. Res.
93
2072-2083
2021
Staphylococcus sp. MEH038S
brenda