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Literature summary for 1.7.1.17 extracted from

  • Qi, J.; Schloemann, M.; Tischler, D.
    Biochemical characterization of an azoreductase from Rhodococcus opacus 1CP possessing methyl red degradation ability (2016), J. Mol. Catal. B, 130, 9-17 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
gene azoR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) Rhodococcus opacus

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ 10% inhibition at 0.05 mM Rhodococcus opacus
Fe2+ 13% inhibition at 0.05 mM Rhodococcus opacus
Fe3+ 14% inhibition at 0.05 mM Rhodococcus opacus
Mg2+ 8% inhibition at 0.05 mM Rhodococcus opacus
additional information the enzyme is oxygen-insensitive Rhodococcus opacus
Zn2+ 16% inhibition at 0.05 mM Rhodococcus opacus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information nonlinear Michaelis-Menten kinetics Rhodococcus opacus
0.0107
-
NADH recombinant enzyme, pH 6.0, 25°C Rhodococcus opacus

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ 43% activation at 0.05 mM Rhodococcus opacus
Mn2+ 119% activation at 0.05 mM Rhodococcus opacus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-(dimethylamino)azobenzene + NADH + H+ Rhodococcus opacus
-
N,N-dimethyl-1,4-phenylenediamine + aniline + NAD+
-
?
4-(dimethylamino)azobenzene + NADH + H+ Rhodococcus opacus 1CP
-
N,N-dimethyl-1,4-phenylenediamine + aniline + NAD+
-
?

Organism

Organism UniProt Comment Textmining
Rhodococcus opacus A0A1B1KJ01
-
-
Rhodococcus opacus 1CP A0A1B1KJ01
-
-

Oxidation Stability

Oxidation Stability Organism
the enzyme is oxygen-insensitive Rhodococcus opacus

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Rhodococcus opacus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
141.25
-
purified recombinant enzyme, pH 4.0, 25°C Rhodococcus opacus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-(4-dimethylaminophenylazo) benzoic acid + NADH + H+ i.e. methyl red Rhodococcus opacus N,N'-dimethyl-p-phenylenediamine + 2-aminobenzoic acid + NAD+
-
?
2-(4-dimethylaminophenylazo) benzoic acid + NADH + H+ i.e. methyl red Rhodococcus opacus 1CP N,N'-dimethyl-p-phenylenediamine + 2-aminobenzoic acid + NAD+
-
?
4-(dimethylamino)azobenzene + NADH + H+
-
Rhodococcus opacus N,N-dimethyl-1,4-phenylenediamine + aniline + NAD+
-
?
4-(dimethylamino)azobenzene + NADH + H+ i.e. methyl yellow Rhodococcus opacus N,N-dimethyl-1,4-phenylenediamine + aniline + NAD+
-
?
4-(dimethylamino)azobenzene + NADH + H+
-
Rhodococcus opacus 1CP N,N-dimethyl-1,4-phenylenediamine + aniline + NAD+
-
?
4-(dimethylamino)azobenzene + NADH + H+ i.e. methyl yellow Rhodococcus opacus 1CP N,N-dimethyl-1,4-phenylenediamine + aniline + NAD+
-
?

Subunits

Subunits Comment Organism
? x * 25000, recombinant His-tagged enzyme, SDS-PAGE, x * 25350, about, His-tagged enzyme, sequence calculation Rhodococcus opacus
More enzyme structure modeling, overview Rhodococcus opacus

Synonyms

Synonyms Comment Organism
azo-dye reductase UniProt Rhodococcus opacus
AzoR
-
Rhodococcus opacus
AzoRo
-
Rhodococcus opacus
flavin-containing oxygen-insensitive azoreductase
-
Rhodococcus opacus
FMN-dependent NADH-azoreductase UniProt Rhodococcus opacus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
53
-
-
Rhodococcus opacus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
10 50 the enzyme activity drops largely after 50°C, and there is no activity left when temperature rises to 70°C Rhodococcus opacus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
10 40 purified recombinant enzyme, pH 7.0, 0.1 M sodium phosphate buffer, 30 min, stable at Rhodococcus opacus
55
-
purified recombinant enzyme, unfolding temperature Rhodococcus opacus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
-
Rhodococcus opacus

Cofactor

Cofactor Comment Organism Structure
FMN a flavin-containing enzyme the enzyme binds 1 FMN per subunit Rhodococcus opacus
additional information no activity with NADPH Rhodococcus opacus
NADH dependent on Rhodococcus opacus

General Information

General Information Comment Organism
evolution the enzyme belongs to the azoreductase type 1 family Rhodococcus opacus
additional information enzyme structure modeling, overview Rhodococcus opacus
physiological function the enzyme catalyses the initial degradation step of azo dyes, characterized by one or more R1-N=N-R2 bonds Rhodococcus opacus