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1.7.1.17: FMN-dependent NADH-azoreductase

This is an abbreviated version!
For detailed information about FMN-dependent NADH-azoreductase, go to the full flat file.

Reaction

anthranilate
+
N,N-dimethyl-1,4-phenylenediamine
 + 2 NAD+ =
2-(4-dimethylaminophenyl)diazenylbenzoate
 + 2 NADH + 2 H+

Synonyms

acpD, AZO, azo-dye reductase, AzoA, AzoR, AzoR1, azoreductase, AzoRo, AzrA, AzrG, flavin-containing oxygen-insensitive azoreductase, FMN dependent azoreductase, FMN-dependent methyl red reductase, FMN-dependent NADH-azo compound oxidoreductase, FMN-dependent NADH-azo reductase, FMN-dependent NADH-azoreductase, FMN-dependent-NADH azoreductase, indigo reductase, NADH-azoreductase

ECTree

     1 Oxidoreductases
         1.7 Acting on other nitrogenous compounds as donors
             1.7.1 With NAD+ or NADP+ as acceptor
                1.7.1.17 FMN-dependent NADH-azoreductase

Engineering

Engineering on EC 1.7.1.17 - FMN-dependent NADH-azoreductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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