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

Crystallization

Crystallization on EC 1.7.1.6 - azobenzene reductase

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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
structure of Orange I bound to AzrC, PDBs ID 3W79
-
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
-
structure of balsalazide bound to paAzoR1, PDBs ID 3LT5
-
structure of reactive black 5 bound to ppAzoR, PDBs ID 4C14
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