1.7.1.6: azobenzene reductase

This is an abbreviated version!
For detailed information about azobenzene reductase, go to the full flat file.

Word Map on EC 1.7.1.6

Reaction

N,N-dimethyl-1,4-phenylenediamine
+
aniline
+ 2 NADP+ =
4-(dimethylamino)azobenzene
+ 2 NADPH + 2 H+

Synonyms

acpD, aerobic azoreductase, Azo 1, azo dye reductase, azo reductase, azo-dye reductase, AzoA, AzoB, AzoC, AzoEF1, AzoI, AzoII, AzoR, AzoR1, azoreductase, azoreductase 1, azoreductase B, azoreductase C, AZR, AzrA, AzrB, AzrC, AzrG, AzrS, bsAzoR, BTI1, class 1 azoreductase, class 2 azoreductase, dibromopropylaminophenylazobenzoic azoreductase, dimethylaminobenzene reductase, EC 1.6.6.7, ecAzoR, EF0404, efAzoR, EF_0404, flavin mononucleotide-containing azoreductase, flavin-dependent azoreductase, FMN-dependent NAD(P)H azoreductase, FMN-dependent NAD(P)H nitroreductase, FMN-dependent NADH-azo compound oxidoreductase, FMN-dependent NADH-azoreductase, methyl red azoreductase, N,N-dimethyl-4-phenylazoaniline azoreductase, NAD(P)H:1-(4'-sulfophenylazo)-2-naphthol oxidoreductase, NADH driven FMN dependent azoreductase, NADH-azoreductase, NADPH-dependent azoreductase Azr, NADPH-flavin azoreductase, NADPH2-dependent azoreductase, NC-reductase, new Coccine (NC)-reductase, nicotinamide adenine dinucleotide (phosphate) azoreductase, Orange I azoreductase, Orange II azoreductase, oxygen insensitive intracellular azoreductase, p-aminoazobenzene reductase, p-dimethylaminoazobenzene azoreductase, paAzoR1, PAMD_1, PpAzoR, reductase, azobenzene, rsAzoR, SO 4396

ECTree

     1 Oxidoreductases
         1.7 Acting on other nitrogenous compounds as donors
             1.7.1 With NAD+ or NADP+ as acceptor
                1.7.1.6 azobenzene reductase

Engineering

Engineering on EC 1.7.1.6 - azobenzene reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A123F
-
36% of wild-type activity
D184G
-
complete loss of activity
E16G
-
46% of wild-type activity
F127G
-
complete loss of activity
L59G
-
10% of wild-type activity
N106A
-
3% of wild-type activity
N121A
-
170% of wild-type activity
R18G
-
9% of wild-type activity
R21G
-
382% of wild-type activity
R66A
-
47% of wild-type activity
V122Y
-
14% of wild-type activity
W105A
-
mutant, complete loss of both affinity for FMN and enzyme activity
W105F
-
mutant, lower Vmax value, decrease 30.6fold
W105G
-
mutant, complete loss of both affinity for FMN and enzyme activity
W105H
-
mutant, lower Vmax value, decrease 8.2fold
W105Q
-
mutant, lower Vmax value, decrease 68.2fold
W105Y
-
mutant, substitution does not significantly decrease the Vmax of the enzyme, 22% reduction
W62A
-
35% of wild-type activity
Y129G
-
complete loss of activity
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
R59G
-
site-directed mutagenesis, the interaction of FMN with substrates methyl red and methyl orange changes from van der Waals interaction in the wild-type to hydrogen bonding in the mutant, the association constants decrease
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
Q192R
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 60 min) relative to parental mutant variant B1G6
Q192R/A46P/V159A
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 90 min) relative to parental mutant variant 16B7
Q192R/A46P/V159A/A48P
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 60°C, 45 min) relative to parental mutant variant 2A1
Q192R/A46P/V159A/C129S
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 60°C, 45 min) relative to parental mutant variant 23C10
Q192R/A46P/V159A/C129S/A178D/A31S/K74E/A88G/L143Q
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 2F11
Q192R/A46P/V159A/C129S/A178D/A77T/F98L/N131D
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 3B9
Q192R/A46P/V159A/C129S/A178D/A88G/N131D/L143Q
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 1B6
Q192R/A46P/V159A/C129S/A178D/K74E/L143Q
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 2E4
Q192R/A46P/V159A/C129S/A178D/N131D/L143Q
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 6F11
Q192R/A46P/V159A/C129S/A77T/N131D
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 14D4
Q192R/A46P/V159A/C129S/D7H/A178D
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 13G10
Q192R/A46P/V159A/C129S/E36D/L143Q
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 1C11
Q192R/A46P/V159A/C129S/I6V/T79R/Y179H
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 32F5
Q192R/A46P/V159A/C129S/K74E/A88G
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 23C5
Q192R/A46P/V159A/C129S/L161M/L169P
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 27E4
Q192R/A46P/V159A/C129S/N14D/L143Q
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 6F10
Q192R/A46P/V159A/C129S/Y179H
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 23E4
Q192R/A46P/V159A/Y179H
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 60°C, 45 min) relative to parental mutant variant 19E4
Q192R/Y179H
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 90 min) relative to parental mutant variant 12B8
Y179H
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 60 min) relative to parental mutant variant K7E3
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
additional information